메뉴 건너뛰기




Volumn 53, Issue 4, 2001, Pages 349-359

Effects of transglutaminase treatment on the production of set skim milk yoghurt: Microbiological aspects

Author keywords

[No Author keywords available]

Indexed keywords


EID: 0039888229     PISSN: 00231347     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (26)

References (36)
  • 2
    • 0034466658 scopus 로고    scopus 로고
    • Physiological study of Lactobacillus delbrueckii subsp. bulgaricus strains in a novel chemically defined medium
    • Chervaux, C., Ehrlich, S. D., Maguin, E.: Physiological study of Lactobacillus delbrueckii subsp. bulgaricus strains in a novel chemically defined medium. Appl. Environ. Microbiol. 66 5306-5311 (2000)
    • (2000) Appl. Environ. Microbiol. , vol.66 , pp. 5306-5311
    • Chervaux, C.1    Ehrlich, S.D.2    Maguin, E.3
  • 5
    • 0030945452 scopus 로고    scopus 로고
    • Viability of yoghurt and probiotic bacteria in yoghurts made from commercial starter cultures
    • Dave, R. I., Shah, N. P.: Viability of yoghurt and probiotic bacteria in yoghurts made from commercial starter cultures. Int. Dairy J. 7 31-41 (1997)
    • (1997) Int. Dairy J. , vol.7 , pp. 31-41
    • Dave, R.I.1    Shah, N.P.2
  • 6
    • 84981836237 scopus 로고
    • J. A medium for the cultivation of lactobacilli
    • De Man, J.C., Rogosa, M., Sharpe, M.E.: J. A medium for the cultivation of lactobacilli. Appl. Bacteriol. 23130-135 (1960)
    • (1960) Appl. Bacteriol. , vol.23 , pp. 130-135
    • De Man, J.C.1    Rogosa, M.2    Sharpe, M.E.3
  • 7
    • 0015504858 scopus 로고
    • Isolation and amino acid composition of casein peptides stimulating growth of Streptococcus thermophilus
    • Desmazeaud, M., Hermier, J. H.: Isolation and amino acid composition of casein peptides stimulating growth of Streptococcus thermophilus. Eur. J. Biochem. 28 190-198 (1972)
    • (1972) Eur. J. Biochem. , vol.28 , pp. 190-198
    • Desmazeaud, M.1    Hermier, J.H.2
  • 8
    • 0034469733 scopus 로고    scopus 로고
    • Hydrolysis of sequenced ß-casein peptides provides new insight into peptidase activity from thermophilic lactic acid bacteria and highlights intrinsic resistance of phosphopeptides
    • Deutsch, S.-M., Molle, D., Gagnaire, V., Piot, M., Atlan, D., Lortal, S.: Hydrolysis of sequenced ß-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)
    • (2000) Appl. Environ. Microbiol. , vol.66 , pp. 5360-5367
    • Deutsch, S.-M.1    Molle, D.2    Gagnaire, V.3    Piot, M.4    Atlan, D.5    Lortal, S.6
  • 9
    • 0031259385 scopus 로고    scopus 로고
    • Enzymic crosslinking as a tool for food colloid rheology control and interfacial stabilization
    • Dickinson, E.: Enzymic crosslinking as a tool for food colloid rheology control and interfacial stabilization. Trends in Food Sci. Technol. 8 334-339 (1997)
    • (1997) Trends in Food Sci. Technol. , vol.8 , pp. 334-339
    • Dickinson, E.1
  • 10
    • 21744448778 scopus 로고    scopus 로고
    • Transglutaminase: Effect on rheological properties, microstructure and permeability of set style acid skim milk gel
    • Færgemand, M. , Qvist, K. B.: Transglutaminase: effect on rheological properties, microstructure and permeability of set style acid skim milk gel. Food Hydrocolloids 11 287-292 (1997)
    • (1997) Food Hydrocolloids , vol.11 , pp. 287-292
    • Færgemand, M.1    Qvist, K.B.2
