Hydrolysis of pork muscle sarcoplasmic proteins by Debaryomyces hansenii

Strains of Debaryomyces hansenii originally isolated from sausages were scr eened for proteinase and aminopeptidase activity towards synthetic substrat es. On the basis of these results, D. hansenii CT12487 was selected for fur ther assays. The activities of the whole cells (WC), cell-free extracts (CF E) and a combination of both from the selected strain on pork muscle sarcop lasmic protein extracts were determined by protein, peptide and free amino acid analyses. There was a pronounced hydrolysis of protein bands of 110 kD a and 27-64 kDa regardless the incorporation of WC, CFE or a combination of both. The proteolytic activity also resulted in the generation of polar an d non-polar peptides showing noticeable differences depending on the additi on of WC or CFE. Whole cells generated greater amounts of free amino acids than the cell-free extracts. (C) 2001 Elsevier Science B.V. All rights rese rved.