메뉴 건너뛰기




Volumn 57, Issue 2-3, 2004, Pages 153-171

Dairy enzymology

Author keywords

Dairy microorganisms; Enzymes; Milk

Indexed keywords

PHOSPHATASE; PLASMIN; TRIACYLGLYCEROL LIPASE;

EID: 2442680162     PISSN: 1364727X     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1471-0307.2004.00144.x     Document Type: Conference Paper
Times cited : (43)

References (155)
  • 1
    • 0033773891 scopus 로고    scopus 로고
    • Formation of lipolytic enzymes by Brevibacterium linens
    • Adamitsch B F and Hampel W A (2000) Formation of lipolytic enzymes by Brevibacterium linens. Biotechnology Letters 22 1643-1646.
    • (2000) Biotechnology Letters , vol.22 , pp. 1643-1646
    • Adamitsch, B.F.1    Hampel, W.A.2
  • 2
    • 0034986675 scopus 로고    scopus 로고
    • Replacements of amino acid residues at subsites and their effects on the catalytic properties of Rhizomucor pusillus pepsin, an aspartic proteinase from Rhizomucor pusillus
    • Aikawa J, Park Y N, Sugiyama M, Nishiyama M, Horinouchi S and Beppu T (2001) Replacements of amino acid residues at subsites and their effects on the catalytic properties of Rhizomucor pusillus pepsin, an aspartic proteinase from Rhizomucor pusillus. Journal of Biochemistry 129 791-794.
    • (2001) Journal of Biochemistry , vol.129 , pp. 791-794
    • Aikawa, J.1    Park, Y.N.2    Sugiyama, M.3    Nishiyama, M.4    Horinouchi, S.5    Beppu, T.6
  • 3
    • 0032439914 scopus 로고    scopus 로고
    • Purification and characterization of an acid phosphatase from cell membrane fraction of Lactococcus lactis ssp. lactis 303
    • Akuzawa R and Fox P F (1998) Purification and characterization of an acid phosphatase from cell membrane fraction of Lactococcus lactis ssp. lactis 303. Food Science International 31 157-165.
    • (1998) Food Science International , vol.31 , pp. 157-165
    • Akuzawa, R.1    Fox, P.F.2
  • 4
    • 0028889680 scopus 로고
    • Purification and characterization of cystathionine β-lyase from Lactococcus lactis subsp. cremoris B78 and its possible role in flavor development in cheese
    • Alting A C, Engels W J M P, van Schalkwijk S and Exterkate F A (1995) Purification and characterization of cystathionine β-lyase from Lactococcus lactis subsp. cremoris B78 and its possible role in flavor development in cheese. Applied and Environmental Microbiology 61 4037-4042.
    • (1995) Applied and Environmental Microbiology , vol.61 , pp. 4037-4042
    • Alting, A.C.1    Engels, W.J.M.P.2    Van Schalkwijk, S.3    Exterkate, F.A.4
  • 5
    • 0025953726 scopus 로고
    • Characterization of a peptidase from Lactococcus lactis ssp. cremoris HP that hydrolyses di- and tripeptides containing proline or hydrophobic residues as the aminoterminal amino acid
    • Baankreis R and Exterkate F A (1991) Characterization of a peptidase from Lactococcus lactis ssp. cremoris HP that hydrolyses di- and tripeptides containing proline or hydrophobic residues as the aminoterminal amino acid. Systematic Applied Microbiology 14 317-323.
    • (1991) Systematic Applied Microbiology , vol.14 , pp. 317-323
    • Baankreis, R.1    Exterkate, F.A.2
  • 8
    • 0031415010 scopus 로고    scopus 로고
    • Purification and immunochemical quantitation of Penicillium roqueforti acid aspartyl proteinase
    • Bracq E, Levieux A and Levieux D (1997) Purification and immunochemical quantitation of Penicillium roqueforti acid aspartyl proteinase. Journal of Dairy Research 64 105-113.
    • (1997) Journal of Dairy Research , vol.64 , pp. 105-113
    • Bracq, E.1    Levieux, A.2    Levieux, D.3
  • 10
    • 0030938985 scopus 로고    scopus 로고
    • Purification and characterisation of cystathionine γ-lyase from Lactococcus lactis subsp. cremoris SK11: Possible role in flavour compound formation during cheese maturation
    • Bruinenberg P G, de Roo G and Limsowtin G K Y (1997) Purification and characterisation of cystathionine γ-lyase from Lactococcus lactis subsp. cremoris SK11: possible role in flavour compound formation during cheese maturation. Applied and Environmental Microbiology 63 561-566.
    • (1997) Applied and Environmental Microbiology , vol.63 , pp. 561-566
    • Bruinenberg, P.G.1    De Roo, G.2    Limsowtin, G.K.Y.3
  • 11
    • 0034914557 scopus 로고    scopus 로고
    • Lipolysis in cheese made from raw, pasteurized or high-pressure-treated goats' milk
    • Buffa M, Guamis B, Pavia M and Trujillo A J (2001) Lipolysis in cheese made from raw, pasteurized or high-pressure-treated goats' milk. International Dairy Journal 11 175-179.
    • (2001) International Dairy Journal , vol.11 , pp. 175-179
    • Buffa, M.1    Guamis, B.2    Pavia, M.3    Trujillo, A.J.4
  • 12
    • 0034633936 scopus 로고    scopus 로고
    • Functional implications of disulfide bond, Cys206-Cys210, in recombinant prochymosin (chymosin)
    • Chen H J, Zhang G B, Zhang Y Y, Dong Y C and Yang K Y (2000) Functional implications of disulfide bond, Cys206-Cys210, in recombinant prochymosin (chymosin). Biochemistry 39 12140-12148.
    • (2000) Biochemistry , vol.39 , pp. 12140-12148
    • Chen, H.J.1    Zhang, G.B.2    Zhang, Y.Y.3    Dong, Y.C.4    Yang, K.Y.5
  • 13
    • 0041807789 scopus 로고    scopus 로고
    • A review of nutritional and physiological factors affecting goat milk lipid synthesis and lipolysis
    • Chilliard Y, Ferlay A, Rouel J and Lamberett G (2003) A review of nutritional and physiological factors affecting goat milk lipid synthesis and lipolysis. Journal of Dairy Science 86 175-1770.
    • (2003) Journal of Dairy Science , vol.86 , pp. 175-1770
    • Chilliard, Y.1    Ferlay, A.2    Rouel, J.3    Lamberett, G.4
  • 14
  • 17
    • 0037324461 scopus 로고    scopus 로고
    • Evidence of a relationship between autolysis of starter bacteria and lipolysis in Cheddar cheese during ripening
    • Collins Y F, McSweeney P L H and Wilkinson M G (2003) Evidence of a relationship between autolysis of starter bacteria and lipolysis in Cheddar cheese during ripening. Journal of Dairy Research 70 105-113.
    • (2003) Journal of Dairy Research , vol.70 , pp. 105-113
    • Collins, Y.F.1    McSweeney, P.L.H.2    Wilkinson, M.G.3
  • 21
    • 0036383322 scopus 로고    scopus 로고
    • The effect of lysosomal proteinases and plasmin on the rennet coagulation properties of skim milk
    • Considine T, McSweeney P L H and Kelly A L (2002b) The effect of lysosomal proteinases and plasmin on the rennet coagulation properties of skim milk. Milchwissenschaft 57 425-428.
    • (2002) Milchwissenschaft , vol.57 , pp. 425-428
    • Considine, T.1    McSweeney, P.L.H.2    Kelly, A.L.3
  • 24
    • 0036580877 scopus 로고    scopus 로고
    • Lactobacillus reuteri DMS 20016. Purification and characterization of a cystathionine γ-lyase and use as adjunct starter in cheesemaking
    • De Angelis M, Curtin A C, McSweeney P L H, Faccia M and Gobbetti M (2002) Lactobacillus reuteri DMS 20016. purification and characterization of a cystathionine γ-lyase and use as adjunct starter in cheesemaking. Journal of Dairy Research 69 255-267.
