Extracellular thermostable alpha-amylase from Bacillus stearothermophilus Q8

H. Y. Lin, S. S. Tsay

Research output: Contribution to journalArticle

Abstract

The alpha-amylase of Bacillus stearothermophilus Q8, previously isolated in our laboratory, was purified by ammonium sulfate precipitation and CM-sephadex chromatography. The activity the of partial purified alpha-amylase was to be protected by bovine serum albumin Ca2+ and Mg2+. The enzyme showed 100% activity at pH 9.0; 98%, at pH 8.0 and 41%; at pH 10.0. It expressed optimal reaction temperature at 90 degrees C, 81% of the activities remained at 100 degrees C. After 15 min incubation at 100 degrees C with the addition of 10 mM Ca2+, the enzyme only retained 67% activity. The enzyme, however, retained 10% of the maximal activity after 2 h incubation at 90 degrees C, in the absence of substrate and with the addition of Ca2+. Of cations, Na+ at 0.1 and 1 mM, Mn2+ at 0.1 mM showed stimulatory effect; of anions OH-Cl-I-HCO3-NO2-N3- at 10 mM showed stimulatory effect. Addition of urea and KMnO4 resulted in the loss of enzyme activities; however, lower concentration of SDS and Tween 80 afforded protection of the enzyme activities. Galactose and maltose were non-inhibitory for the enzyme activities, while, fructose, mannose, xylose and lactose were slightly inhibitory. The relative hydrolysis sequence of polysaccharides were amylose greater than soluble starch = corn starch greater than glycogen.

Original languageEnglish
Pages (from-to)327-338
Number of pages12
JournalZhonghua Minguo wei sheng wu ji mian yi xue za zhi = Chinese journal of microbiology and immunology
Volume20
Issue number4
Publication statusPublished - Jan 1 1987
Externally publishedYes

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Geobacillus stearothermophilus
alpha-Amylases
Enzymes
Starch
Amylose
Maltose
Polysorbates
Xylose
Ammonium Sulfate
Lactose
Mannose
Bovine Serum Albumin
Fructose
Glycogen
Galactose
Zea mays
Anions
Polysaccharides
Urea
Cations

ASJC Scopus subject areas

  • Medicine(all)

Cite this

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title = "Extracellular thermostable alpha-amylase from Bacillus stearothermophilus Q8",
abstract = "The alpha-amylase of Bacillus stearothermophilus Q8, previously isolated in our laboratory, was purified by ammonium sulfate precipitation and CM-sephadex chromatography. The activity the of partial purified alpha-amylase was to be protected by bovine serum albumin Ca2+ and Mg2+. The enzyme showed 100{\%} activity at pH 9.0; 98{\%}, at pH 8.0 and 41{\%}; at pH 10.0. It expressed optimal reaction temperature at 90 degrees C, 81{\%} of the activities remained at 100 degrees C. After 15 min incubation at 100 degrees C with the addition of 10 mM Ca2+, the enzyme only retained 67{\%} activity. The enzyme, however, retained 10{\%} of the maximal activity after 2 h incubation at 90 degrees C, in the absence of substrate and with the addition of Ca2+. Of cations, Na+ at 0.1 and 1 mM, Mn2+ at 0.1 mM showed stimulatory effect; of anions OH-Cl-I-HCO3-NO2-N3- at 10 mM showed stimulatory effect. Addition of urea and KMnO4 resulted in the loss of enzyme activities; however, lower concentration of SDS and Tween 80 afforded protection of the enzyme activities. Galactose and maltose were non-inhibitory for the enzyme activities, while, fructose, mannose, xylose and lactose were slightly inhibitory. The relative hydrolysis sequence of polysaccharides were amylose greater than soluble starch = corn starch greater than glycogen.",
author = "Lin, {H. Y.} and Tsay, {S. S.}",
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TY - JOUR

T1 - Extracellular thermostable alpha-amylase from Bacillus stearothermophilus Q8

AU - Lin, H. Y.

AU - Tsay, S. S.

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AB - The alpha-amylase of Bacillus stearothermophilus Q8, previously isolated in our laboratory, was purified by ammonium sulfate precipitation and CM-sephadex chromatography. The activity the of partial purified alpha-amylase was to be protected by bovine serum albumin Ca2+ and Mg2+. The enzyme showed 100% activity at pH 9.0; 98%, at pH 8.0 and 41%; at pH 10.0. It expressed optimal reaction temperature at 90 degrees C, 81% of the activities remained at 100 degrees C. After 15 min incubation at 100 degrees C with the addition of 10 mM Ca2+, the enzyme only retained 67% activity. The enzyme, however, retained 10% of the maximal activity after 2 h incubation at 90 degrees C, in the absence of substrate and with the addition of Ca2+. Of cations, Na+ at 0.1 and 1 mM, Mn2+ at 0.1 mM showed stimulatory effect; of anions OH-Cl-I-HCO3-NO2-N3- at 10 mM showed stimulatory effect. Addition of urea and KMnO4 resulted in the loss of enzyme activities; however, lower concentration of SDS and Tween 80 afforded protection of the enzyme activities. Galactose and maltose were non-inhibitory for the enzyme activities, while, fructose, mannose, xylose and lactose were slightly inhibitory. The relative hydrolysis sequence of polysaccharides were amylose greater than soluble starch = corn starch greater than glycogen.

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