Proteolytic specificity of elastase on bovine alpha(s1)-casein

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Abstract

Proteases from polymorphonuclear leukocytes (PMN or neutrophils) and macrophages, the main somatic cells found in milk of healthy cows, may contribute to hydrolysis of caseins at neutral or acid pH in high somatic cell count milks. The objective of this study was to determine the cleavage specificity of elastase, one of the principal PMN proteinases, on α(s1)-casein. α(s1)-Casein (5 mg ml-1) was dissolved in phosphate buffer, pH 7.5, and elastase added. Samples were taken over a 24 h period and analyzed by urea polyacrylamide gel electrophoresis and high performance liquid chromatography. Twenty-five cleavage sites were identified showing that elastase had a broad cleavage specificity on α(s1)-casein. Copyright (C) 2000 Elsevier Science Ltd.

Original languageEnglish (Ireland)
Pages (from-to)19-26
Number of pages8
JournalFood Chemistry
Volume69
Issue number1
Publication statusPublished - Apr 2000

Keywords

  • α(s1)-Casein
  • Elastase
  • Somatic cells
  • Specificity

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