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184 related items for PubMed ID: 25465631
1. Classification of Lactococcus lactis cell envelope proteinase based on gene sequencing, peptides formed after hydrolysis of milk, and computer modeling. Børsting MW, Qvist KB, Brockmann E, Vindeløv J, Pedersen TL, Vogensen FK, Ardö Y. J Dairy Sci; 2015 Jan; 98(1):68-77. PubMed ID: 25465631 [Abstract] [Full Text] [Related]
2. Diversity of cell envelope proteinase specificity among strains of Lactococcus lactis and its relationship to charge characteristics of the substrate-binding region. Exterkate FA, Alting AC, Bruinenberg PG. Appl Environ Microbiol; 1993 Nov; 59(11):3640-7. PubMed ID: 8285671 [Abstract] [Full Text] [Related]
3. Engineering of the substrate-binding region of the subtilisin-like, cell-envelope proteinase of Lactococcus lactis. Siezen RJ, Bruinenberg PG, Vos P, van Alen-Boerrigter I, Nijhuis M, Alting AC, Exterkate FA, de Vos WM. Protein Eng; 1993 Nov; 6(8):927-37. PubMed ID: 8309942 [Abstract] [Full Text] [Related]
4. The contribution of caseins to the amino acid supply for Lactococcus lactis depends on the type of cell envelope proteinase. Flambard B, Helinck S, Richard J, Juillard V. Appl Environ Microbiol; 1998 Jun; 64(6):1991-6. PubMed ID: 9603805 [Abstract] [Full Text] [Related]
5. Specificity of hydrolysis of bovine kappa-casein by cell envelope-associated proteinases from Lactococcus lactis strains. Reid JR, Coolbear T, Pillidge CJ, Pritchard GG. Appl Environ Microbiol; 1994 Mar; 60(3):801-6. PubMed ID: 8161175 [Abstract] [Full Text] [Related]
6. Specificity of a cell-envelope-located proteinase (PIII-type) from Lactococcus lactis subsp. cremoris AM1 in its action on bovine beta-casein. Visser S, Robben AJ, Slangen CJ. Appl Microbiol Biotechnol; 1991 Jul; 35(4):477-83. PubMed ID: 1367552 [Abstract] [Full Text] [Related]
7. Substrate specificity of the cell envelope-located proteinase of Lactococcus lactis subsp. lactis NCDO 763. Monnet V, Ley JP, Gonzàlez S. Int J Biochem; 1992 May; 24(5):707-18. PubMed ID: 1592148 [Abstract] [Full Text] [Related]
8. Cloning and partial sequencing of the proteinase gene complex from Lactococcus lactis subsp. lactis UC317. Law J, Vos P, Hayes F, Daly C, de Vos WM, Fitzgerald G. J Gen Microbiol; 1992 Apr; 138(4):709-18. PubMed ID: 1588305 [Abstract] [Full Text] [Related]
9. The autoproteolysis of Lactococcus lactis lactocepin III affects its specificity towards beta-casein. Flambard B, Juillard V. Appl Environ Microbiol; 2000 Dec; 66(12):5134-40. PubMed ID: 11097880 [Abstract] [Full Text] [Related]
10. Accumulation of casein-derived peptides during growth of proteinase-positive strains of Lactococcus lactis in milk: their contribution to subsequent bacterial growth is impaired by their internal transport. Foucaud C, Juillard V. J Dairy Res; 2000 May; 67(2):233-40. PubMed ID: 10840677 [Abstract] [Full Text] [Related]
11. The extracellular PI-type proteinase of Lactococcus lactis hydrolyzes beta-casein into more than one hundred different oligopeptides. Juillard V, Laan H, Kunji ER, Jeronimus-Stratingh CM, Bruins AP, Konings WN. J Bacteriol; 1995 Jun; 177(12):3472-8. PubMed ID: 7768856 [Abstract] [Full Text] [Related]
12. Action of a cell-envelope proteinase (CEPIII-type) from Lactococcus lactis subsp. cremoris AM1 on bovine kappa-casein. Visser S, Slangen CJ, Robben AJ, van Dongen WD, Heerma W, Haverkamp J. Appl Microbiol Biotechnol; 1994 Aug; 41(6):644-51. PubMed ID: 7765163 [Abstract] [Full Text] [Related]
13. Transport of beta-casein-derived peptides by the oligopeptide transport system is a crucial step in the proteolytic pathway of Lactococcus lactis. Kunji ER, Hagting A, De Vries CJ, Juillard V, Haandrikman AJ, Poolman B, Konings WN. J Biol Chem; 1995 Jan 27; 270(4):1569-74. PubMed ID: 7829486 [Abstract] [Full Text] [Related]
14. Prevention of C-terminal autoprocessing of Lactococcus lactis SK11 cell-envelope proteinase by engineering of an essential surface loop. Bruinenberg PG, de Vos WM, Siezen RJ. Biochem J; 1994 Sep 15; 302 ( Pt 3)(Pt 3):957-63. PubMed ID: 7945226 [Abstract] [Full Text] [Related]
15. Role of calcium in activity and stability of the Lactococcus lactis cell envelope proteinase. Exterkate FA, Alting AC. Appl Environ Microbiol; 1999 Apr 15; 65(4):1390-6. PubMed ID: 10103227 [Abstract] [Full Text] [Related]
16. Hydrolysis of caseins and formation of hydrophilic and hydrophobic peptides by wild Lactococcus lactis strains isolated from raw ewes' milk cheese. Morales P, Fernández-García E, Gaya P, Medina M, Nuñez M. J Appl Microbiol; 2001 Nov 15; 91(5):907-15. PubMed ID: 11722669 [Abstract] [Full Text] [Related]
17. Peptides inhibitory to endopeptidase and aminopeptidase from Lactococcus lactis ssp. lactis MG1363, released from bovine beta-casein by chymosin, trypsin or chymotrypsin. Stepaniak L, Gobbetti M, Sørhaug T, Fox PF, Højrup P. Z Lebensm Unters Forsch; 1996 Apr 15; 202(4):329-33. PubMed ID: 8638436 [Abstract] [Full Text] [Related]
18. Reconstruction of the proteolytic pathway for use of beta-casein by Lactococcus lactis. Kunji ER, Fang G, Jeronimus-Stratingh CM, Bruins AP, Poolman B, Konings WN. Mol Microbiol; 1998 Mar 15; 27(6):1107-18. PubMed ID: 9570397 [Abstract] [Full Text] [Related]
19. The effects of adding lactococcal proteinase on the growth rate of Lactococcus lactis in milk depend on the type of enzyme. Helinck S, Richard J, Juillard V. Appl Environ Microbiol; 1997 Jun 15; 63(6):2124-30. PubMed ID: 9172328 [Abstract] [Full Text] [Related]
20. Involvement of enzyme-substrate charge interactions in the caseinolytic specificity of lactococcal cell envelope-associated proteinases. Reid JR, Coolbear T, Moore CH, Harding DR, Pritchard GG. Appl Environ Microbiol; 1995 Nov 15; 61(11):3934-9. PubMed ID: 8526506 [Abstract] [Full Text] [Related] Page: [Next] [New Search]