  • 12
    • 0033457897 scopus 로고    scopus 로고
    • Matrix-assisted laser desorption/ionization mass spectrometry for monitoring bacterial protein digestion in yoghurt production
    • Fedele, L., Seraglia, R., Battistotti, B., Pinelli, C., Traldi, P.: Matrix-assisted laser desorption/ionization mass spectrometry for monitoring bacterial protein digestion in yoghurt production. J. Mass Spectrom. 34 1338-1345 (1999)
    • (1999) J. Mass Spectrom. , vol.34 , pp. 1338-1345
    • Fedele, L.1    Seraglia, R.2    Battistotti, B.3    Pinelli, C.4    Traldi, P.5
  • 13
    • 0033759602 scopus 로고    scopus 로고
    • Streptococcus thermophilus cell wallanchored proteinase: Release, purification, and biochemical and genetic characterization
    • Fernandez-Espla, M. D., Garault, P., Monnet, V., Rul., F.: Streptococcus thermophilus cell wallanchored proteinase: release, purification, and biochemical and genetic characterization. Appl. Environ. Microbiol. 66 4772-4778 (2000)
    • (2000) Appl. Environ. Microbiol. , vol.66 , pp. 4772-4778
    • Fernandez-Espla, M.D.1    Garault, P.2    Monnet, V.3    Rul, F.4
  • 14
    • 0037016736 scopus 로고    scopus 로고
    • Three oligopeptide-binding proteins are involved in the oligopeptide transport of Streptococcus thermophilus
    • Garault, P., Le Bars, D., Besset, C., Monnet, V.: Three oligopeptide-binding proteins are involved in the oligopeptide transport of Streptococcus thermophilus. J. Biol. Chem. 277 32-39 (2002)
    • (2002) J. Biol. Chem. , vol.277 , pp. 32-39
    • Garault, P.1    Le Bars, D.2    Besset, C.3    Monnet, V.4
  • 15
    • 0029941580 scopus 로고    scopus 로고
    • A new cell surface proteinase: Sequencing and analysis of the prtB gene from Lactobacillus delbrueckii subsp. bulgaricus
    • Gilbert, C., Atlan, D., Blanc, B., Portalier, R., Germond, J. E., Lapierre, L., Mollet, B.: A new cell surface proteinase: sequencing and analysis of the prtB gene from Lactobacillus delbrueckii subsp. bulgaricus. J. Bacteriol. 1783059-3065 (1996)
    • (1996) J. Bacteriol. , vol.178 , pp. 3059-3065
    • Gilbert, C.1    Atlan, D.2    Blanc, B.3    Portalier, R.4    Germond, J.E.5    Lapierre, L.6    Mollet, B.7
  • 16
    • 0027223075 scopus 로고
    • Primary structure of microbial transglutaminase from Streptoverticillium sp. strain s-8112
    • Kanaji, T., Ozaki, H., Takao, T., Kawajiri, H., Ide, H., Motoki, M., Shimonishi, Y.: Primary structure of microbial transglutaminase from Streptoverticillium sp. strain s-8112. J. Biol. Chem. 268 11565-11572 (1993)
    • (1993) J. Biol. Chem. , vol.268 , pp. 11565-11572
    • Kanaji, T.1    Ozaki, H.2    Takao, T.3    Kawajiri, H.4    Ide, H.5    Motoki, M.6    Shimonishi, Y.7
  • 18
    • 0001299553 scopus 로고    scopus 로고
    • Relationship between the crosslinking of caseins by transglutaminase and the gel strength of yoghurt
    • Lauber, S., Henle, T., Klostermeyer, H.: Relationship between the crosslinking of caseins by transglutaminase and the gel strength of yoghurt. Eur. Food Res. Technol. 210 305-309 (2000)
    • (2000) Eur. Food Res. Technol. , vol.210 , pp. 305-309
    • Lauber, S.1    Henle, T.2    Klostermeyer, H.3
  • 19
    • 0030890402 scopus 로고    scopus 로고
    • Review article: Proteolytic enzymes of lactic acid bacteria
