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

Authors:Fadda, Silvina
Sanz, Yolanda
Vignolo, Graciela
Oliver, Guillermo
Toldrá Vilardell, Fidel
Keywords:Lactobacillus plantarum, Myofibrillar protein hydrolysis, Proteinase activity, Aminopeptidase activity
Issue Date:Aug-1999
Publisher:American Society for Microbiology
Citation:Applied and Environmental Microbiology 65 (8) : 3540-3546 (1999)
Abstract:Strains of Lactobacillus plantarum originally isolated from sausages were screened for proteinase and aminopeptidase activities toward synthetic substrates; on the basis of that screening, L. plantarum CRT, 681 was selected for further assays on muscle proteins. The activities of whole cells, cell extracts (CE), and a combination of both on sarcoplasmic and myofibrillar protein extracts were determined by protein, peptide, and free-amino-acid analyses. Proteinase from whole cells initiated the hydrolysis of sarcoplasmic proteins. The addition of CE intensified the proteolysis. Whole cells generated hydrophilic peptides from both sarcoplasmic and myofibrillar proteins. Other peptides of a hydrophobic nature resulted from the combination of whole cells and CE, The action of both enzymatic sources on myofibrillar proteins caused maximal increases in lysine, arginine, and leucine, while the action of those on sarcoplasmic proteins mainly released alanine, In general, pronounced hydrolysis of muscle proteins required enzyme activities from whole cells in addition to those supplied by CE.
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