    • (2002) Journal of Dairy Research , vol.69 , pp. 255-267
    • De Angelis, M.1    Curtin, A.C.2    McSweeney, P.L.H.3    Faccia, M.4    Gobbetti, M.5
  • 26
    • 0034469733 scopus 로고    scopus 로고
    • Hydrolysis of sequenced β-casein peptides provides new insight into peptidase activity from thermophilic lactic acid bacteria and highlights intrinsic resistance of phosphapeptides
    • Deutsch S M, Molle D, Gagnaire V, Piot M, Atlan D and Lortal S (2000) Hydrolysis of sequenced β-casein peptides provides new insight into peptidase activity from thermophilic lactic acid bacteria and highlights intrinsic resistance of phosphapeptides. Applied and Environmental Microbiology 66 5360-5367.
    • (2000) Applied and Environmental Microbiology , vol.66 , pp. 5360-5367
    • Deutsch, S.M.1    Molle, D.2    Gagnaire, V.3    Piot, M.4    Atlan, D.5    Lortal, S.6
  • 27
    • 0031687912 scopus 로고    scopus 로고
    • Conversion of methionine to thiols by lactococci, lactobacilli and brevibacteria
    • Dias B and Weimer B (1998a) Conversion of methionine to thiols by lactococci, lactobacilli and brevibacteria. Applied and Environmental Microbiology 64 3320-3326.
    • (1998) Applied and Environmental Microbiology , vol.64 , pp. 3320-3326
    • Dias, B.1    Weimer, B.2
  • 28
    • 0031662724 scopus 로고    scopus 로고
    • Purification and characterization of L-methionine T γ-lyase from Brevibacterium linens
    • Dias B and Weimer B (1998b) Purification and characterization of L-methionine T γ-lyase from Brevibacterium linens. Applied and Environmental Microbiology 64 3327-3331.
    • (1998) Applied and Environmental Microbiology , vol.64 , pp. 3327-3331
    • Dias, B.1    Weimer, B.2
  • 29
    • 0033988405 scopus 로고    scopus 로고
    • Identification and characterisation of a cystathionine β/γ-lyase from Lactococcus lactis susp. cremoris MG 1363
    • Dobric N, Limsowtin G K Y, Hillier A J, Dudman N P B and Davidson B E (2000) Identification and characterisation of a cystathionine β/γ-lyase from Lactococcus lactis susp. cremoris MG 1363. FEMS Microbiology Letters 182 249-254.
    • (2000) FEMS Microbiology Letters , vol.182 , pp. 249-254
    • Dobric, N.1    Limsowtin, G.K.Y.2    Hillier, A.J.3    Dudman, N.P.B.4    Davidson, B.E.5
  • 30
    • 0038295982 scopus 로고    scopus 로고
    • A new approach to monitoring proteolysis phenomena using antibodies specifically directed against the enzyme cleavage site on its substrate
    • Dupont D, Rolet-Repecaud O and Senocq D (2003) A new approach to monitoring proteolysis phenomena using antibodies specifically directed against the enzyme cleavage site on its substrate. Analytical Biochemistry 317 240-246.
    • (2003) Analytical Biochemistry , vol.317 , pp. 240-246
    • Dupont, D.1    Rolet-Repecaud, O.2    Senocq, D.3
  • 31
    • 0033752968 scopus 로고    scopus 로고
    • Partial purification and characterization of two aminotransferases from Lactococcus lactis subsp. cremoris B78 involved in the catabolism of methionine and branched-chain amino acids
    • Engels W J M, Alting A C, Arntz M M T G, Gruppen H, Voragen A G J, Smit G and Visser S (2000) Partial purification and characterization of two aminotransferases from Lactococcus lactis subsp. cremoris B78 involved in the catabolism of methionine and branched-chain amino acids. International Dairy Journal 10 443-452.
    • (2000) International Dairy Journal , vol.10 , pp. 443-452
    • Engels, W.J.M.1    Alting, A.C.2    Arntz, M.M.T.G.3    Gruppen, H.4    Voragen, A.G.J.5    Smit, G.6    Visser, S.7
  • 32
    • 33645387601 scopus 로고    scopus 로고
    • Other enzymes
    • Fox P F and McSweeney P L H, eds. New York: Kluwer Academic
    • Farkye N Y (2003) Other enzymes. In Advanced Dairy Chemistry, Vol. 1, Part A, pp 581-603. Fox P F and McSweeney P L H, eds. New York: Kluwer Academic.
    • (2003) Advanced Dairy Chemistry , vol.1 , Issue.PART A , pp. 581-603
    • Farkye, N.Y.1
  • 33
    • 84974083144 scopus 로고
    • Contribution of plasmin to Cheddar cheese ripening: Effect of added plasmin
    • Farkye N Y and Fox P F (1992) Contribution of plasmin to Cheddar cheese ripening: effect of added plasmin. Journal of Dairy Research 59 209-216.
    • (1992) Journal of Dairy Research , vol.59 , pp. 209-216
    • Farkye, N.Y.1    Fox, P.F.2
  • 34
    • 0002931507 scopus 로고
    • Thermal denaturation of indigenous milk enzymes
    • Fox P F, ed. Brussels: International Dairy Federation
    • Farkye N Y and Imafidon G I (1995) Thermal denaturation of indigenous milk enzymes. In Heat-Induced Changes in Milk, pp 331-348. Fox P F, ed. Brussels: International Dairy Federation.
    • (1995) Heat-Induced Changes in Milk , pp. 331-348
    • Farkye, N.Y.1    Imafidon, G.I.2
  • 35
    • 0034002469 scopus 로고    scopus 로고
    • Characterization of an arylesterase from Lactobacillus helveticus CNRZ32
    • Fenster K M, Parkin K L and Steele J L (2000) Characterization of an arylesterase from Lactobacillus helveticus CNRZ32. Journal of Applied Microbiology 88 572-583.
    • (2000) Journal of Applied Microbiology , vol.88 , pp. 572-583
    • Fenster, K.M.1    Parkin, K.L.2    Steele, J.L.3
  • 36
    • 0038749416 scopus 로고    scopus 로고
    • Intracellular esterase from Lactobacillus casei LILA. Nucleotide sequencing, purification and characterization
    • Fenster K M, Parkin K L and Steele J L (2003a) Intracellular esterase from Lactobacillus casei LILA. Nucleotide sequencing, purification and characterization. Journal of Dairy Science 86 1118-1129.
    • (2003) Journal of Dairy Science , vol.86 , pp. 1118-1129
    • Fenster, K.M.1    Parkin, K.L.2    Steele, J.L.3
  • 37
    • 2142856118 scopus 로고    scopus 로고
    • Nucleotide sequencing, purification and biochemical properties of an arylesterase from Lactobacillus casei LILA
    • Fenster K M, Parkin K L and Steele J L (2003b) Nucleotide sequencing, purification and biochemical properties of an arylesterase from Lactobacillus casei LILA. Journal of Dairy Science 86 2547-2557.
    • (2003) Journal of Dairy Science , vol.86 , pp. 2547-2557
    • Fenster, K.M.1    Parkin, K.L.2    Steele, J.L.3
  • 38
    • 0642279742 scopus 로고    scopus 로고
    • Accumulation of short n-chain ethyl esters by esterases of lactic acid bacteria under conditions simulating ripening Parmesan cheese
    • Fenster K M, Rankin S A and Steele J L (2003c) Accumulation of short n-chain ethyl esters by esterases of lactic acid bacteria under conditions simulating ripening Parmesan cheese. Journal of Dairy Science 86 2818-2825.
