Casein utilization by lactococci

Smid, Ej; Poolman, Berend; Konings, Wn

doi:10.1128/aem.57.9.2447-2452.1991

Cited by 104 publications

(35 citation statements)

References 35 publications

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“…Some of the orally administered ACEI peptides have demonstrated strong antihypertensive effects in SHR (Table 1). Lactic acid bacteria have proteolytic systems that can hydrolyze milk protein and have been reported to utilize the peptides released from the milk protein casein (25)(26)(27). Among lactic acid bacteria, Lactobacillus helveticus had the highest extracellular proteinase activity and the ability to release the largest amount of peptides in the fermented milk ( Table 2).…”

Section: Ace Inhibitory Peptides From Milk Proteinsmentioning

confidence: 99%

“…The first step in casein decomposition is typically caused by an extracellular proteinase, and further digestion to amino acids is catalyzed by many kinds of intracellular peptidases (25,36). Among the lactic acid bacteria, L. helveticus has the highest extracellular proteinase activity and the ability to release the highest amount of peptides in fermented milk ( Table 2).…”

Section: Processing By a Cell Wall-associated Proteinasementioning

confidence: 99%

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Antihypertensive Peptides Specific to Lactobacillus helveticus Fermented Milk

Wakai¹,

Yamamoto²

2012

Biotechnology - Molecular Studies and Novel Applications for Improved Quality of Human Life

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Japan L. helveticus CP209 J 45 kDa 45 kDa A 4 L. helveticus CP210 J 45 kDa 45 kDa A 5 L. helveticus CP293 J 45 kDa 45 kDa A 6 L. helveticus CP510 J 45 kDa 45 kDa A 7 L. helveticus CP611 J 45 kDa 45 kDa A 8 L. helveticus CP615 J 45 kDa 45 kDa A 9 L. helveticus CP617 J 45 kDa 45 kDa A 10 L. helveticus CP789 J 45 kDa 45 kDa A 11 L. helveticus CP790 J 45 kDa 45 kDa A 12 L. helveticus JCM1004 H ND 53, 170 kDa B 13 L. helveticus JCM1006 J 45 kDa 45 kDa A 14 L. helveticus JCM1007 J ND 53, 170 kDa B 15 L. helveticus JCM1062 J ND 53, 170 kDa B 16 L. helveticus JCM1103 H ND 53, 170 kDa B 17 L. helveticus JCM1120

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Section: Ace Inhibitory Peptides From Milk Proteinsmentioning

confidence: 99%

Section: Processing By a Cell Wall-associated Proteinasementioning

confidence: 99%

Antihypertensive Peptides Specific to Lactobacillus helveticus Fermented Milk

Wakai¹,

Yamamoto²

2012

Biotechnology - Molecular Studies and Novel Applications for Improved Quality of Human Life

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“…The casein degradation pathway is initiated by a cell wallbound serine protease called PrtP or CEP (192,744). The prtP gene has been cloned and sequenced in a number of L. lactis strains (155,429,439), and each displays Ͼ95% homology to the other prtP genes.…”

Section: Lactococcimentioning

confidence: 99%

Surface Proteins of Gram-Positive Bacteria and Mechanisms of Their Targeting to the Cell Wall Envelope

Navarre

Schneewind

1999

Microbiol Mol Biol Rev

1,192

601

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SUMMARY The cell wall envelope of gram-positive bacteria is a macromolecular, exoskeletal organelle that is assembled and turned over at designated sites. The cell wall also functions as a surface organelle that allows gram-positive pathogens to interact with their environment, in particular the tissues of the infected host. All of these functions require that surface proteins and enzymes be properly targeted to the cell wall envelope. Two basic mechanisms, cell wall sorting and targeting, have been identified. Cell well sorting is the covalent attachment of surface proteins to the peptidoglycan via a C-terminal sorting signal that contains a consensus LPXTG sequence. More than 100 proteins that possess cell wall-sorting signals, including the M proteins of Streptococcus pyogenes, protein A of Staphylococcus aureus, and several internalins of Listeria monocytogenes, have been identified. Cell wall targeting involves the noncovalent attachment of proteins to the cell surface via specialized binding domains. Several of these wall-binding domains appear to interact with secondary wall polymers that are associated with the peptidoglycan, for example teichoic acids and polysaccharides. Proteins that are targeted to the cell surface include muralytic enzymes such as autolysins, lysostaphin, and phage lytic enzymes. Other examples for targeted proteins are the surface S-layer proteins of bacilli and clostridia, as well as virulence factors required for the pathogenesis of L. monocytogenes (internalin B) and Streptococcus pneumoniae (PspA) infections. In this review we describe the mechanisms for both sorting and targeting of proteins to the envelope of gram-positive bacteria and review the functions of known surface proteins.

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“…The proteolytic systems of LAB have received a great deal of attention over the past decade, due to the well documented role of proteolysis in cheese flavor and texture development [1]. Also, since insufficient free amino acids are present in milk to support growth to high cell density, these bacteria require a complex proteolytic system to obtain essential amino acids from casein [2].…”

Section: Introductionmentioning

confidence: 99%