    • Law, J., Haandrikman, A.: Review article: proteolytic enzymes of lactic acid bacteria. Int. Dairy J. 71-11 (1997)
    • (1997) Int. Dairy J. , vol.7 , pp. 1-11
    • Law, J.1    Haandrikman, A.2
  • 20
    • 0033931002 scopus 로고    scopus 로고
    • Identification of stress-inducible proteins in Lactobacillus delbrueckii subsp. bulgaricus
    • Lim, E. M., Ehrlich, S. D., Maguin, E.: Identification of stress-inducible proteins in Lactobacillus delbrueckii subsp. bulgaricus. Electrophoresis 21 2557-2561 (2000)
    • (2000) Electrophoresis , vol.21 , pp. 2557-2561
    • Lim, E.M.1    Ehrlich, S.D.2    Maguin, E.3
  • 21
    • 0041048223 scopus 로고    scopus 로고
    • Auswirkung der enzymatischen quervernetzung von milchproteinen auf die resultierenden eigenschaften von joghurterzeugnissen
    • Lorenzen, P. Chr., Mautner, A., Schlimme, E.: Auswirkung der enzymatischen Quervernetzung von Milchproteinen auf die resultierenden Eigenschaften von Joghurterzeugnissen. Kiel. Milchwirtsch. Forschungsber. 51 89-97 (1999)
    • (1999) Kiel. Milchwirtsch. Forschungsber. , vol.51 , pp. 89-97
    • Lorenzen, P.Chr.1    Mautner, A.2    Schlimme, E.3
  • 22
    • 0002139312 scopus 로고    scopus 로고
    • Properties and potential fields of application of transglutaminase preparations in dairying
    • Lorenzen, P. Chr., Schlimme, E.: Properties and potential fields of application of transglutaminase preparations in dairying. Bulletin of the IDF 332 47-53 (1998)
    • (1998) Bulletin of the IDF , vol.332 , pp. 47-53
    • Lorenzen, P.Chr.1    Schlimme, E.2
  • 23
    • 0034366655 scopus 로고    scopus 로고
    • Techno-functional properties of transglutaminase-treated milk proteins
    • Lorenzen, P. Chr.: Techno-functional properties of transglutaminase-treated milk proteins. Milchwissenschaft 55 667-670 (2000)
    • (2000) Milchwissenschaft , vol.55 , pp. 667-670
    • Lorenzen, P.Chr.1
  • 24
    • 0040162341 scopus 로고    scopus 로고
    • Isolierung von Lactobacillus delbrueckii subsp. bulgaricus mutanten zur herstellung eines joghurts mit milder geschmackscharakteristik
    • Möller, C., Bockelmann, W., Heller, K. J.: Isolierung von Lactobacillus delbrueckii subsp. bulgaricus Mutanten zur Herstellung eines Joghurts mit milder Geschmackscharakteristik. Kiel. Milchwirtsch. Forschungsber. 53 167-185 (2001)
    • (2001) Kiel. Milchwirtsch. Forschungsber. , vol.53 , pp. 167-185
    • Möller, C.1    Bockelmann, W.2    Heller, K.J.3
  • 27
    • 0033666883 scopus 로고    scopus 로고
    • Cross-linking casein micelles by a microbial transglutaminase conditions for formation of transglutaminase-induced gels
    • Schorsch, C., Carrie, H., Clark, A. H., Norton, I. T.: Cross-linking casein micelles by a microbial transglutaminase conditions for formation of transglutaminase-induced gels. Int. Dairy J. 10 519-528 (2000)
    • (2000) Int. Dairy J. , vol.10 , pp. 519-528
    • Schorsch, C.1    Carrie, H.2    Clark, A.H.3    Norton, I.T.4
  • 28
    • 0033673716 scopus 로고    scopus 로고
    • Cross-linking casein micelles by a microbial transglutaminase: Influence of cross-links in acid-induced gelation
    • Schorsch, C., Carrie, H., Norton, I. T.: Cross-linking casein micelles by a microbial transglutaminase: influence of cross-links in acid-induced gelation. Int. Dairy J. 10 529-539 (2000)
    • (2000) Int. Dairy J. , vol.10 , pp. 529-539
    • Schorsch, C.1    Carrie, H.2    Norton, I.T.3