    • (2003) Journal of Dairy Science , vol.86 , pp. 2818-2825
    • Fenster, K.M.1    Rankin, S.A.2    Steele, J.L.3
  • 40
    • 0037214940 scopus 로고    scopus 로고
    • Functional properties of Bacillus proteinase hydrolysates of sodium caseinate incubated with transglutaminase pre- and post-hydrolysis of sodium caseinate incubated with transglutaminase pre- and post-hydrolysis
    • Flanagan J and FitzGerald R J (2003) Functional properties of Bacillus proteinase hydrolysates of sodium caseinate incubated with transglutaminase pre- and post-hydrolysis of sodium caseinate incubated with transglutaminase pre- and post-hydrolysis. International Dairy Journal 13 135-143.
    • (2003) International Dairy Journal , vol.13 , pp. 135-143
    • Flanagan, J.1    FitzGerald, R.J.2
  • 41
    • 0038058813 scopus 로고    scopus 로고
    • Antibacterial and antiviral effects of milk proteins and derivatives thereof
    • Floris R, Recio I, Berkhout B and Visser S (2003) Antibacterial and antiviral effects of milk proteins and derivatives thereof. Current Pharmaceutical Design 9 1257-1275.
    • (2003) Current Pharmaceutical Design , vol.9 , pp. 1257-1275
    • Floris, R.1    Recio, I.2    Berkhout, B.3    Visser, S.4
  • 42
    • 84911221722 scopus 로고
    • Proteolysis during cheese manufacture and ripening
    • Fox P F (1989) Proteolysis during cheese manufacture and ripening. Journal of Dairy Science 72 1379-1400.
    • (1989) Journal of Dairy Science , vol.72 , pp. 1379-1400
    • Fox, P.F.1
  • 43
    • 33645403277 scopus 로고    scopus 로고
    • Indigenous enzymes in milk
    • Fox P F and McSweeney P L H, eds. New York: Kluwer Academic
    • Fox P F (2003) Indigenous enzymes in milk. In Advanced Dairy Chemistry, Vol. 1, Part A, pp 467-471. Fox P F and McSweeney P L H, eds. New York: Kluwer Academic.
    • (2003) Advanced Dairy Chemistry , vol.1 , Issue.PART A , pp. 467-471
    • Fox, P.F.1
  • 44
    • 0000796762 scopus 로고
    • Exogenous enzymes in dairy technology
    • Fox P F, ed. London: Elsevier
    • Fox P F and Grufferty M D (1991) Exogenous enzymes in dairy technology. In Food Enzymology, Vol. 1, pp 219-270. Fox P F, ed. London: Elsevier.
    • (1991) Food Enzymology , vol.1 , pp. 219-270
    • Fox, P.F.1    Grufferty, M.D.2
  • 49
    • 0035987666 scopus 로고    scopus 로고
    • A history of pepsin and related enzymes
    • Fruton J S (2002) A history of pepsin and related enzymes. Quarterly Review of Biology 77 127-147.
    • (2002) Quarterly Review of Biology , vol.77 , pp. 127-147
    • Fruton, J.S.1
  • 51
    • 0030829690 scopus 로고    scopus 로고
    • Controls of the expression of aspA, the aspartyl protease gene from Penicillium roqueforti
    • Gente S, Durand N, Poussereau N and Fevre M (1997) Controls of the expression of aspA, the aspartyl protease gene from Penicillium roqueforti. Molecular and General Genetics 256 557-565.
    • (1997) Molecular and General Genetics , vol.256 , pp. 557-565
    • Gente, S.1    Durand, N.2    Poussereau, N.3    Fevre, M.4
  • 53
    • 21844519372 scopus 로고
    • Effect of aminopeptidase from Pseudomonas fluorescens ATTC-948 on synthetic bitter peptides, bitter hydrolysates of UHT milk proteins and on the ripening of Italian Caciotta-type cheese
    • Gobbetti M, Cossignani L, Simonetti M S and Diamani P (1995) Effect of aminopeptidase from Pseudomonas fluorescens ATTC-948 on synthetic bitter peptides, bitter hydrolysates of UHT milk proteins and on the ripening of Italian Caciotta-type cheese. Lait 75 169-179.
    • (1995) Lait , vol.75 , pp. 169-179
    • Gobbetti, M.1    Cossignani, L.2    Simonetti, M.S.3    Diamani, P.4
  • 54
    • 0031300639 scopus 로고    scopus 로고
    • Isolation and characterization of a tributyrin esterase from Lactobacillus plantarum 2739
    • Gobbetti M, Fox P F and Stepaniak L (1997a) Isolation and characterization of a tributyrin esterase from Lactobacillus plantarum 2739. Journal of Dairy Science 80 3099-3106.
    • (1997) Journal of Dairy Science , vol.80 , pp. 3099-3106
    • Gobbetti, M.1    Fox, P.F.2    Stepaniak, L.3
  • 55
    • 0030998505 scopus 로고    scopus 로고
    • Purification and characterization of a cell surface-associated esterase from Lactobacillus fermentum DT41
    • Gobbetti M, Smacchi E and Corsetti A (1997b) Purification and characterization of a cell surface-associated esterase from Lactobacillus fermentum DT41. International Dairy Journal 7 13-21.
    • (1997) International Dairy Journal , vol.7 , pp. 13-21
    • Gobbetti, M.1    Smacchi, E.2    Corsetti, A.3
  • 56
    • 0035104615 scopus 로고    scopus 로고
    • Purification and characterization of an extracellular proline iminopeptidase from Corynebacterium variabilis NCDO 2101
    • Gobbetti M, Smacchi E, Semeraro M, Fox P F, Lanciotti R and Cogan T (2001) Purification and characterization of an extracellular proline iminopeptidase from Corynebacterium variabilis NCDO 2101. Journal of Applied Microbiology 90 449-456.
    • (2001) Journal of Applied Microbiology , vol.90 , pp. 449-456
    • Gobbetti, M.1    Smacchi, E.2    Semeraro, M.3    Fox, P.F.4    Lanciotti, R.5    Cogan, T.6
  • 58
  • 59
    • 0031582837 scopus 로고    scopus 로고
    • Possible implications of milk pasteurization on the manufacture and sensory quality of ripened cheese
    • Grappin R and Beuvier E (1997) Possible implications of milk pasteurization on the manufacture and sensory quality of ripened cheese. International Dairy Journal 7 751-761.
    • (1997) International Dairy Journal , vol.7 , pp. 751-761
    • Grappin, R.1    Beuvier, E.2
  • 61
    • 0039712749 scopus 로고    scopus 로고
    • Accelerated maturation of cheese by proteolytic enzymes produced by Brevibacterium linens
    • Hayashi K (1996) Accelerated maturation of cheese by proteolytic enzymes produced by Brevibacterium linens. Japan Agricultural Research Quarterly 30 129-137.
    • (1996) Japan Agricultural Research Quarterly , vol.30 , pp. 129-137
    • Hayashi, K.1
  • 62
    • 0036012576 scopus 로고    scopus 로고
    • The influence of native and heat-denatured whey proteins on enzyme activity. 1. Plasmin
    • Hayes M G, McSweeney P L H and Kelly A L (2002) The influence of native and heat-denatured whey proteins on enzyme activity. 1. Plasmin. Milchwissenschaft 57 208-211.
    • (2002) Milchwissenschaft , vol.57 , pp. 208-211
    • Hayes, M.G.1    McSweeney, P.L.H.2    Kelly, A.L.3
  • 64
    • 0030087916 scopus 로고    scopus 로고
    • Purification of tributyrin esterase from Lactococcus lactis subsp. cremoris E8
    • Holland R and Coolbear T (1996) Purification of tributyrin esterase from Lactococcus lactis subsp. cremoris E8. Journal of Dairy Research 63 131-140.
    • (1996) Journal of Dairy Research , vol.63 , pp. 131-140
    • Holland, R.1    Coolbear, T.2
  • 66
    • 0036066607 scopus 로고    scopus 로고
    • Effects of high pressure on constituents and properties of milk
    • Huppertz T, Kelly A L and Fox P F (2002) Effects of high pressure on constituents and properties of milk. International Dairy Journal 12 561-572.
