Purification and characterization of three amylases from viscera of hard clam Meretrix lusoria View Full Text


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Article Info

DATE

2004-02

AUTHORS

Ching‐Yu TSAO, Yen‐Hsin HSU, Li‐Min CHAO, Shann‐Tzong JIANG

ABSTRACT

ABSTRACT: Three amylases were purified to electrophoretic homogeneity from viscera of hard clam Meretrix lusoria by ammonium sulfate fractionation, Sepharose 6B, DEAE-Sephadex A-50, Sephadex G-200 and PBE 94 chromatographies. The purified amylases had molecular masses of 49.6, 58.7 and 100 kDa and were designated AI-1, AI-2 and AII, respectively. Both AI-1 and AI-2 could digest amylose into glucose and maltose, while AII could digest amylose and pullulan into glucose. The optimal pH and temperatures for AI-1, AI-2 and AII were 7.0, 7.5 and 7.5, and 40, 50 and 50°C, respectively. According to the substrate specificity, the purified AI-1 and AI-2 were considered to be multifunctional exo- and endo-types of α-amylase-like enzymes, while AII was exo-type γ-amylase-like enzyme. They were Ca2+-independent enzymes. More... »

PAGES

174-182

References to SciGraph publications

  • 1991. Enzymatic Depolymerization of Starch in BIOCATALYSTS FOR INDUSTRY
  • 1985-01. Bacillus stearothermophilus KP 1064 pullulan hydrolase in APPLIED MICROBIOLOGY AND BIOTECHNOLOGY
  • 1991. Biocatalysts for Industry in NONE
  • 1992-12. Purification of α-amylase from Bacillus lentus cultures in APPLIED MICROBIOLOGY AND BIOTECHNOLOGY
  • Identifiers

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    http://scigraph.springernature.com/pub.10.1111/j.1444-2906.2003.00786.x

    DOI

    http://dx.doi.org/10.1111/j.1444-2906.2003.00786.x

    DIMENSIONS

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