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Molecular cloning, expression and characterization of α-amylase gene from a marine bacterium Pseudoalteromonas sp. MY-1

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Title Molecular cloning, expression and characterization of α-amylase gene from a marine bacterium Pseudoalteromonas sp. MY-1
 
Creator Tao, Xueying
Jang, Moon-Sun
Kim, Kyoung-Sook
 
Subject Pseudoalteromonas
α Amylase
Cloning
Characterization
 
Description 305-309
A gene (amyA) encoding an extracellular α-amylase from a marine bacterium Pseudoalteromonas sp. MY-1 was
cloned and expressed in Escherichia coli. It comprised an open-reading-frame of 2,007 base pairs and encoded a protein of
669 amino acids with a predicted molecular weight of 73,770 daltons and a pI of 5.15. The entire amino acid sequence of
amyA gene showed 86% similarity to the α-amylase preproprotein from Pseudoalteromonas haloplanktis. It consisted of a
signal peptide, α-amylase catalytic domain and an amy C domain. The recombinant amylase was purified to homogeneity
and biochemically characterized. The enzyme revealed maximum activity at pH 7.0 and 40ºC. The enzyme hydrolyzed
soluble starch and some maltooligosaccharides to several oligosaccharides, and maltose was the common product from
different substrates.
 
Date 2008-11-06T04:09:01Z
2008-11-06T04:09:01Z
2008-10
 
Type Article
 
Identifier 0301-1208
http://hdl.handle.net/123456789/2371
 
Language en_US
 
Publisher CSIR
 
Source IJBB Vol.45(5) [October 2008]