    • (2002) International Dairy Journal , vol.12 , pp. 561-572
    • Huppertz, T.1    Kelly, A.L.2    Fox, P.F.3
  • 69
    • 4043148450 scopus 로고    scopus 로고
    • Enzymatic coagulation of milk
    • Fox P F and McSweeney P L H, eds. New York: Kluwer Academic
    • Hyslop D B (2003) Enzymatic coagulation of milk. In Advanced Dairy Chemistry, Vol. 1 Part B, pp 839-878. Fox P F and McSweeney P L H, eds. New York: Kluwer Academic.
    • (2003) Advanced Dairy Chemistry , vol.1 , Issue.PART B , pp. 839-878
    • Hyslop, D.B.1
  • 70
    • 0039006236 scopus 로고    scopus 로고
    • Plasmin digestion of bovine beta-casein dephosphorylated with one protein phosphatase type 2A purified from Yarrowia lipolytica
    • Jolivet P, Macedo I Q, Wu M and Meunier J C (2000) Plasmin digestion of bovine beta-casein dephosphorylated with one protein phosphatase type 2A purified from Yarrowia lipolytica. Lait 80 517-526.
    • (2000) Lait , vol.80 , pp. 517-526
    • Jolivet, P.1    Macedo, I.Q.2    Wu, M.3    Meunier, J.C.4
  • 71
    • 0036181085 scopus 로고    scopus 로고
    • Pepsinogens, progastricins and prochymosins: Structure, function, evolution and development
    • Kageyama T (2002) Pepsinogens, progastricins and prochymosins: structure, function, evolution and development. Cellular and Molecular Life Sciences 59 288-306.
    • (2002) Cellular and Molecular Life Sciences , vol.59 , pp. 288-306
    • Kageyama, T.1
  • 72
    • 0742296737 scopus 로고    scopus 로고
    • Indigenous proteinases in milk
    • Fox P F and McSweeney P L H, eds. New York: Kluwer Academic
    • Kelly A L and McSweeney P L H (2003) Indigenous proteinases in milk. In Advanced Dairy Chemistry, Vol. 1, Part B, pp 495-521. Fox P F and McSweeney P L H, eds. New York: Kluwer Academic.
    • (2003) Advanced Dairy Chemistry , vol.1 , Issue.PART B , pp. 495-521
    • Kelly, A.L.1    McSweeney, P.L.H.2
  • 74
    • 0037008441 scopus 로고    scopus 로고
    • Determination of key enzyme activities in commercial peptidase and lipase preparations from microbial or animal sources
    • Kilcawley K N, Wilkinson M G and Fox P F (2002a) Determination of key enzyme activities in commercial peptidase and lipase preparations from microbial or animal sources. Enzyme Microbiology and Technology 31 310-320.
    • (2002) Enzyme Microbiology and Technology , vol.31 , pp. 310-320
    • Kilcawley, K.N.1    Wilkinson, M.G.2    Fox, P.F.3
  • 75
    • 0036263252 scopus 로고    scopus 로고
    • Properties of commercial microbial proteinase preparations
    • Kilcawley K N, Wilkinson M G and Fox P F (2002b) Properties of commercial microbial proteinase preparations. Food Biotechnology 16 29-55.
    • (2002) Food Biotechnology , vol.16 , pp. 29-55
    • Kilcawley, K.N.1    Wilkinson, M.G.2    Fox, P.F.3
  • 76
    • 0141922991 scopus 로고    scopus 로고
    • A novel lipase from Pseudomonas fluorescens HU380. Gene cloning, overproduction, renaturation-activation, two-step purification, and characterization
    • Kojima Y, Kobayashi M and Shimizu S (2003) A novel lipase from Pseudomonas fluorescens HU380. Gene cloning, overproduction, renaturation-activation, two-step purification, and characterization. Journal of Bioscience and Bioengineering 96 242-249.
    • (2003) Journal of Bioscience and Bioengineering , vol.96 , pp. 242-249
    • Kojima, Y.1    Kobayashi, M.2    Shimizu, S.3
  • 77
    • 0033899997 scopus 로고    scopus 로고
    • Investigation of the ability of a purified protease from Pseudomonas fluorescens RO98 to hydrolyze bitter peptides from cheese
    • Koka R and Wimer B C (2000) Investigation of the ability of a purified protease from Pseudomonas fluorescens RO98 to hydrolyze bitter peptides from cheese. International Dairy Journal 10 75-79.
    • (2000) International Dairy Journal , vol.10 , pp. 75-79
    • Koka, R.1    Wimer, B.C.2
  • 79
    • 0033987037 scopus 로고    scopus 로고
    • Hydrolysis of phospholipids by purified milk lipoprotein lipase-effect of apoprotein CII, CIII, A and E, and synthetic fragments
    • Lambert D A, Smith L C, Pownall H, Sparrow J T, Nicolas J P and Gotto A M (2000) Hydrolysis of phospholipids by purified milk lipoprotein lipase-effect of apoprotein CII, CIII, A and E, and synthetic fragments. Clinica Chimica Acta 291 19-33.
    • (2000) Clinica Chimica Acta , vol.291 , pp. 19-33
    • Lambert, D.A.1    Smith, L.C.2    Pownall, H.3    Sparrow, J.T.4    Nicolas, J.P.5    Gotto, A.M.6
  • 80
    • 0000717276 scopus 로고    scopus 로고
    • The individual or combined action of chymosin and plasmin on sodium caseinate or β-casein in solution: Effect of NaCl and pH
    • Lane C N and Fox P F (1999) The individual or combined action of chymosin and plasmin on sodium caseinate or β-casein in solution: effect of NaCl and pH. Lait 79 423-434.
    • (1999) Lait , vol.79 , pp. 423-434
    • Lane, C.N.1    Fox, P.F.2
  • 81
    • 0031767739 scopus 로고    scopus 로고
    • Cloning, expression, and chromosomal stabilization of the Propionibacterium shermanii proline iminopeptidase gene (pip) for food-grade application in Lactococcus lactis
    • Leenhouts K, Bolhuis A, Boot J, Deutz I, Toonen M, Venema G, Kok J and Ledeboer A (1998) Cloning, expression, and chromosomal stabilization of the Propionibacterium shermanii proline iminopeptidase gene (pip) for food-grade application in Lactococcus lactis. Applied and Environmental Microbiology 64 4736-4742.
    • (1998) Applied and Environmental Microbiology , vol.64 , pp. 4736-4742
    • Leenhouts, K.1    Bolhuis, A.2    Boot, J.3    Deutz, I.4    Toonen, M.5    Venema, G.6    Kok, J.7    Ledeboer, A.8
  • 82
    • 0032560081 scopus 로고    scopus 로고
    • Functional implications of the 21-24 loop in recombinant prochymosin
    • Li H Y, Zhang Y Y, Dong Y C and Yang K Y (1998) Functional implications of the 21-24 loop in recombinant prochymosin. Biochimica et Biophysica Acta 1384 121-129.
    • (1998) Biochimica et Biophysica Acta , vol.1384 , pp. 121-129
    • Li, H.Y.1    Zhang, Y.Y.2    Dong, Y.C.3    Yang, K.Y.4
  • 83
    • 0034960378 scopus 로고    scopus 로고
    • Purification and properties of intracellular esterases from Streptococcus thermophilus
    • Liu S Q, Holland R and Crow V L (2001) Purification and properties of intracellular esterases from Streptococcus thermophilus. International Dairy Journal 11 27-35.
    • (2001) International Dairy Journal , vol.11 , pp. 27-35
    • Liu, S.Q.1    Holland, R.2    Crow V, L.3
  • 84
    • 0037051526 scopus 로고    scopus 로고
    • Characterization of 'lettucine', a serine-like protease from Lactuca sativa leaves, as a novel enzyme for milk clotting
    • Lo Piero A R, Puglisi I and Petrone G (2002) Characterization of 'lettucine', a serine-like protease from Lactuca sativa leaves, as a novel enzyme for milk clotting. Journal of Agricultural and Food Chemistry 50 2439-2443.
