메뉴 건너뛰기




Volumn 77, Issue 1, 2011, Pages 179-186

Simultaneous presence of PrtH and PrtH2 proteinases in Lactobacillus helveticus strains improves breakdown of the pure αs1-casein

Author keywords

[No Author keywords available]

Indexed keywords

CASEIN MICELLES; CELL ENVELOPES; CLEAVAGE SPECIFICITY; HYDROLYSIS KINETICS; LACTOBACILLUS HELVETICUS; PROTEOLYTIC ACTIVITIES; SODIUM DODECYL SULFATE; SYNTHETIC SUBSTRATES; WHOLE CELL;

EID: 79251633760     PISSN: 00992240     EISSN: 10985336     Source Type: Journal    
DOI: 10.1128/AEM.01466-10     Document Type: Article
Times cited : (67)

References (47)
  • 1
    • 0027169421 scopus 로고
    • Two cellwall- associated aminopeptidases from Lactobacillus helveticus and the purification and characterization of APII from strain ITGL1
    • Blanc, B., P. Laloi, D. Atlan, C. Gilbert, and R. Portalier. 1993. Two cellwall- associated aminopeptidases from Lactobacillus helveticus and the purification and characterization of APII from strain ITGL1. J. Gen. Microbiol. 139:1441-1448.
    • (1993) J. Gen. Microbiol. , vol.139 , pp. 1441-1448
    • Blanc, B.1    Laloi, P.2    Atlan, D.3    Gilbert, C.4    Portalier, R.5
  • 4
    • 38949186542 scopus 로고    scopus 로고
    • Occurrence of the angiotensin-converting enzyme inhibiting tripeptides Val- Pro-Pro and Ile-Pro-Pro in different cheese varieties of Swiss origin
    • Bütikofer, U., J. Meyer, R. Sieber, B. Walther, and D. Wechsler. 2008. Occurrence of the angiotensin-converting enzyme inhibiting tripeptides Val- Pro-Pro and Ile-Pro-Pro in different cheese varieties of Swiss origin. J. Dairy Sci. 91:29-38.
    • (2008) J. Dairy Sci. , vol.91 , pp. 29-38
    • Bütikofer, U.1    Meyer, J.2    Sieber, R.3    Walther, B.4    Wechsler, D.5
  • 6
    • 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 phosphopeptides
    • Deutsch, S. M., D. Mollé, V. Gagnaire, M. Piot, D. Atlan, and S. Lortal. 2000. Hydrolysis of sequenced β-casein peptides provides new insight into peptidase activity from thermophilic lactic acid bacteria and highlights intrinsic resistance of phosphopeptides. Appl. Environ. Microbiol. 66:5360-5367.
    • (2000) Appl. Environ. Microbiol. , vol.66 , pp. 5360-5367
    • Deutsch, S.M.1    Mollé, D.2    Gagnaire, V.3    Piot, M.4    Atlan, D.5    Lortal, S.6
  • 7
    • 0037088879 scopus 로고    scopus 로고
    • Early lysis of Lactobacillus helveticus CNRZ 303 in Swiss cheese is not prophage-related
    • Deutsch, S. M., A. Neveu, S. Guezenec, P. Ritzenthaler, and S. Lortal. 2003. Early lysis of Lactobacillus helveticus CNRZ 303 in Swiss cheese is not prophage-related. Int. J. Food Microbiol. 81:147-157.
    • (2003) Int. J. Food Microbiol. , vol.81 , pp. 147-157
    • Deutsch, S.M.1    Neveu, A.2    Guezenec, S.3    Ritzenthaler, P.4    Lortal, S.5
  • 8
    • 0025087747 scopus 로고
    • Differences in short peptide-substrate cleavage by two cell-envelope-located serine proteinases of Lactococcus lactis subsp Cremoris are related to secondary binding specificity
    • Exterkate, F. A. 1990. Differences in short peptide-substrate cleavage by two cell-envelope-located serine proteinases of Lactococcus lactis subsp. Cremoris are related to secondary binding specificity. Appl. Microbiol. Biotechnol. 33:401-406.
    • (1990) Appl. Microbiol. Biotechnol. , vol.33 , pp. 401-406
    • Exterkate, F.A.1
  • 10
    • 0033759602 scopus 로고    scopus 로고
    • Streptococcus thermophilus cell wall-anchored proteinase: Release, purification, and biochemical and genetic characterization
    • Fernandez-Espla, M. D., P. Garault, V. Monnet, and F. Rul. 2000. Streptococcus thermophilus cell wall-anchored proteinase: release, purification, and biochemical and genetic characterization. Appl. Environ. Microbiol. 66:4772-4778.
    • (2000) Appl. Environ. Microbiol. , vol.66 , pp. 4772-4778
