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All Journal Biodiversitas Journal of Biological Diversity
ELFI SUSANTI VH
Program Studi Kimia Jurusan PMIPA FKIP Universitas Sebelas Maret Surakarta 57126
Agriculture, Biological Sciences & Forestry Biochemistry, Genetics & Molecular Biology

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Genom Gene Cloning of Penicillin V Acylase from Bacillus sp BAC4 by Genomic Library ELFI SUSANTI VH; SRI RETNO DWI ARIANI
Biodiversitas Journal of Biological Diversity Vol. 5 No. 1 (2004)
Publisher : Society for Indonesian Biodiversity

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.13057/biodiv/d050101

Abstract

This research was aimed to clone and identify penicillin V acylase (PVA) gene of Bacillus sp. BAC4 by genomic library.Chromosome DNA of Bacillus sp. BAC4 was isolated by Wang method. pHB201 of E. coli was isolated by alkali lyses method. Recombinant DNA of Bacillus sp. BAC4 chromosome fragment and pHB201 was made by ligase process using T4 DNA ligase. Transformation of E. coli using this recombinant plasmid was carried out according to Mandel-Higa method. The results indicated that chromosome DNA fragment of Bacillus sp. BAC4 was bigger 23 kb with purity 1,3. Plasmid DNA fragment of E coli was 6,5 kb. Transformants laboring pHB201 recombinant plasmid was screen as blue-white colonies in a medium containing IPTG/X-gal and chloramphenicol. 2004 Jurusan Biologi FMIPA UNS SurakartaKey words: genomic library, penicillin acylase, transformation, plasmid, chromosome
Isolation and characterization of protease from Bacillus subtilis 1012M15 ELFI SUSANTI VH
Biodiversitas Journal of Biological Diversity Vol. 4 No. 1 (2003)
Publisher : Society for Indonesian Biodiversity

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.13057/biodiv/d040103

Abstract

A local strain of Bacillus sp. BAC4, is known to produce penicillin G acylase (PGA) enzyme with relatively high activity. This strain secretes the PGA into the culture medium. However, it has been reported that PGA activity fall and rise during culture, and the activity plummets during storege at –200C, which probably due to usage protease activity of Bacillus sp. BAC4. To study the possible use of Bacillus subtilis 1012M15 as a host cell for cloning the pga gene from Bacillus sp. BAC4, the protease activity of Bacillus subtilis 1012M15 were studied. Protease activity was determined by Horikoshi method. In this experiment, maximum protease activity in Bacillus subtilis 1012M15 culture was obsereved after 8 hours. At this optimum condition, protease activity of Bacillus sp. BAC4 is five time higher than that of Bacillus subtilis 1012M15. This situation promised the possible usage of Bacillus subtilis 1012M15 as a host cell for pga expression. For protease characterization, the bacterial culture had been separated from the cell debris by centrifugation. The filtrate was concentrated by freeze drying, fractionated by ammonium sulphate, dialyzed in selovan tube, and then fractionated by ion exchance chromatography employing DEAE-cellulose. The five peaks resulted indicated the presence of five protease. Based on inhibitor and activator influence analysis, it could be concluded that proteases from Bacillus subtilis 1012M15 contained of serin protease as well as metalloprotease and serin protease mixture.© 2003 Jurusan Biologi FMIPA UNS SurakartaKey words: protease, penicillin G acylase, cloning, host cell.
Co-Authors SRI RETNO DWI ARIANI