    • (2002) Journal of Agricultural and Food Chemistry , vol.50 , pp. 2439-2443
    • Lo Piero, A.R.1    Puglisi, I.2    Petrone, G.3
  • 85
    • 0032981257 scopus 로고    scopus 로고
    • Purification and characterization of an acid phosphatase from Lactobacillus plantarum DPC2739
    • Magboul A A A and McSweeney P L H (1999a) Purification and characterization of an acid phosphatase from Lactobacillus plantarum DPC2739. Food Chemistry 65 15-22.
    • (1999) Food Chemistry , vol.65 , pp. 15-22
    • Magboul, A.A.A.1    McSweeney, P.L.H.2
  • 86
    • 0033494986 scopus 로고    scopus 로고
    • Purification and characterization of an acid phosphatase from Lactobacillus curvatus DPC2024
    • Magboul A A A and McSweeney P L H (1999b) Purification and characterization of an acid phosphatase from Lactobacillus curvatus DPC2024. International Dairy Journal 9 849-855.
    • (1999) International Dairy Journal , vol.9 , pp. 849-855
    • Magboul, A.A.A.1    McSweeney, P.L.H.2
  • 87
    • 0037735238 scopus 로고    scopus 로고
    • High pressure effects on proteolytic and glycolytic enzymes involved in cheese manufacturing
    • Malone A S, Wick C, Shellhammer T H and Courtney P D (2003) High pressure effects on proteolytic and glycolytic enzymes involved in cheese manufacturing. Journal of Dairy Science 86 1139-1146.
    • (2003) Journal of Dairy Science , vol.86 , pp. 1139-1146
    • Malone, A.S.1    Wick, C.2    Shellhammer, T.H.3    Courtney, P.D.4
  • 90
    • 0033887205 scopus 로고    scopus 로고
    • Predictive modelling of inactivation of bovine milk α-L-fucosidase in a high-temperature short-time pasteurizer
    • McKellar R C and Piyasena P (2000) Predictive modelling of inactivation of bovine milk α-L-fucosidase in a high-temperature short-time pasteurizer. International Dairy Journal 10 1-6.
    • (2000) International Dairy Journal , vol.10 , pp. 1-6
    • McKellar, R.C.1    Piyasena, P.2
  • 91
    • 0034409791 scopus 로고    scopus 로고
    • Biochemical pathways for the production of flavor compounds in cheeses during ripening: A review
    • McSweeney P L H and Sousa M J (2000) Biochemical pathways for the production of flavor compounds in cheeses during ripening: a review. Lait 80 293-324.
    • (2000) Lait , vol.80 , pp. 293-324
    • McSweeney, P.L.H.1    Sousa, M.J.2
  • 93
    • 0000615909 scopus 로고
    • Proteolysis of bovine caseins by cathepsin D: Preliminary observations and comparison with chymosin
    • McSweeney P L H, Fox P F and Olson N F (1995) Proteolysis of bovine caseins by cathepsin D: preliminary observations and comparison with chymosin. International Dairy Journal 5 321-336.
    • (1995) International Dairy Journal , vol.5 , pp. 321-336
    • McSweeney, P.L.H.1    Fox, P.F.2    Olson, N.F.3
  • 94
    • 0033267811 scopus 로고    scopus 로고
    • Optimization of a culture medium for acid proteolytic enzyme production by Penicillium camemberti
    • Mechakra A, Auberger B, Remeuf F and Lenoir J (1999) Optimization of a culture medium for acid proteolytic enzyme production by Penicillium camemberti. Sciences des Aliments 19 663-675.
    • (1999) Sciences des Aliments , vol.19 , pp. 663-675
    • Mechakra, A.1    Auberger, B.2    Remeuf, F.3    Lenoir, J.4
  • 95
    • 0141816841 scopus 로고    scopus 로고
    • Angiotensin I-converting-enzyme-inhibitory and antimicrobial peptides from Lactobacillus helveticus PR4 proteinase-hydrolyzed caseins of milk from six species
    • Minervini F F, Algaron F, Rizzello G G, Fox P F, Monnet V and Gobbetti M (2003) Angiotensin I-converting-enzyme-inhibitory and antimicrobial peptides from Lactobacillus helveticus PR4 proteinase-hydrolyzed caseins of milk from six species. Applied and Environmental Microbiology 69 5297-5305.
    • (2003) Applied and Environmental Microbiology , vol.69 , pp. 5297-5305
    • Minervini, F.F.1    Algaron, F.2    Rizzello, G.G.3    Fox, P.F.4    Monnet, V.5    Gobbetti, M.6
  • 96
    • 0034388496 scopus 로고    scopus 로고
    • Identification of peptides obtained via hydrolysis of bovine casein by chymosin using HPLC and mass spectrometry
    • Minkiewicz P, Slangen C J, Dziuba J, Visser S and Mioduszewska H (2000) Identification of peptides obtained via hydrolysis of bovine casein by chymosin using HPLC and mass spectrometry. Milchwissenschaft 55 14-17.
    • (2000) Milchwissenschaft , vol.55 , pp. 14-17
    • Minkiewicz, P.1    Slangen, C.J.2    Dziuba, J.3    Visser, S.4    Mioduszewska, H.5
  • 97
    • 0032172098 scopus 로고    scopus 로고
    • Identification of the principal water-insoluble peptides in Cheddar cheese
    • Mooney J S, Fox P F, Healy A and Leaver J (1998) Identification of the principal water-insoluble peptides in Cheddar cheese. International Dairy Journal 9 813-818.
    • (1998) International Dairy Journal , vol.9 , pp. 813-818
    • Mooney, J.S.1    Fox, P.F.2    Healy, A.3    Leaver, J.4
  • 98
    • 0034768744 scopus 로고    scopus 로고
    • Production of recombinant human bile salt-stimulated lipase in Pichia pastoris
    • Murasugi A, Asami Y and Mera-Kikuchi Y (2001) Production of recombinant human bile salt-stimulated lipase in Pichia pastoris. Protein Expression and Purification 23 282-288.
    • (2001) Protein Expression and Purification , vol.23 , pp. 282-288
    • Murasugi, A.1    Asami, Y.2    Mera-Kikuchi, Y.3
  • 99
    • 1842843894 scopus 로고    scopus 로고
    • The EstA esterase is responsible for the main capacity of Lactococcus lactis to synthesize short chain fatty acid esters in vitro
    • Nardi M, Fiez-Vandal C, Tailliez P and Monnet V (2002) The EstA esterase is responsible for the main capacity of Lactococcus lactis to synthesize short chain fatty acid esters in vitro. Journal of Applied Microbiology 93 994-1002.
    • (2002) Journal of Applied Microbiology , vol.93 , pp. 994-1002
    • Nardi, M.1    Fiez-Vandal, C.2    Tailliez, P.3    Monnet, V.4
  • 100
    • 0037164071 scopus 로고    scopus 로고
    • Plasmin system and microbial proteases in milk. Characteristics, roles and relationship
    • Nielsen S S (2002) Plasmin system and microbial proteases in milk. Characteristics, roles and relationship. Journal of Agricultural and Food Chemistry 50 6628-6634.
    • (2002) Journal of Agricultural and Food Chemistry , vol.50 , pp. 6628-6634
    • Nielsen, S.S.1
  • 101
    • 0036091967 scopus 로고    scopus 로고
    • Diversity in specificity of the extracellular proteinases in Lactobacillus helveticus and Lactobacillus delbrueckii subsp. bulgaricus
    • Oberg C J, Broadbent J R, Strickland M and McMahon D J (2002) Diversity in specificity of the extracellular proteinases in Lactobacillus helveticus and Lactobacillus delbrueckii subsp. bulgaricus. Letters in Applied Microbiology 34 455-460.
