Abstract
The gene encoding a novel alkaline pectate lyase (Apel) from Bacillus subtilis was cloned and expressed in B. subtilis WB600. Apel contained an ORF of 1,260 bp, encoding a signal peptide of 21 amino acids and a mature protein of 399 amino acids with a calculated molecular mass of 45497.9 Da. The mature Apel was structurally related to the enzymes in the polysaccharide lyase family 1. After purification, the recombinant Apel had a specific activity of 445 U mg(-1). The enzyme was optimally active at 50°C and pH 9.
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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Bacillus subtilis / enzymology*
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Bacillus subtilis / genetics
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Cloning, Molecular
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DNA, Bacterial / chemistry
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DNA, Bacterial / genetics
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Enzyme Stability
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Gene Expression
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Hydrogen-Ion Concentration
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Models, Molecular
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Molecular Sequence Data
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Molecular Weight
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Open Reading Frames
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Polysaccharide-Lyases / chemistry
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Polysaccharide-Lyases / genetics
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Polysaccharide-Lyases / metabolism*
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Protein Sorting Signals
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Protein Structure, Tertiary
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Recombinant Proteins / chemistry
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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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Sequence Analysis, DNA
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Temperature
Substances
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DNA, Bacterial
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Protein Sorting Signals
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Recombinant Proteins
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Polysaccharide-Lyases
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pectate lyase