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All Journal ANNALES BOGORIENSES
Puspita Suci Wulandari
Carbohydrate and Bioengineering Research Group Research Center for Biotechnology, Indonesian Institute of Sciences (LIPI), Indonesia
Agriculture, Biological Sciences & Forestry Biochemistry, Genetics & Molecular Biology Chemical Engineering, Chemistry & Bioengineering Chemistry Immunology & microbiology Medicine & Pharmacology

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Site-Directed Mutagenesis of Glu-269 L-Arabinose Isomerase from Geobacillus stearothermophilus Isolated from Tanjung Api Poso, Indonesia Dewi Fitriani Fitriani; Puspita Suci Wulandari; Budi Saksono
ANNALES BOGORIENSES Vol 14, No 2 (2010): Annales Bogorienses
Publisher : Research Center for Biotechnology - Indonesian Institute of Sciences (LIPI)

Show Abstract | Download Original | Original Source | Check in Google Scholar | Full PDF (600.974 KB) | DOI: 10.14203/ann.bogor.2010.v14.n2.33-37

Abstract

Industrializing of tagatose requires enzymes that meet to industrial need such as thermophile, slightly acidic and metal independent.  Previously,  we  cloned,  sequenced  and  expressed  L-arabinose  isomerase  from  Geobacillus stearothermophilus  isolated  from Tanjung  Api, Poso, Indonesia. Based on DNA alignment analysis, the gene had  high  homology  with  those  of  G.  stearothermophilus  T6  (Gene  Bank  Acc  No:  AAD45718)  which  has optimum  activity  at  high  temperature  and  alkaline  condition.  In  this  p aper,  we  described  site-directed mutagenesis approach to mutate Glu-269 (Q269) to Lys-269 (K269) to decrease the optimum pH of the strain. Sequencing  result  showed  that  mutagenesis  had  been  successful  to  mutate  amino  acid  at  position  269  from glutamine (Q) into lysine (K). Expression of mutant Q269 showed protein with molecular mass ~56 kDa. Keywords: site-directed mutagenesis, Q269K, L-arabinose isomerase, Geobacillus stearothermophilus
Co-Authors Budi Saksono Dewi Fitriani Fitriani