    • (2002) Letters in Applied Microbiology , vol.34 , pp. 455-460
    • Oberg, C.J.1    Broadbent, J.R.2    Strickland, M.3    McMahon, D.J.4
  • 102
    • 2442642385 scopus 로고    scopus 로고
    • Lipases in milk
    • Fox P F and McSweeney P L H, eds. New York: Kluwer Academic
    • Olivecrona T, Vilaró S and Olivecrona G (2003) Lipases in milk. In Advanced Dairy Chemistry, Vol. 1, Part A, pp 473-494. Fox P F and McSweeney P L H, eds. New York: Kluwer Academic.
    • (2003) Advanced Dairy Chemistry , vol.1 , Issue.PART A , pp. 473-494
    • Olivecrona, T.1    Vilaró, S.2    Olivecrona, G.3
  • 103
    • 0037301297 scopus 로고    scopus 로고
    • Proteolysis in miniature Cheddar-type cheeses made using blends of chymosin and Cynara cardunculus proteinases as coagulant
    • O'Mahony J A, Sousa M J and McSweeney P L H (2003) Proteolysis in miniature Cheddar-type cheeses made using blends of chymosin and Cynara cardunculus proteinases as coagulant. International Journal of Dairy Technology 53 52-58.
    • (2003) International Journal of Dairy Technology , vol.53 , pp. 52-58
    • O'Mahony, J.A.1    Sousa, M.J.2    McSweeney, P.L.H.3
  • 104
    • 0025123346 scopus 로고
    • The multicatalytic proteinase complex, a major extra-lysosomal proteolytic system
    • Orlowski M (1990) The multicatalytic proteinase complex, a major extra-lysosomal proteolytic system. Biochemistry 29 10289-10297.
    • (1990) Biochemistry , vol.29 , pp. 10289-10297
    • Orlowski, M.1
  • 105
    • 0036697624 scopus 로고    scopus 로고
    • Influence of transglutaminase treatment on some physico-chemical properties of milk
    • O'Sullivan M M, Kelly A L and Fox P F (2002) Influence of transglutaminase treatment on some physico-chemical properties of milk. Journal of Dairy Research 69 433-442.
    • (2002) Journal of Dairy Research , vol.69 , pp. 433-442
    • O'Sullivan, M.M.1    Kelly, A.L.2    Fox, P.F.3
  • 106
    • 0037691597 scopus 로고    scopus 로고
    • Measurement of plasminogen concentration and differentiation of plasmin and plasminogen using Fourier-transform infrared spectroscopy
    • Ozen B F, Hayes K D and Mauer L J (2003) Measurement of plasminogen concentration and differentiation of plasmin and plasminogen using Fourier-transform infrared spectroscopy. International Dairy Journal 13 441-446.
    • (2003) International Dairy Journal , vol.13 , pp. 441-446
    • Ozen, B.F.1    Hayes, K.D.2    Mauer, L.J.3
  • 107
    • 0033965923 scopus 로고    scopus 로고
    • Molecular mechanisms of plasminogen activation: Bacterial cofactors provide clues
    • Parry M A A, Zhang X C and Bode W (2000) Molecular mechanisms of plasminogen activation: bacterial cofactors provide clues. Trends in Biochemical Sciences 25 53-59.
    • (2000) Trends in Biochemical Sciences , vol.25 , pp. 53-59
    • Parry, M.A.A.1    Zhang, X.C.2    Bode, W.3
  • 108
    • 0037254316 scopus 로고    scopus 로고
    • Exchanging lactocepin plasmids in lactococcal starters to study bitterness development in Gouda cheese: A preliminary investigation
    • Pillidge C J, Crow V L, Coolbear T and Reid J R (2003) Exchanging lactocepin plasmids in lactococcal starters to study bitterness development in Gouda cheese: a preliminary investigation. International Dairy Journal 13 345-354.
    • (2003) International Dairy Journal , vol.13 , pp. 345-354
    • Pillidge, C.J.1    Crow, V.L.2    Coolbear, T.3    Reid, J.R.4
  • 109
    • 0034792492 scopus 로고    scopus 로고
    • Molecular characterization of a phosphatidylcholine-hydrolyzing phospholipase C
    • Preuss I, Kaiser I and Gehring U (2001) Molecular characterization of a phosphatidylcholine-hydrolyzing phospholipase C. European Journal of Biochemistry 268 5081-5091.
    • (2001) European Journal of Biochemistry , vol.268 , pp. 5081-5091
    • Preuss, I.1    Kaiser, I.2    Gehring, U.3
  • 110
    • 75149173568 scopus 로고    scopus 로고
    • Lactoperoxidase
    • Fox P F and McSweeney P L H, eds. New York: Kluwer Academic
    • Pruitt K (2003) Lactoperoxidase. In Advanced Dairy Chemistry, Vol. 1, Part A, pp 545-561. Fox P F and McSweeney P L H, eds. New York: Kluwer Academic.
    • (2003) Advanced Dairy Chemistry , vol.1 , Issue.PART A , pp. 545-561
    • Pruitt, K.1
  • 112
    • 0031507342 scopus 로고    scopus 로고
    • Purification and characterisation of an intracellular aminopeptidase from Brevibacterium linens ATCC 9174
    • Rattray F P and Fox P F (1997) Purification and characterisation of an intracellular aminopeptidase from Brevibacterium linens ATCC 9174. Lait 77 169-180.
    • (1997) Lait , vol.77 , pp. 169-180
    • Rattray, F.P.1    Fox, P.F.2
  • 113
    • 0040577827 scopus 로고    scopus 로고
    • Recently identified enzymes of Brevibacterium linens ATCC 9174 - A review
    • Rattray F P and Fox P F (1998) Recently identified enzymes of Brevibacterium linens ATCC 9174 - a review. Journal of Food Biochemistry 22 353-373.
    • (1998) Journal of Food Biochemistry , vol.22 , pp. 353-373
    • Rattray, F.P.1    Fox, P.F.2
  • 114
    • 0033125574 scopus 로고    scopus 로고
    • Aspects of enzymology and biochemical properties of Brevibacterium linens relevant to cheese ripening: A review
    • Rattray F P and Fox P F (1999) Aspects of enzymology and biochemical properties of Brevibacterium linens relevant to cheese ripening: a review. Journal of Dairy Science 82 91-908.
    • (1999) Journal of Dairy Science , vol.82 , pp. 91-908
    • Rattray, F.P.1    Fox, P.F.2
  • 115
    • 0029088274 scopus 로고
    • Purification and characterization of an extracellular proteinase from Brevibacterium linens ATCC 9174
    • Rattray F P, Bockelmann W and Fox P F (1995) Purification and characterization of an extracellular proteinase from Brevibacterium linens ATCC 9174. Applied and Environmental Microbiology 61 3454-3456.
    • (1995) Applied and Environmental Microbiology , vol.61 , pp. 3454-3456
    • Rattray, F.P.1    Bockelmann, W.2    Fox, P.F.3
  • 117
    • 0030920070 scopus 로고    scopus 로고
    • Specificity of an extracellular proteinase from Brevibacterium linens ATCC 9174 on bovine β-casein
    • Rattray F P, Fox P F and Healy A (1997) Specificity of an extracellular proteinase from Brevibacterium linens ATCC 9174 on bovine β-casein. Applied and Environmental Microbiology 63 2468-2471.
    • (1997) Applied and Environmental Microbiology , vol.63 , pp. 2468-2471
    • Rattray, F.P.1    Fox, P.F.2    Healy, A.3
  • 118
    • 0029036451 scopus 로고
    • Evolutionary families of metallopeptidases
    • Rawling N D and Barret A J (1995) Evolutionary families of metallopeptidases. Methods in Enzymology 248 183-228.
