Microbiology and Biotechnology Letters (한국미생물·생명공학회지)

The Korean Society for Microbiology and Biotechnology (한국미생물·생명공학회)
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The Purification and Properties of $\alpha$-Amylase from Schwanniomyces casrellii CBS 2863

Schwanniomyces castellii CBS 2863(ATCC 26077)으로부터 $\alpha$-Amylase 정제 및 특성

  • Park, Jong-Chun (Department of Biology, Chonnam National University) ;
  • Bai, Suk (Department of Microbiology, Chonnam National University) ;
  • Lim, Suhn-Young (Department of Microbiology, Chonnam National University) ;
  • Lee, Jin-Jong (Department of Biology, Chonnam National University) ;
  • Lee, Hyang (Department of Biology, Chonnam National University) ;
  • Chun, Soon-Bai (Department of Microbiology, Chonnam National University)
  • 박종천 (전남대학교 생물학과) ;
  • 배석 (전남대학교 미생물학과) ;
  • 임선영 (전남대학교 미생물학과) ;
  • 이진종 (전남대학교 생물학과) ;
  • 이향 (전남대학교 생물학과) ;
  • 전순배 (전남대학교 미생물학과)
  • Published : 1993.12.01
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Abstract

The extracellular alpha-amylase was purified to homogenity from the culture filtrate of starch grown Sch. castellii CBS 2863. The purified enzyme was glycoprotein with a molecular weight of about 56 kDa. The pH and temperature optimum were 5.5 and 40C, respectively. The enzyme was fairly stable up to 40C and at acid pH range (pH 4.0-7.0). The apparent Km and Vmax of the enzyme toward starch was 1.0mg/ml and 100U/mg protein, respectively. The analysis of amino acid composition was found to be acidic protein. The amino acid sequence of N-terminal peptide consisted of Asp-Val-Ser-Ser-Ala-X-X-Thr-Arg-Ser-Glu-Ser-Ile-Tyr.

Keywords

References

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