Angiotensin I‐converting‐enzyme‐inhibitory and antimicrobial bioactive peptides

Angiotensin I‐converting‐enzyme‐inhibitory and antimicrobial bioactive peptides Bioactivities of peptides encrypted in major milk proteins are latent until they are released and activated by enzymatic proteolysis. After a brief description of the properties of some bioactive peptides, an overview of the angiotensin I‐converting‐enzyme (ACE)‐inhibitory and antimicrobial peptides is given. Emphasis is on the capacity of lactic acid bacteria to generate ACE‐inhibitory peptides and on the exploitation of the potential role of antimicrobial peptides derived from milk proteins. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png International Journal of Dairy Technology Wiley

Angiotensin I‐converting‐enzyme‐inhibitory and antimicrobial bioactive peptides

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Publisher
Wiley
Copyright
Copyright © 2004 Wiley Subscription Services, Inc., A Wiley Company
ISSN
1364-727X
eISSN
1471-0307
D.O.I.
10.1111/j.1471-0307.2004.00139.x
Publisher site
See Article on Publisher Site

Abstract

Bioactivities of peptides encrypted in major milk proteins are latent until they are released and activated by enzymatic proteolysis. After a brief description of the properties of some bioactive peptides, an overview of the angiotensin I‐converting‐enzyme (ACE)‐inhibitory and antimicrobial peptides is given. Emphasis is on the capacity of lactic acid bacteria to generate ACE‐inhibitory peptides and on the exploitation of the potential role of antimicrobial peptides derived from milk proteins.

Journal

International Journal of Dairy TechnologyWiley

Published: May 1, 2004

References

  • Combinatorial libraries: a tool to design antimicrobial and antifungal peptide analogues having lytic specificities for structure–activity relationship studies
    Blondelle, Blondelle; Lohner, Lohner
  • Diversity of antimicrobial peptides and their mechanisms of action
    Epand, Epand; Vogel, Vogel
  • Potential uses of caseinophosphopeptides
    FitzGerald, FitzGerald
  • Cationic peptides: a new source of antibiotics
    Hancock, Hancock; Leher, Leher
  • The bacterial growth inhibitor (lactenin) of milk
    Jones, Jones; Simms, Simms
  • Estimation of calcium‐binding constants of casein phosphopeptides by capillary zone electrophoresis
    Meisel, Meisel; Olieman, Olieman
  • Angiotensin converting enzyme inhibitors: medicinal chemistry and biological actions
    Petrillo, Petrillo; Ondetti, Ondetti
  • Angiotensin I converting enzyme inhibitory peptides from bovine milk proteins
    Pihlanto‐Leppälä, Pihlanto‐Leppälä; Rokka, Rokka; Korhonen, Korhonen
  • Isolation and characterization of sheep lactoferrin, in an inhibitor of platelet aggregation and comparison with human lactoferrin
    Quian, Quian; Jollès, Jollès; Migliore‐Samour, Migliore‐Samour; Fiat, Fiat
  • Antibacterial and binding characteristics of bovine, ovine and caprine lactoferrins: a comparative study
    Recio, Recio; Visser, Visser
  • A new type of ripened, low‐fat cheese with bioactive properties
    Ryhänen, Ryhänen; Pihlanto‐Leppala, Pihlanto‐Leppala; Pahkala, Pahkala
  • Milk‐borne bioactive peptides
    Schanbacher, Schanbacher; Talhouk, Talhouk; Murray, Murray; Gherman, Gherman; Willet, Willet
  • Peptides from several Italian cheeses inhibitory to proteolytic enzymes of lactic acid bacteria, Pseudomonas fluorescens ATCC 948 and to the angiotensin I‐converting enzyme
    Smacchi, Smacchi; Gobbetti, Gobbetti
  • Antihypertensive peptides derived from food proteins
    Yamamoto, Yamamoto

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