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        Gelatinolytic Enzymes from Bacillus amyloliquefaciens Isolated from Fish Docks: Characteristics and Hydrolytic Activity

        Samart Sai-Ut,Soottawat Benjakul,Punnanee Sumpavapol 한국식품과학회 2013 Food Science and Biotechnology Vol.22 No.4

        Fifty-five bacteria with gelatinolytic activity were screened from over 500 isolates obtained from fishing docks in Songkhla, Thailand. Based on 16S rRNA gene sequence analysis, 3 selected strains (K12, O02, and S13)were identified as Bacillus cereus with 99.8% similarity. Three other stains (D10, G02, and H11) were identified as Bacillus amyloliquefaciens with 99.7% similarity. Gelatinolytic enzymes of the D10, G02, and H11 strains were precipitated using ammonium sulfate precipitation, followed by dialysis with an increase in purity between 19-34-fold. Maximal gelatinolytic activities towards fish gelatin were attained at 50oC and pH 7.5. Metallo- and serine-gelatinolytic enzymes were dominant for all 3 strains. All gelatinolytic enzymes showed similar hydrolysis towards fish gelatin to commercial Alcalase, but higher hydrolysis was found in the formers within the first 60 min. Therefore, gelatinolytic enzymes from selected B. amyloliquefaciens strains can be used for production of fish gelatin hydrolysate.

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