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从日本曲霉中提取β-呋喃果糖苷酶的纯化和性质。

Purification and properties ofβ-fructofuranosidase from Aspergillus japonicus.

机构信息

Department of Industrial Chemistry, Faculty of Engineering, Miyazaki University, 1-1 Gakuen Kibanadai Nishi, 889-21, Miyazaki, Japan.

出版信息

World J Microbiol Biotechnol. 1992 May;8(3):276-9. doi: 10.1007/BF01201878.


DOI:10.1007/BF01201878
PMID:24425477
Abstract

β-Fructofuranosidase fromAspergillus japonicus, which produces 1-kestose (O-β-D-fructofuranosyl-(2→1)-β-D-fructofuranosyl α-D-glucopyranoside) and nystose (O-β-D-fructofuranosyl-(2→1)-β-D-fructofuranosyl-(2→1)-β-D-fructofuranosyl α-D-glucopyranoside) from sucrose, was purified to homogeneity by fractionation with calcium acetate and ammonium sulphate and chromatography with DEAE-Cellulofine and Sephadex G-200. Its molecular size was estimated to be about 304,000 Da by gel filtration. The enzyme was a glycoprotein which contained about 20% (w/w) carbohydrate. Optimum pH for the enzymatic reaction was 5.5 to 6. The enzyme was stable over a wide pH range, from pH 4 to 9. Optimum reaction temperature for the enzyme was 60 to 65°C and it was stable below 60°C. The Km value for sucrose was 0.21M. The enzyme was inhibited by metal ions, such as those of silver, lead and iron, and also byp-chloromercuribenzoate.

摘要

米曲霉β-呋喃果糖苷酶能将蔗糖分解为棉子糖(O-β-D-呋喃果糖基-(2→1)-β-D-呋喃果糖基-α-D-吡喃葡萄糖苷)和昆布二糖(O-β-D-呋喃果糖基-(2→1)-β-D-呋喃果糖基-(2→1)-β-D-呋喃果糖基-α-D-吡喃葡萄糖苷),本研究通过乙酸钙和硫酸铵分级、DEAE-纤维素和 Sephadex G-200 层析对其进行了纯化,获得了均一性酶制剂。凝胶过滤法估计该酶的分子大小约为 304,000 Da。该酶是一种糖蛋白,含有约 20%(w/w)的碳水化合物。酶促反应的最适 pH 值为 5.5 至 6。该酶在较宽的 pH 范围内稳定,pH 值为 4 至 9。该酶的最适反应温度为 60 至 65°C,低于 60°C 时稳定。蔗糖的 Km 值为 0.21M。该酶被银、铅和铁等金属离子以及对氯汞苯甲酸抑制。

相似文献

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Purification and properties ofβ-fructofuranosidase from Aspergillus japonicus.

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[2]
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[3]
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3 Biotech. 2020-10

[2]
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[3]
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Curr Microbiol. 2017-9

[4]
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[5]
Production of the Functional Trisaccharide 1-Kestose from Cane Sugar Molasses Using Aspergillus japonicus β-Fructofuranosidase.

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[6]
Properties of Aspergillus japonicus β-fructofuranosidase immobilized on porous silica.

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本文引用的文献

[1]
Production of β-fructofuranosidase byAspergillus japonicus.

World J Microbiol Biotechnol. 1992-3

[2]
The gel-filtration behaviour of proteins related to their molecular weights over a wide range.

Biochem J. 1965-9

[3]
Cleavage of structural proteins during the assembly of the head of bacteriophage T4.

Nature. 1970-8-15

[4]
Purification and some properties of beta-fructofuranosidase I from Arthrobacter sp. K-1.

Agric Biol Chem. 1990-4

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