Sumardi, Sumardi and christina, Nugroho Ekowati and rismayanti, rismayanti (2019) THE ACTIVITY ASSAY OF PROTEASE, CELLULASE, AMYLASE, XYLANASE AND MANNANASE FROM BACILLUS SP. AS A CANDIDATE OF PROBIOTICS. World Journal of Pharmaceutical and Life Sciences, 5 (3). pp. 88-93. ISSN 2454-2229

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Abstract

The purpose of this study was determineted the potential for five strains of Bacillus sp. KPP212, Bacillus sp IP121, Bacillus sp UJ131, Bacillus sp UJ132, and Bacillus sp SB141 isolated from the mangrove forest ecosystem. The bacteria were selected to produce hydrolase enzymes (proteases, cellulases, amylases, xylanases, and mannanase s). Enzyme production was also carried out on production media with shrimp and fish feed as main substrate. The method consisted of assay of selection and enzyme activity. The data analyzed descriptively. The research showed there are four strains that produce protease and xylanase enzyme namely Bacillus sp. KPP212, Bacillus sp. IP121, Bacillus sp. UJ131, and Bacillus sp. UJ132. The highest protease enzyme activity is Bacillus sp UJ131 i.e. 0.07 U ml-1. The highest xylanase enzyme is Bacillus sp UJ131 i.e. 0.05 U ml-1. Bacillus sp. UJ132 is a bacteria that produced three kind of enzyme with the highest cellulase activity of 0.06 U ml-1. The five bacteria did not produce amylase and mannanase. The production of enzyme from shrimp feeds medium yielded protease activity of 0.05 U ml-1, xylanase activity of 0.2 U ml-1, and cellulase activity of 0.07 U ml-1. While, enzyme activity from fish feeds medium as follows: protease: 0.08 U ml-1 xylanase: 0.31 U ml-1; cellulase: 0.15 U ml-1. While, production of enzyme from fish feeds medium yielded protease activity i.e. 0.08 U ml-1; xylanase activity i.e. 0.31 U ml-1; and cellulase activity i.e. 0.15 U ml-1

Item Type: Article
Subjects: Q Science > QR Microbiology
Divisions: Fakultas Matematika dan Ilmu Pengetahuan Alam (FMIPA) > Prodi Magister Ilmu Biologi
Depositing User: Sumardi Sumardi
Date Deposited: 09 Apr 2019 02:25
Last Modified: 09 Apr 2019 02:25
URI: http://repository.lppm.unila.ac.id/id/eprint/11105

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