SARCOPLASMIC PROTEIN HYDROLYSIS ACTIVITY OFrnLACTOBACILLUS PLANTARUM 120 ISOLATED FROM SUANYU:rnA TRADITIONAL CHINESE LOW SALT FERMENTED FISH

摘要

The hydrolysis of sarcoplasmic proteins during the growth of Lactobacillus plantarumrn120 originally isolated from Suanyu, a traditional Chinese low salt fermentedrnfish, was evaluated. Fermentation was carried out in a fish meat model system atrn30C for 96 h. Proteolytic activity of this strain on fish muscle sarcoplasmic proteinrnwas determined by proteins, peptides and free amino acids analyses. There was arnpronounced hydrolysis of almost all protein bands in electrophoretic pattern by L.rnplantarum 120. It also resulted in the generation of new peptides and disappearancernof original peaks. In addition, the studied strain generated greater amountsrnof free amino acids than the control, especially for alanine, glutamic acid, phenylalanine,rnvaline, methionine, aspartic acid, isoleucine and leucine. In general, proteolysisrnof fish sarcoplasmic proteins by L. plantarum 120 occurred duringrnfermentation, resulting in increase in peptides and free amino acids, which mayrncontribute to the taste and aroma of Suanyu.