Zobrazeno 1 - 10
of 66
pro vyhledávání: '"J.-C. Gripon"'
Autor:
S. Kawabata, L. Vassal, D. Le Bars, B. Cesselin, M. Nardi, J. C. Gripon, M. P. Chapot-Chartier
Publikováno v:
Le Lait. 77:229-239
Summary - The autolysis of starter bacteria during chee se ripening results in the release of intracellular enzymes, especially peptidases, into the curd and in consequence is expected to accelerate and enhance the development of cheese flavour. In t
Autor:
H.-E. Spinnler, J.-C. Gripon
Publisher Summary This chapter discusses the different methods of production and technologies of these cheeses, the microflora, the various biochemical changes that occur during their ripening, their aroma and textural properties, and the control of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::2e8c263b1f3cc6088580801ebf6c4507
https://doi.org/10.1016/s1874-558x(04)80043-5
https://doi.org/10.1016/s1874-558x(04)80043-5
Autor:
J.-C Gripon, M.-Y Mistou
Publikováno v:
Biochimica et Biophysica Acta (BBA)-Protein Structure and Molecular Enzymology
Biochimica et Biophysica Acta (BBA)-Protein Structure and Molecular Enzymology, Elsevier, 1998, 1383, pp.63-70
Biochimica et Biophysica Acta (BBA)-Protein Structure and Molecular Enzymology, Elsevier, 1998, 1383, pp.63-70
PepC is a cytoplasmic thiol aminopeptidase widely conserved among lactic acid bacteria. PepC from Lactococcus lactis shares 35-38% identity with aminopeptidases of eukaryotic origins: the yeast and mammalian bleomycin hydrolases (BLMase). In this wor
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::257cdd73dd41f3b2c8ecc2eed7144cdd
https://hal.inrae.fr/hal-02693349
https://hal.inrae.fr/hal-02693349
Autor:
J.-C. Gripon
Publikováno v:
Microbiology and Biochemistry of Cheese and Fermented Milk ISBN: 9781461284277
Cheeses can be classified schematically according to their moisture content into three major categories: hard, semi-hard and soft cheeses. The higher the moisture content/casein ratio, the softer the casein matrix of cheese. Soft cheeses have a typic
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::121dae9f1299771fecf72d4394539f17
https://doi.org/10.1007/978-1-4613-1121-8_5
https://doi.org/10.1007/978-1-4613-1121-8_5
Publikováno v:
Biotechnology and applied biochemistry. 20(1)
Xaa-Pro-dipeptidyl-aminopeptidase (EC 3.4.14.5) from Lactococcus lactis (PepX) was used, for the first time, as a catalyst in kinetically controlled synthesis of peptide bonds involving proline. PepX had amidase and esterase activities in addition to
Publikováno v:
Biotechnology and applied biochemistry. 18(1)
In previous papers we have reported that an aminopeptidase A (EC 3.4.11.7) purified from Staphylococcus chromogenes was able to catalyse the introduction of L-malic acid at the N-terminus of Tyr and Phe derivatives. We now show that this enzyme can b
Autor:
J. C. Gripon
Publikováno v:
Cheese: Chemistry, Physics and Microbiology ISBN: 9781461361374
Cheese: Chemistry, Physics and Microbiology ISBN: 9780834213395
Cheese: Chemistry, Physics and Microbiology ISBN: 9780834213395
Mould-ripened cheeses represent a small proportion of world cheese production. However, these cheeses are becoming increasingly popular with consumers and there is an increasing demand for them. Blue-veined cheeses have long been produced in various
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::be5291f82cded7b2ecc14a318b603473
https://doi.org/10.1007/978-1-4615-2648-3_4
https://doi.org/10.1007/978-1-4615-2648-3_4
Publikováno v:
Biomedica biochimica acta. 50(10-11)
A peptidase from the non pathogenic Staphylococcus sp. strain BEC 299 was purified to a final specific activity of 84,400 U/mg protein. Its molecular weight is 450 kDa and optimum pH 10.0. This enzyme catalyzes the synthesis of dipeptides (aspartame)
Autor:
T Hofmann, J C Gripon
Publikováno v:
Biochemical Journal. 193:55-65
Butane-2,3-dione inactivates the aspartyl proteinases from Penicillium roqueforti and Penicillium caseicolum, as well as pig pepsin, penicillopepsin and Rhizopus pepsin, at pH 6.0 in the presence of light but not in the dark. The inactivation is due