    • Fernandez-Espla, M.D.1    Garault, P.2    Monnet, V.3    Rul, F.4
  • 11
    • 0035997811 scopus 로고    scopus 로고
    • Role of bacterial cell wall proteinase in antihypertension
    • Flambard, B. 2002. Role of bacterial cell wall proteinase in antihypertension. Sci. Aliment. 22:209-222.
    • (2002) Sci. Aliment. , vol.22 , pp. 209-222
    • Flambard, B.1
  • 13
    • 0034832894 scopus 로고    scopus 로고
    • Peptides identified during Emmental cheese ripening: Origin and proteolytic systems involved
    • Gagnaire, V., D. Mollé, M. Herrouin, and J. Léonil. 2001. Peptides identified during Emmental cheese ripening: origin and proteolytic systems involved. J. Agric. Food Chem. 49:4402-4413.
    • (2001) J. Agric. Food Chem. , vol.49 , pp. 4402-4413
    • Gagnaire, V.1    Mollé, D.2    Herrouin, M.3    Léonil, J.4
  • 14
    • 0030207403 scopus 로고    scopus 로고
    • Phosphopeptides interacting with colloidal calcium phosphate isolated by tryptic hydrolysis of bovine casein micelles
    • Gagnaire, V., A. Pierre, D. Mollé, and J. Léonil. 1996. Phosphopeptides interacting with colloidal calcium phosphate isolated by tryptic hydrolysis of bovine casein micelles. J. Dairy Res. 63:405-422.
    • (1996) J. Dairy Res. , vol.63 , pp. 405-422
    • Gagnaire, V.1    Pierre, A.2    Mollé, D.3    Léonil, J.4
  • 15
    • 0042427117 scopus 로고    scopus 로고
    • Relationship between acidification capacity in milk, presence of yeast extract, proteolytic and peptidase activities in Lactobacillus helveticus species
    • Gatti, M., M. E. Fornasari, A. Perrone, and E. Neviani. 1999. Relationship between acidification capacity in milk, presence of yeast extract, proteolytic and peptidase activities in Lactobacillus helveticus species. Microbiol. Aliment. Nutr. 17:23-31.
    • (1999) Microbiol. Aliment. Nutr. , vol.17 , pp. 23-31
    • Gatti, M.1    Fornasari, M.E.2    Perrone, A.3    Neviani, E.4
  • 16
    • 66249097755 scopus 로고    scopus 로고
    • PrtH2, not prtH, is the ubiquitous cell wall proteinase gene in Lactobacillus helveticus
    • Genay, M., L. Sadat, V. Gagnaire, and S. Lortal. 2009. prtH2, not prtH, is the ubiquitous cell wall proteinase gene in Lactobacillus helveticus. Appl. Environ. Microbiol. 75:3238-3249.
    • (2009) Appl. Environ. Microbiol. , vol.75 , pp. 3238-3249
    • Genay, M.1    Sadat, L.2    Gagnaire, V.3    Lortal, S.4
  • 17
    • 0030668063 scopus 로고    scopus 로고
    • Comparison of cell surface proteinase activities within the Lactobacillus genus
    • Gilbert, C., B. Blanc, J. Frot-Coutaz, R. Portalier, and D. Atlan. 1997. Comparison of cell surface proteinase activities within the Lactobacillus genus. J. Dairy Res. 64:561-571.
    • (1997) J. Dairy Res. , vol.64 , pp. 561-571
    • Gilbert, C.1    Blanc, B.2    Frot-Coutaz, J.3    Portalier, R.4    Atlan, D.5
  • 18
    • 0000514035 scopus 로고
    • The colorimetric determination of leucine aminopeptidase in urine and serum of normal subjects and patients with cancer or diseases
    • Goldbarg, J. A., and A. M. Rutenberg. 1958. The colorimetric determination of leucine aminopeptidase in urine and serum of normal subjects and patients with cancer or diseases. Cancer 11:283-291.
    • (1958) Cancer , vol.11 , pp. 283-291
    • Goldbarg, J.A.1    Rutenberg, A.M.2
  • 19
    • 0001719953 scopus 로고
    • Analyse quantitative des caseines dans le lait de vache par chromatographie liquide rapide d'échange d'ions (FPLC)
    • Guillou, H., G. Miranda, and J. P. Pelissier. 1987. Analyse quantitative des caseines dans le lait de vache par chromatographie liquide rapide d'échange d'ions (FPLC). Lait 67:135-148.
    • (1987) Lait , vol.67 , pp. 135-148
    • Guillou, H.1    Miranda, G.2    Pelissier, J.P.3
  • 21
    • 1842414318 scopus 로고    scopus 로고
    • Characterization of a cell membrane-associated proteinase from Lactobacillus helveticus CRL 581
