米曲霉β-呋喃果糖苷酶固定在多孔硅上的性质。

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

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. 1993 Mar;9(2):216-20. doi: 10.1007/BF00327841.

DOI:10.1007/BF00327841

PMID:24419951

Abstract

β-Fructofuranosidase from Aspergillus japonicus MU-2, which produces fructo-oligosaccharides (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 immobilized, covalently with glutaraldehyde onto alkylamine porous silica, at high efficiency (64%). Optimum pore diameter of porous silica for immobilization of the enzyme was 91.7 nm. After immobilization, the enzyme's stabilities to temperature, metal ions and proteolysis were improved, while its optimum pH and temperature were unchanged. The highest efficiency of continuous production of fructo-oligosaccharides (more than 60%), using a column packed with the immobilized enzyme, was obtained at 40% to 50% (w/v) sucrose. The half-life of the column during long-term continuous operation at 55°C was 29 days.

摘要

米曲霉 MU-2 β-呋喃果糖苷酶能够将蔗糖转化为低聚果糖（蔗果三糖：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；蔗果四糖：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），该酶通过戊二醛共价固定在烷基胺多孔硅上，具有很高的效率（64%）。用于酶固定的最佳多孔硅孔径为 91.7nm。固定化后，酶对温度、金属离子和蛋白水解的稳定性得到提高，而最适 pH 值和温度保持不变。使用填充有固定化酶的柱子，在 40%至 50%（w/v）蔗糖浓度下，可获得最高的连续生产低聚果糖效率（超过 60%）。在 55°C 下进行长期连续运行时，柱子的半衰期为 29 天。