Record Details

Cloning, expression and characterization of L-arabinose isomerise from thermophilic Anoxybacillus kestanbolensis AC26Sari strain: Bioconversation of L-arabinose to L-ribulose

NOPR - NISCAIR Online Periodicals Repository

View Archive Info
 
 
Field Value
 
Title Cloning, expression and characterization of L-arabinose isomerise from thermophilic Anoxybacillus kestanbolensis AC26Sari strain: Bioconversation of L-arabinose to L-ribulose
 
Creator Ozer, Aysegul
Sal, Fulya Ay
Dalkıran, Nazan
Belduz, Ali Osman
Canakcı, Sabriye
 
Subject Biocatalysis
Microbial pentose phosphate pathway
 
Description 343-350
L-Arabinose isomerase (L-AI) is a pivotal enzyme in the microbial pentose phosphate pathway. It is considered as a
significant biological catalyst in rare sugar production. This enzyme can isomerize L-arabinose into L-ribulose and also
D-galactose into D-tagatose. Here, we cloned the araA gene encoding L-arabinose isomerase from Anoxybacillus
kestanbolensis AC26Sari strain, sequenced and over-expressed in E. coli BL21 (DE3): pLysS. This gene is involved in
L-arabinose operon in A. kestanbolensis AC26Sari. DNA sequence analysis revealed an open reading frame of 1,506 bp,
capable of encoding a polypeptide of 502 amino acid residues with calculated molecular weight of 55.6776 kDa. The
recombinant was purified by heat treatment and Ni-HisTaq chromatography. The purified enzyme showed maximal activity
at pH 8.5 and 65ºC and required divalent cations such as Co2+ and Mn2+ for its activity and thermostability. The apparent Km
value of the enzyme for L-arabinose was 6.5 mM (Vmax, 140.1002 U/mg) as determined in the precence of both 1 mM Co2+
and Mn2+.
 
Date 2022-05-02T11:09:52Z
2022-05-02T11:09:52Z
2022-05
 
Type Article
 
Identifier 0975-1009 (Online); 0019-5189 (Print)
http://nopr.niscair.res.in/handle/123456789/59637
 
Language en
 
Publisher NIScPR-CSIR, India
 
Source IJEB Vol.60(05) [May 2022]