Abstract
A gene (acas) designated as alpha-amylase was cloned from Arthrobacter chlorophenolicus A6. The multiple amino acid sequence analysis and functional expression of acas revealed that this gene really encoded an amylosucrase (ASase) instead of alpha-amylase. In fact, the recombinant enzyme exhibited typical ASase activity by showing both sucrose hydrolysis and glucosyltransferase activities. The purified enzyme has a molecular mass of 72 kDa and exhibits optimal hydrolysis activity at 45 degrees C and a pH of 8.0. The analysis of the oligomeric state of ACAS with gel permeation chromatography revealed that the ACAS existed as a monomer.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Arthrobacter / enzymology*
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Arthrobacter / genetics
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Bacterial Proteins / biosynthesis*
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Bacterial Proteins / genetics
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Bacterial Proteins / isolation & purification
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Escherichia coli / enzymology
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Escherichia coli / genetics
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Glucosyltransferases / biosynthesis*
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Glucosyltransferases / genetics
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Glucosyltransferases / isolation & purification
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Molecular Sequence Data
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Recombinant Proteins / genetics
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Recombinant Proteins / isolation & purification
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Recombinant Proteins / metabolism*
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Sequence Alignment
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Sucrose / metabolism
Substances
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Bacterial Proteins
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Recombinant Proteins
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Sucrose
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Glucosyltransferases
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amylosucrase