  • 29
    • 0035209417 scopus 로고    scopus 로고
    • Influence of transglutaminase treatment of skim milk on the formation of ε-(γ-glutamyl)lysine and the susceptibility of individual proteins towards crosslinking
    • Sharma, R., Lorenzen, P. Chr., Qvist, K. B.: Influence of transglutaminase treatment of skim milk on the formation of ε-(γ-glutamyl)lysine and the susceptibility of individual proteins towards crosslinking. Int. Dairy J. 11 785-793 (2001)
    • (2001) Int. Dairy J. , vol.11 , pp. 785-793
    • Sharma, R.1    Lorenzen, P.Chr.2    Qvist, K.B.3
  • 30
    • 0034048221 scopus 로고    scopus 로고
    • Dynamic changes of intercellular ph in individual lactic acid bacterium cells in response to a rapid drop in extracellular pH
    • Siegumfeldt, H., Rechinger, K. B., Jakobsen, M.: Dynamic changes of intercellular pH in individual lactic acid bacterium cells in response to a rapid drop in extracellular pH. Appl. Environ. Microbiol. 66 2330-2335 (2000)
    • (2000) Appl. Environ. Microbiol. , vol.66 , pp. 2330-2335
    • Siegumfeldt, H.1    Rechinger, K.B.2    Jakobsen, M.3
  • 31
    • 0032871626 scopus 로고    scopus 로고
    • Multi-domain, cell-envelope proteinases of lactic acid bacteria
    • Siezen, R. J.: Multi-domain, cell-envelope proteinases of lactic acid bacteria. Ant. v. Leeuwenhoek 76 139-155 (1999)
    • (1999) Ant. V. Leeuwenhoek , vol.76 , pp. 139-155
    • Siezen, R.J.1
  • 32
    • 0030889269 scopus 로고    scopus 로고
    • A zinc-dependent proteinase from the cell wall of lactobacillus delbrueckii subsp. bulgaricus
    • Stefanitsi, D., Garel, J.-R.: A zinc-dependent proteinase from the cell wall of Lactobacillus delbrueckii subsp. bulgaricus. Lett. Appl. Microbiol. 24: 180-184 (1997)
    • (1997) Lett. Appl. Microbiol. , vol.24 , pp. 180-184
    • Stefanitsi, D.1    Garel, J.-R.2
  • 33
    • 0038182440 scopus 로고    scopus 로고
    • Biochemistry of fermentation
    • (Tamine, A. Y., Robinson, R. K., eds.). CRC Press, Boca Raton, New York, Washington DC
    • nd ed. (Tamine, A. Y., Robinson, R. K., eds.) pp. 432-485. CRC Press, Boca Raton, New York, Washington DC (1999)
    • (1999) nd Ed. , pp. 432-485
    • Tamine, A.Y.1    Robinson, R.K.2
  • 34
    • 77953151430 scopus 로고    scopus 로고
    • Microbiology of yogurt and "bio"starter cultures
    • (Tamine, A. Y., Robinson, R. K., eds.), CRC Press, Boca Raton, New York, Washington DC
    • nded. (Tamine, A. Y., Robinson, R. K., eds.) pp. 389-431, CRC Press, Boca Raton, New York, Washington DC (1999)
    • (1999) nded. , pp. 389-431
    • Tamine, A.Y.1    Robinson, R.K.2
  • 35
    • 0016686551 scopus 로고
    • Improved medium for lactic streptococci and their bacteriophages
    • Terzaghi, B.E., Sandine, W.E.: Improved medium for lactic streptococci and their bacteriophages. Appl. Microbiol. 29 807-813 (1975)
    • (1975) Appl. Microbiol. , vol.29 , pp. 807-813
    • Terzaghi, B.E.1    Sandine, W.E.2
  • 36
    • 0003142603 scopus 로고
    • Metabolism and biochemical characteristics of yogurt bacteria
    • Zourari, A., Accolas, J. P., Desmazeaud, M. J.: Metabolism and biochemical characteristics of yogurt bacteria. A review. Lait 72 1-34 (1992)
    • (1992) A Review. Lait , vol.72 , pp. 1-34
    • Zourari, A.1    Accolas, J.P.2    Desmazeaud, M.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.