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All Journal Vegetalika Indonesian Journal of Biotechnology ASEAN Journal on Science and Technology for Development
Muhammad Saifur Rohman
Departemen Mikrobiologi, Fakultas Pertanian, Universitas Gadjah Mada
Agriculture, Biological Sciences & Forestry Biochemistry, Genetics & Molecular Biology Chemical Engineering, Chemistry & Bioengineering Computer Science & IT Immunology & microbiology Materials Science & Nanotechnology Mathematics

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Journal : Indonesian Journal of Biotechnology

 1 
Identification of Protease Producing Halophilic Bacteria from Bledug KuwuMud Volcano Muhammad Saifur Rohman; Irfan Dwidya Prijambada; Yohanna Anisa Indriyani; Heri Hendrosatriyo
Indonesian Journal of Biotechnology Vol 17, No 1 (2012)
Publisher : Universitas Gadjah Mada

Show Abstract | Download Original | Original Source | Check in Google Scholar | Full PDF (221.147 KB) | DOI: 10.22146/ijbiotech.15995

Abstract

The objective of this research was to isolate and identify the halophilic bacteria from Bledug Kuwu-mudvolacano having an ability to produce proteolytic enzyme. From this work, 6 bacterial isolates were obtainedfrom mud and water samples using artificial sea water media after incubation at room temperature. Threeout of the 6 isolates (BKL-3, BKL-5, and BKA-1) were selected for further analysis. BKL-3, BKL-5 and BKA-1exhibited an ability to grow at salt concentration greater than 10%. BKL-3 could grow on media supplementedwith 15% of salt, meanwhile BKL-5 and BKA-1 could grow at 20% of salt, respectively. Furthermore, thoseisolates also exhibited proteolytic activity when they were grown on casein media. The phylogenetic analysisbased on the 16SrRNA gene sequences showed that the BKL-3 belong to the group of Bacillaceae, whilst BKL-5and BKA-1 isolates were relatively distance from the group of Halomonadaceae. Therefore, BKL-5 and BKA-1could be considered as the allegedly new species that were separated from Halomonadaceae
The structural insight of class III of polyhydroxyalkanoate synthase from Bacillus sp. PSA10 as revealed by in silico analysis Listia Pradani; Muhammad Saifur Rohman; Sebastian Margino
Indonesian Journal of Biotechnology Vol 25, No 1 (2020)
Publisher : Universitas Gadjah Mada

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.22146/ijbiotech.53717

Abstract

PhaC synthase is an enzyme responsible for PHA polymerization. In this work, the catalytic mechanism class III of PhaC synthase from Bacillus sp. PSA10 (BacPhaCSynt) was reported through in silico modelling approach based on the primary sequence of the PhaC synthase. The open reading frame BacPhaCSynt has been successfully isolated, cloned and overexpressed the recombinant protein in Escherichia coli BL21(DE3). To know the global architecture and catalytic mechanism, the structural prediction of BacPhaCSynt has been carried out by using MODELLER. The recombinant BacPhaCSynt exhibited monomeric molecular weight (MW) of 43.6 kDa, when it was analyzed on 12% SDS‐PAGE gel. Based on the structural prediction, BacPhaCSynt exhibited global architecture of α/β hydrolase fold, with the root mean square deviation (r.m.s.d) value of 0.94Å. The catalytic residues composition of BacPhaCSynt consists of C151, D307, and H336, but the H336 and D307 residues of the model have been distorted 62.8o and 175.2o from the corresponding residues of the template. Since the D307 is quite a distance from the H336, it might act as a general base for the activation of ‐OH group of the substrate. The results strongly suggested that the mode of action of BacPhaCSynt obeyed the covalent catalysis mechanism.
Co-Authors Donny Widianto Dyah Weny Respatie Heri Hendrosatriyo Irfan Dwidya Prijambada JAKA WIDADA Listia Pradani Naoto Ogawa Sebastian Margino Sheila Ava Siti Subandiyah Tri Joko Yohanna Anisa Indriyani