    • Hébert, E. M., R. R. Raya, and G. S. De Giori. 1997. Characterization of a cell membrane-associated proteinase from Lactobacillus helveticus CRL 581. Curr. Microbiol. 35:161-164.
    • (1997) Curr. Microbiol. , vol.35 , pp. 161-164
    • Hébert, E.M.1    Raya, R.R.2    De Giori, G.S.3
  • 22
    • 0036884532 scopus 로고    scopus 로고
    • Modulation of the cell-surface proteinase activity of thermophilic lactobacilli by the peptide supply
    • Hébert, E. M., R. R. Raya, and G. S. De Giori. 2002. Modulation of the cell-surface proteinase activity of thermophilic lactobacilli by the peptide supply. Curr. Microbiol. 45:385-389.
    • (2002) Curr. Microbiol. , vol.45 , pp. 385-389
    • Hébert, E.M.1    Raya, R.R.2    De Giori, G.S.3
  • 23
    • 33846202861 scopus 로고    scopus 로고
    • Characterization of proteolytic activity of Lactobacillus helveticus strains in milk
    • Hébert, E. M., R. R. Raya, G. Oliver, and G. S. De Giori. 1996. Characterization of proteolytic activity of Lactobacillus helveticus strains in milk. Microbiol. Aliment. Nutr. 14:65-72.
    • (1996) Microbiol. Aliment. Nutr. , vol.14 , pp. 65-72
    • Hébert, E.M.1    Raya, R.R.2    Oliver, G.3    De Giori, G.S.4
  • 24
    • 0343244629 scopus 로고    scopus 로고
    • Characterization of natural isolates of Lactobacillus strains to be used as starter cultures in dairy fermentation
    • Hébert, E. M., R. R. Raya, P. Tailliez, and G. S. De Giori. 2000. Characterization of natural isolates of Lactobacillus strains to be used as starter cultures in dairy fermentation. Int. J. Food Microbiol. 59:19-27.
    • (2000) Int. J. Food Microbiol. , vol.59 , pp. 19-27
    • Hébert, E.M.1    Raya, R.R.2    Tailliez, P.3    De Giori, G.S.4
  • 26
    • 69349102534 scopus 로고    scopus 로고
    • Variation in caseinolytic properties of six cheese related Lactobacillus helveticus strains
    • Jensen, M. P., F. K. Vogensen, and Y. Ardo. 2009. Variation in caseinolytic properties of six cheese related Lactobacillus helveticus strains. Int. Dairy J. 19:661-668.
    • (2009) Int. Dairy J. , vol.19 , pp. 661-668
    • Jensen, M.P.1    Vogensen, F.K.2    Ardo, Y.3
  • 29
    • 0027586726 scopus 로고
    • Three-dimensional molecular modeling of bovine caseins: An energy-minimized β-casein structure
    • Kumosinski, T. F., E. M. Brown, and H. M. Farrell, Jr. 1993. Three-dimensional molecular modeling of bovine caseins: an energy-minimized β-casein structure. J. Dairy Sci. 76:931-945.
    • (1993) J. Dairy Sci. , vol.76 , pp. 931-945
    • Kumosinski, T.F.1    Brown, E.M.2    Farrell Jr., H.M.3
  • 31
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 32
    • 0028269929 scopus 로고
    • Purification and characterization of the mature, membrane-associated cell-envelope proteinase of Lactobacillus helveticus L89
    • Martin-Hernandez, M. C., A. C. Alting, and F. A. Exterkate. 1994. Purification and characterization of the mature, membrane-associated cell-envelope proteinase of Lactobacillus helveticus L89. Appl. Microbiol. Biotechnol. 40: 828-834.
    • (1994) Appl. Microbiol. Biotechnol. , vol.40 , pp. 828-834
    • Martin-Hernandez, M.C.1    Alting, A.C.2    Exterkate, F.A.3
  • 33
    • 0035523213 scopus 로고    scopus 로고
    • Immunomodulating effects of milks fermented by Lactobacillus helveticus and its non-proteolytic variant
    • Matar, C., J. C. Valdez, M. Medina, M. Rachid, and G. Perdigon. 2001. Immunomodulating effects of milks fermented by Lactobacillus helveticus and its non-proteolytic variant. J. Dairy Res. 68:601-609.
    • (2001) J. Dairy Res. , vol.68 , pp. 601-609
    • Matar, C.1    Valdez, J.C.2    Medina, M.3    Rachid, M.4    Perdigon, G.5
  • 34
    • 0036091967 scopus 로고    scopus 로고
    • Diversity in specificity of the extracellular proteinases in Lactobacillus helveticus and Lactobacillus delbrueckii subsp bulgaricus
