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. 1988 Sep 15;254(3):835–840. doi: 10.1042/bj2540835

Purification and characterization of a novel thermostable beta-amylase from Clostridium thermosulphurogenes.

G J Shen 1, B C Saha 1, Y E Lee 1, L Bhatnagar 1, J G Zeikus 1
PMCID: PMC1135158  PMID: 2461701

Abstract

An extracellular beta-amylase from Clostridium thermosulphurogenes was purified 811-fold to homogeneity, and its general molecular, physico-chemical and catalytic properties were determined. The native enzyme was a tetramer of 210 kDa composed of a single type subunit; its 20 amino acid N-terminus displayed 45% homology with Bacillus polymyxa beta-amylase. The beta-amylase was enriched in both acidic and hydrophobic amino acids. The pure enzyme displayed an isoelectric point of 5.1 and a pH activity optimum of 5.5. The optimum temperature for beta-amylase activity was 75 degrees C, and enzyme thermostability at 80 degrees C was enhanced by substrate and Ca2+ addition. The beta-amylase hydrolysed amylose to maltose and amylopectin and glycogen to maltose and limit dextrins, and it was inhibited by alpha- and beta-cyclodextrins. The enzyme displayed kcat. and Km values for boiled soluble starch of 400,000 min-1 per mol and 1.68 mg/ml, respectively. The enzyme was antigenically distinct from plant beta-amylases.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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