Hydrolytic activity of Penicillium chrysogenum Pg222 on pork myofibrillar proteins

Int J Food Microbiol. 2003 Dec 31;89(2-3):155-61. doi: 10.1016/s0168-1605(03)00117-x.

Abstract

Moulds grow on many different dry-cured meat products and are able to hydrolyse muscle proteins. However, their contribution to proteolysis in these products is not well known. Only recently, the ability of just a few strains of Penicillium spp. to increase proteolysis in dry-cured meat products has been shown. For these strains to be used as starter cultures, their hydrolytic activity under standard conditions should be characterised. With this purpose, the effect of Penicillium chrysogenum Pg222 on pork myofibrillar proteins has been assayed in a culture medium containing 5% (w/v) NaCl. SDS-PAGE revealed that Pg222 was responsible for extensive hydrolysis of the main myofibrillar proteins except alpha-actinin. The proteolysis led to increases in free amino acids, reaching peak values at 84 h. Ala, Tyr and Lys were present in the greatest amount. These results suggest that P. chrysogenum Pg222 would contribute to development of desired texture and flavours in dry-cured meat products.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Consumer Behavior
  • Food Microbiology
  • Humans
  • Hydrolysis*
  • Meat Products / microbiology*
  • Muscle Proteins / metabolism*
  • Penicillium chrysogenum / enzymology
  • Penicillium chrysogenum / metabolism*
  • Swine
  • Taste
  • Time Factors

Substances

  • Muscle Proteins