    • Oberg, C. J., J. R. Broadbent, M. Strickland, and D. J. McMahon. 2002. Diversity in specificity of the extracellular proteinases in Lactobacillus helveticus and Lactobacillus delbrueckii subsp. bulgaricus. Lett. Appl. Microbiol. 34:455-460.
    • (2002) Lett. Appl. Microbiol. , vol.34 , pp. 455-460
    • Oberg, C.J.1    Broadbent, J.R.2    Strickland, M.3    McMahon, D.J.4
  • 36
    • 0032783298 scopus 로고    scopus 로고
    • Genetic characterization of a cell envelope-associated proteinase from Lactobacillus helveticus CNRZ32
    • Pederson, J. A., G. J. Mileski, and B. C. Weimer. 1999. Genetic characterization of a cell envelope-associated proteinase from Lactobacillus helveticus CNRZ32. J. Bacteriol. 181:4592-4597.
    • (1999) J. Bacteriol. , vol.181 , pp. 4592-4597
    • Pederson, J.A.1    Mileski, G.J.2    Weimer, B.C.3
  • 37
    • 0026605009 scopus 로고
    • s2-casein. Parallel and antiparallel alignments of the polypeptide chains
    • 2-casein. Parallel and antiparallel alignments of the polypeptide chains. J. Biochem. 203:381-386.
    • (1992) J. Biochem. , vol.203 , pp. 381-386
    • Rasmussen, L.K.1    Hojrup, P.2    Petersen, T.E.3
  • 40
    • 0023472472 scopus 로고
    • Tricine-sodium dodecyl sulfatepolyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa
    • Schägger, H., and G. von Jagow. 1987. Tricine-sodium dodecyl sulfatepolyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa. Anal. Biochem. 166:368-379.
    • (1987) Anal. Biochem. , vol.166 , pp. 368-379
    • Schägger, H.1    Von Jagow, G.2
  • 41
    • 0002022204 scopus 로고
    • Déshydratation des laits enrichis en caséine micellaire par microfiltration; Comparaison des propriétés des poudres obtenues avec celles d'une poudre de lait ultra-propre
    • Schuck, P., M. Piot, S. Mejean, J. Fauquant, G. Brulé, and J. L. Maubois. 1994. Déshydratation des laits enrichis en caséine micellaire par microfiltration; comparaison des propriétés des poudres obtenues avec celles d'une poudre de lait ultra-propre. Lait 74:47-63.
    • (1994) Lait , vol.74 , pp. 47-63
    • Schuck, P.1    Piot, M.2    Mejean, S.3    Fauquant, J.4    Brulé, G.5    Maubois, J.L.6
  • 42
    • 33749388946 scopus 로고    scopus 로고
    • Extraction and partial characterization of proteolytic activities from the cell surface of Lactobacillus helveticus Zuc2
    • Scolari, G., M. Vescovo, C. Zacconi, and F. Vescovi. 2006. Extraction and partial characterization of proteolytic activities from the cell surface of Lactobacillus helveticus Zuc2. J. Dairy Sci. 89:3800-3809.
    • (2006) J. Dairy Sci. , vol.89 , pp. 3800-3809
    • Scolari, G.1    Vescovo, M.2    Zacconi, C.3    Vescovi, F.4
  • 44
    • 0029150758 scopus 로고
    • Zymogram and preliminary characterization of Lactobacillus helveticus autolysins
    • Valence, F., and S. Lortal. 1995. Zymogram and preliminary characterization of Lactobacillus helveticus autolysins. Appl. Environ. Microbiol. 61:3391-3399.
    • (1995) Appl. Environ. Microbiol. , vol.61 , pp. 3391-3399
    • Valence, F.1    Lortal, S.2
  • 45
    • 0027373433 scopus 로고
    • Purification and specificity of a cell-wall-associated proteinase from Lactobacillus helveticus CP790
    • Yamamoto, N., A. Akino, and T. Takano. 1993. Purification and specificity of a cell-wall-associated proteinase from Lactobacillus helveticus CP790. J. Biochem. 114:740-745.
    • (1993) J. Biochem. , vol.114 , pp. 740-745
    • Yamamoto, N.1    Akino, A.2    Takano, T.3
  • 46
    • 0001236615 scopus 로고
    • Properties and specificity of a cell-wall proteinase from Lactobacillus helveticus
    • Zevaco, C., and J.-C. Gripon. 1988. Properties and specificity of a cell-wall proteinase from Lactobacillus helveticus. Lait 68:393-408.
    • (1988) Lait , vol.68 , pp. 393-408
    • Zevaco, C.1    Gripon, J.-C.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.