Proteolytic enzyme activities of whole cells and cell free extracts (CFE) o
f Lactobacillus curvatus CECT 904 and Lactobacillus sake CECT 4808 were cha
racterised using synthetic chromogenic compounds and myofibrillar proteins
as substrates. The hydrolytic action was monitored by SDS-PAGE and reverse
phase-HPLC analyses. The CFE of L. sake partially contributed, together wit
h muscle enzymes, to the initial hydrolysis of myofibrillar proteins. Whole
-cells of both L. curvatus and L. sake generated peptides considered import
ant for cured-meat taste. The peptide mapping, resulting from the action on
the substrates assayed, revealed a profile of extra and intracellular enzy
mes. Both strains expressed strong amino acid metabolism. (C) 1999 Elsevier
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