    • (1995) Methods in Enzymology , vol.248 , pp. 183-228
    • Rawling, N.D.1    Barret, A.J.2
  • 119
  • 120
    • 0001737559 scopus 로고
    • Spectrophotometric assay of plasmin and plasminogen in bovine milk
    • Rollema H S, Visser S and Poll J K (1983) Spectrophotometric assay of plasmin and plasminogen in bovine milk. Milchwissenschaft 38 214-217.
    • (1983) Milchwissenschaft , vol.38 , pp. 214-217
    • Rollema, H.S.1    Visser, S.2    Poll, J.K.3
  • 121
    • 0034868610 scopus 로고    scopus 로고
    • Debittering of protein hydrolyzates
    • Saha B and Hayashi K (2001) Debittering of protein hydrolyzates. Biotechnology Advances 19 355-370.
    • (2001) Biotechnology Advances , vol.19 , pp. 355-370
    • Saha, B.1    Hayashi, K.2
  • 122
    • 0034768028 scopus 로고    scopus 로고
    • Enzymatic assays for native plasmin, plasminogen and plasminogen activators in bovine milk
    • Saint-Denis T, Humbert G and Gaillard J L (2001) Enzymatic assays for native plasmin, plasminogen and plasminogen activators in bovine milk. Journal of Dairy Research 68 437-449.
    • (2001) Journal of Dairy Research , vol.68 , pp. 437-449
    • Saint-Denis, T.1    Humbert, G.2    Gaillard, J.L.3
  • 123
    • 0033113750 scopus 로고    scopus 로고
    • A new carboxylesterase from Brevibacterium linens IFO 12171 responsible for the conversion of 1,4-butanediol diacrylate to 4-hydroxybutyl acrylate: Purification, characterization, gene cloning, and gene expression in Escherichia coli
    • Sakai Y, Ishikawa J, Fukasaka S, Yurimoto H, Mitsui R, Yanase H and Kato N (1999) A new carboxylesterase from Brevibacterium linens IFO 12171 responsible for the conversion of 1,4-butanediol diacrylate to 4-hydroxybutyl acrylate: purification, characterization, gene cloning, and gene expression in Escherichia coli. Bioscience, Biotechnology and Biochemistry 63 688-697.
    • (1999) Bioscience, Biotechnology and Biochemistry , vol.63 , pp. 688-697
    • Sakai, Y.1    Ishikawa, J.2    Fukasaka, S.3    Yurimoto, H.4    Mitsui, R.5    Yanase, H.6    Kato, N.7
  • 126
    • 2442693702 scopus 로고    scopus 로고
    • Indigenous phosphatases in milk
    • Fox P F and McSweeney P L H, eds. New York: Kluwer Academic
    • Shakeel-ur-Rehman, Fleming C M, Farkye N Y and Fox P F (2003) Indigenous phosphatases in milk. In Advanced Dairy Chemistry, Vol. 1, Part A, pp 523-543. Fox P F and McSweeney P L H, eds. New York: Kluwer Academic.
    • (2003) Advanced Dairy Chemistry , vol.1 , Issue.PART A , pp. 523-543
    • Shakeel-Ur-Rehman1    Fleming, C.M.2    Farkye, N.Y.3    Fox, P.F.4
  • 127
    • 0037049937 scopus 로고    scopus 로고
    • Extracellular protease from Pseudomonas sp (CL 1457) active against Xanthomonas campestris
    • Shastry S and Prasad M S (2002) Extracellular protease from Pseudomonas sp (CL 1457) active against Xanthomonas campestris. Process Biochemistry 37 611-621.
    • (2002) Process Biochemistry , vol.37 , pp. 611-621
    • Shastry, S.1    Prasad, M.S.2
  • 128
    • 0032529909 scopus 로고    scopus 로고
    • Purification and characterization of cystathionine γ-lyase from Lactobacillus fermentum DT41
    • Smacchi E and Gobbetti M (1998) Purification and characterization of cystathionine γ-lyase from Lactobacillus fermentum DT41. FEMS Microbiology Letters 166 197-202.
    • (1998) FEMS Microbiology Letters , vol.166 , pp. 197-202
    • Smacchi, E.1    Gobbetti, M.2
  • 129
    • 0032774442 scopus 로고    scopus 로고
    • Purification and characterization of an extracellular proline iminopeptidase from Arthrobacter nicotianae 9458
    • Smacchi E, Gobbetti M, Lanciotti R and Fox P F (1999) Purification and characterization of an extracellular proline iminopeptidase from Arthrobacter nicotianae 9458. FEMS Microbiology Letters 178 191-197.
    • (1999) FEMS Microbiology Letters , vol.178 , pp. 191-197
    • Smacchi, E.1    Gobbetti, M.2    Lanciotti, R.3    Fox, P.F.4
  • 130
    • 0036217926 scopus 로고    scopus 로고
    • Matrix-assisted laser desorption/ionization time-of-flight mass spectrometry method for the quantification of β-casein fragment (f193-209)
    • Soeryapranata E, Powers J R, Hill H H, Siems W F, Al-Saad K and Weller K M (2002) Matrix-assisted laser desorption/ionization time-of-flight mass spectrometry method for the quantification of β-casein fragment (f193-209). Journal of Food Science 67 534-538.
    • (2002) Journal of Food Science , vol.67 , pp. 534-538
    • Soeryapranata, E.1    Powers, J.R.2    Hill, H.H.3    Siems, W.F.4    Al-Saad, K.5    Weller, K.M.6
  • 131
    • 0001291004 scopus 로고
    • Microbial enzymes in spoilage of milk and dairy products
    • Fox P F, ed. London: Elsevier
    • Sørhaug T and Stepaniak L (1991) Microbial enzymes in spoilage of milk and dairy products. In Food Enzymology, Vol. 1, pp 169-218. Fox P F, ed. London: Elsevier.
    • (1991) Food Enzymology , vol.1 , pp. 169-218
    • Sørhaug, T.1    Stepaniak, L.2
  • 132
    • 0031079863 scopus 로고    scopus 로고
    • Psychrotrophs and their enzymes in milk and dairy products: Quality aspects
    • Sørhaug T and Stepaniak L (1997) Psychrotrophs and their enzymes in milk and dairy products: quality aspects. Trends in Food Science and Technology 8 35-41.
    • (1997) Trends in Food Science and Technology , vol.8 , pp. 35-41
    • Sørhaug, T.1    Stepaniak, L.2
  • 133
    • 0028936937 scopus 로고
    • The presence of two proteinases associated with the cell wall of Lactobacillus bulgaricus
    • Stefanitsi D, Sakellaris G and Garel J R (1995) The presence of two proteinases associated with the cell wall of Lactobacillus bulgaricus. FEMS Microbiology Letters 128 53-58.
    • (1995) FEMS Microbiology Letters , vol.128 , pp. 53-58
    • Stefanitsi, D.1    Sakellaris, G.2    Garel, J.R.3
  • 134
    • 0036006179 scopus 로고    scopus 로고
    • Isolation and partial characterization of catalytic antibodies with oligonuclease activity from bovine colostrum
    • Stepaniak L (2002) Isolation and partial characterization of catalytic antibodies with oligonuclease activity from bovine colostrum. Preparative Biochemistry and Biotechnology 32 17-28.
    • (2002) Preparative Biochemistry and Biotechnology , vol.32 , pp. 17-28
    • Stepaniak, L.1
  • 135
    • 75149173568 scopus 로고    scopus 로고
    • Indigenous nucleases in milk
    • Fox P F and McSweeney P L H, eds. New York: Kluwer Academic
    • Stepaniak L, Fleming C M, Gobbetti M, Corsetti A and Fox P F (2003) Indigenous nucleases in milk. In Advanced Dairy Chemistry, Vol. 1, Part A, pp 545-561. Fox P F and McSweeney P L H, eds. New York: Kluwer Academic.
