Purification and characterization of a X-prolyl-dipeptidyl peptidase from Lactobacillus sakei

Article Abstract:

A peptidase from the meat fermentative organism Lactobacillus sakei that can hydrolyze proline peptide bonds is described. It almost exclusively hydrolyzes X-Pro from the N terminus of the peptide.

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Hydrolysis of pork muscle sarcoplasmic proteins by Lactobacillus curvatus and Lactobacillus sake

Article Abstract:

Research was conducted to examine the hydrolysis of pork muscle sarcoplasmic proteins by Lactobacillus curvatus and Lactobacillus sake. The objective is to determine the proteolytic activities of various enzyme combinations from L. curvatus and L. sake strains on sarcoplasmic proteins to predict their suitability and their proteolytic enzymes as starter cultures or additives, respectively, for the processing of dry fermented sausages. Results suggest that the differences in proteolytic activities may result in distinct flavor profiles for final products.

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Characterization of muscle sarcoplasmic and myofibrillar protein hydrolysis caused by Lactobacillus plantarum

Article Abstract:

Proteinases from Lactobacillus plantarum release lysine, arginine, and leucine when hydrolyzing myofibrillar proteins but release alanine when hydrolyzing sarcoplasmic proteins. This bacterium is used to cure sausages, and manipulating the starter culture can affect the taste and aroma of the finished product.

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