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All Journal Indonesian Journal of Chemistry
Tri Joko Raharjo
Department of Chemistry, Faculty of Mathematics and Natural Sciences, Universitas Gadjah Mada, Sekip Utara BLS 21, Bulaksumur, Yogyakarta 55281, Indonesia
Chemical Engineering, Chemistry & Bioengineering Chemistry

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Three Dimensional Structural Modelling of Lipase Encoding Gene from Soil Bacterium Alcaligenes sp. JG3 Using Automated Protein Homology Analysis Dilin Rahayu Nataningtyas; Tri Joko Raharjo; Endang Astuti
Indonesian Journal of Chemistry Vol 19, No 3 (2019)
Publisher : Universitas Gadjah Mada

Show Abstract | Download Original | Original Source | Check in Google Scholar | Full PDF (14.741 KB) | DOI: 10.22146/ijc.34152

Abstract

Bacterial lipases have significant potential to be used as the biocatalyst for many chemical reactions. In this study, a novel gene encoding lipase was isolated from an Alcaligenes sp. JG3. A pair of designed primer has successfully isolated 1 kb (LipJG3) that shares 98% identity towards lipase from Alcaligenes faecalis during sequence analysis. By using in silico tools, LipJG3 was related to the transporter protein sequences. Three highly conserved regions consisting of EASGSKT, VILLD, and LSGGQQQRVAIA were found. These regions were known as ATP-binding signature at Walker-A and Walker-B motifs and the S signature of ABC transporter family respectively. In addition, the 3-D structure of LipJG3 has been suggested but the role of the catalytic triad residues have been not fully understood.
Overexpression of Lipase Gene from Alcaligenes sp. JG3 and its Activity toward Hydrolysis Reaction Norman Yoshi Haryono; Winarto Haryadi; Tri Joko Raharjo
Indonesian Journal of Chemistry Vol 20, No 1 (2020)
Publisher : Universitas Gadjah Mada

Show Abstract | Download Original | Original Source | Check in Google Scholar | Full PDF (657.531 KB) | DOI: 10.22146/ijc.45663

Abstract

Bacterial lipase holds an important role as a new source for many industrial catalysts. The investigation and understanding of the lipase-encoding gene become apparent as the key step for generating high-quality lipase as biocatalyst for many chemical reactions. In this study, bacterial lipase from Alcaligenes sp. JG3 was produced via overexpression gene method. This specific lipase was successfully overexpressed using pQE-30 vector and E. coli M15[pREP4] as host, producing His-tagged protein sized 46 kDa and was able to hydrolyze triacylglycerol from olive oil with the calculated unit activity and specific activity of 0.012 U and 1.175 U/mg respectively. The in silico investigation towards lipase JG3 revealed that it was categorized as ABC transporter protein as opposed to the conventional hydrolase family. Lastly, amino acid sequences SGSGKTT from lipase JG3 was highly conserved sequences and was predicted as the ATP-binding site but the catalytic triad of serine, histidine, and aspartate has not been solved yet.
Co-Authors Dilin Rahayu Nataningtyas Endang Astuti Norman Yoshi Haryono Winarto Haryadi