    • (2003) Advanced Dairy Chemistry , vol.1 , Issue.PART A , pp. 545-561
    • Stepaniak, L.1    Fleming, C.M.2    Gobbetti, M.3    Corsetti, A.4    Fox, P.F.5
  • 136
    • 0000554706 scopus 로고
    • Characterization of the principal intracellular endopeptidase from Lactococcus lactis sbsp. lactis MG1363
    • Stepaniak L and Fox P F (1995) Characterization of the principal intracellular endopeptidase from Lactococcus lactis sbsp. lactis MG1363. International Dairy Journal 5 699-713.
    • (1995) International Dairy Journal , vol.5 , pp. 699-713
    • Stepaniak, L.1    Fox, P.F.2
  • 137
    • 0011172666 scopus 로고
    • Thermal inactivation of bacterial enzymes in milk
    • Fox P F, ed. Brussels: International Dairy Federation
    • Stepaniak L and Sørhaug T (1995) Thermal inactivation of bacterial enzymes in milk. In Heat-Induced Changes in Milk, pp 349-363. Fox P F, ed. Brussels: International Dairy Federation.
    • (1995) Heat-Induced Changes in Milk , pp. 349-363
    • Stepaniak, L.1    Sørhaug, T.2
  • 138
    • 0041118861 scopus 로고    scopus 로고
    • Degradation of β-casein fragments 193-209 and 194-209 by oligopeptidases and cytoplasms from Lactococcus and Lactobacillus
    • Stepaniak L and Sørhaug T (2001) Degradation of β-casein fragments 193-209 and 194-209 by oligopeptidases and cytoplasms from Lactococcus and Lactobacillus. Natural Sciences (Poland) 8 145-152.
    • (2001) Natural Sciences (Poland) , vol.8 , pp. 145-152
    • Stepaniak, L.1    Sørhaug, T.2
  • 140
    • 0034803741 scopus 로고    scopus 로고
    • Immunorelatedness of oligopeptidases from Lactobacillus and Lactococcus and proline iminopeptidase from Propionibacterium using double immunodiffusion assay
    • Stepaniak L, Wróblewska B, Jedrychowski L and Sørhaug T (2001) Immunorelatedness of oligopeptidases from Lactobacillus and Lactococcus and proline iminopeptidase from Propionibacterium using double immunodiffusion assay. Food and Agricultural Immunology 13 183-187.
    • (2001) Food and Agricultural Immunology , vol.13 , pp. 183-187
    • Stepaniak, L.1    Wróblewska, B.2    Jedrychowski, L.3    Sørhaug, T.4
  • 143
    • 0036780428 scopus 로고    scopus 로고
    • Overexpression of peptidases in Lactococcus and evaluation of their release from leaky cells
    • Tuler T R, Callanan M J and Klaenhammer T R (2002) Overexpression of peptidases in Lactococcus and evaluation of their release from leaky cells. Journal of Dairy Science 85 2438-2450.
    • (2002) Journal of Dairy Science , vol.85 , pp. 2438-2450
    • Tuler, T.R.1    Callanan, M.J.2    Klaenhammer, T.R.3
  • 144
    • 0036132417 scopus 로고    scopus 로고
    • Effect of added α-ketoglutaric acid, pyruvic acid or pyridoxal phosphate on proteolyis and quality of Cheddar cheese
    • Ur-Rehman S and Fox P F (2002) Effect of added α-ketoglutaric acid, pyruvic acid or pyridoxal phosphate on proteolyis and quality of Cheddar cheese. Food Chemistry 76 21-26.
    • (2002) Food Chemistry , vol.76 , pp. 21-26
    • Ur-Rehman, S.1    Fox, P.F.2
  • 145
    • 0031725571 scopus 로고    scopus 로고
    • Autolysis of Lactobacillus helveticus and Propionibacterium freudenreichii in Swiss cheese: First evidence using species-specific lysis markers
    • Valence F, Richoux R, Thierry A and Lortal S (1998) Autolysis of Lactobacillus helveticus and Propionibacterium freudenreichii in Swiss cheese: first evidence using species-specific lysis markers. Journal of Dairy Research 65 609-620.
    • (1998) Journal of Dairy Research , vol.65 , pp. 609-620
    • Valence, F.1    Richoux, R.2    Thierry, A.3    Lortal, S.4
  • 146
    • 0029018457 scopus 로고
    • The vegetable rennet of Cynara cardunculus L. contains two proteinases with chymosin and pepsin-like specificities
    • Veríssimo P, Esteves C, Faro C and Pires E (1995) The vegetable rennet of Cynara cardunculus L. contains two proteinases with chymosin and pepsin-like specificities. Biotechnology Letters 17 621-626.
    • (1995) Biotechnology Letters , vol.17 , pp. 621-626
    • Veríssimo, P.1    Esteves, C.2    Faro, C.3    Pires, E.4
  • 147
    • 0035158341 scopus 로고    scopus 로고
    • Leaky Lactococcus cultures that externalize enzymes and antigens independently of culture lysis and secretion and export pathways
    • Walker S A and Klaenhammer T R (2001) Leaky Lactococcus cultures that externalize enzymes and antigens independently of culture lysis and secretion and export pathways. Applied and Environmental Microbiology 67 251-259.
    • (2001) Applied and Environmental Microbiology , vol.67 , pp. 251-259
    • Walker, S.A.1    Klaenhammer, T.R.2
  • 148
    • 0036653591 scopus 로고    scopus 로고
    • Whey components: Millennia of evolution create functionalities for mammalian nutrition. What we know and what we may be overlooking
    • Walzem R L, Dillard C J and German J B (2002) Whey components: millennia of evolution create functionalities for mammalian nutrition. What we know and what we may be overlooking. Critical Reviews in Food Science and Nutrition 42 353-375.
    • (2002) Critical Reviews in Food Science and Nutrition , vol.42 , pp. 353-375
    • Walzem, R.L.1    Dillard, C.J.2    German, J.B.3
  • 149
    • 0034692872 scopus 로고    scopus 로고
    • First demonstration of an inhibitory activity of milk proteins against human immunodeficiency virus-1 reverse transcriptase and the effect of succinylation
    • Wang X, Ye X and Ng T B (2002) First demonstration of an inhibitory activity of milk proteins against human immunodeficiency virus-1 reverse transcriptase and the effect of succinylation. Life Sciences 67 2745-2752.
    • (2002) Life Sciences , vol.67 , pp. 2745-2752
    • Wang, X.1    Ye, X.2    Ng, T.B.3
  • 152
    • 0033981077 scopus 로고    scopus 로고
    • Characterization and role of the branched-chain aminotransferase (BcaT) isolated from Lactococcus lactis subsp. cremoris NCDO 763
    • Yvon M, Chambellon E, Bolotin A and Roudot-Algaron F (2000) Characterization and role of the branched-chain aminotransferase (BcaT) isolated from Lactococcus lactis subsp. cremoris NCDO 763. Applied and Environmental Microbiology 66 571-577.
    • (2000) Applied and Environmental Microbiology , vol.66 , pp. 571-577
    • Yvon, M.1    Chambellon, E.2    Bolotin, A.3    Roudot-Algaron, F.4
  • 153
    • 0034878905 scopus 로고    scopus 로고
    • Cheese flavour formation by amino acid catabolism
    • Yvon M and Rijnen L (2001) Cheese flavour formation by amino acid catabolism. International Dairy Journal 11 185-201.
    • (2001) International Dairy Journal , vol.11 , pp. 185-201
    • Yvon, M.1    Rijnen, L.2
  • 154
    • 0030999851 scopus 로고    scopus 로고
    • An aminotransferase from Lactococcus lactis initiates conversion of aromatic amino acids to flavor compounds
    • Yvon M, Thirouin L, Rijnen D, Fromentier D and Gripon J C (1997) An aminotransferase from Lactococcus lactis initiates conversion of aromatic amino acids to flavor compounds. Applied and Environmental Microbiology 63 414-419.
    • (1997) Applied and Environmental Microbiology , vol.63 , pp. 414-419
    • Yvon, M.1    Thirouin, L.2    Rijnen, D.3    Fromentier, D.4    Gripon, J.C.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.