Recombinant .beta.-amylase

Chemistry: molecular biology and microbiology – Enzyme – proenzyme; compositions thereof; process for... – Hydrolase

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435 95, 4351721, 435275, C12N 924, C12N 1500, C12P 1922, C08B 3004

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active

058637842

ABSTRACT:
A recombinant .beta.-amylase which is superior to the original recombinant .beta.-amylase in thermostability has been obtained by a site-directed mutagenesis with the recombinant .beta.-amylase gene coding 531 amino acid residues. Substitutions were MET.sub.181 of said enzyme with Leu, Ser.sub.291 with Ala, Ile.sub.293 with Val, Ser.sub.346 with Pro, Ser.sub.347 with Pro, Gln.sub.348, with Asp and Ala.sub.372 with Ser.

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Oyo Toshitsu kagaku, vol. 41, No. 2, pp. 261-271, 1994, Naohiro Yoshigi et al., "Structure of Barley B-amylase and Expression in Escherichia Coli of cDNA".
Eur. J. Biochem., vol. 169, pp. 517-525, 1987, Martin Kreis et al., "Primary Structure and Differential Expression of B-amylase in Normal and Mutant Barleys".
Biosci. Biotech. Biochem, vol. 58, No. 6, pp. 1080-1086, 1994, Naohiro Yoshigi et al., "Expression in Escherichia Coli of cDNA Encoding Barley B-amylase and Properties of Recombinant B-amylase".
J. Biochem., vol. 115, pp. 47-51, 1994, Naohiro Yoshigi et al., "PCR Cloning and Sequencing of the B-amylase cDNA from Barley".
J. Biochem., vol. 118, pp. 562-567, 1995, Naohiro Yoshigi et al., "Construction of a Plasmid Used for the Expression of a Sevenfold-Mutant Barley B-amylase with Increased Thermostability in Escherichia Coli and Properties of the Sevenfold-Mutant B-amylase".

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