Production of β-fructofuranosidases by Aspergillus niveus using agroindustrial residues as carbon sources: Characterization of an intracellular enzyme accumulated in the presence of glucose

被引：41

作者：

Guimaraes, Luis Henrique S. ^{[1
]}

Somera, Alexandre Favarin ^{[1
]}

Terenzi, Hector Francisco ^{[1
]}

Teixeira de Moraes Polizeli, Maria de Lourdes ^{[1
]}

Jorge, Joao Atilio ^{[1
]}

机构：

[1] Univ Sao Paulo, Dept Biol, Fac Filosofia Ciencias & Letras Ribeirao Preto, BR-14040901 Ribeirao Preto, SP, Brazil

来源：

PROCESS BIOCHEMISTRY | 2009年 / 44卷 / 02期

关键词：

Invertase; Aspergillus niveus; Glucose; beta-D-Fructofuranosidase; Purification; Sucrose; SOLID-STATE FERMENTATION; INVERTASE EXPRESSION; ACID INVERTASE; NIGER; PURIFICATION; JAPONICUS; SUCROSE; FUNGUS;

D O I：

10.1016/j.procbio.2008.10.011

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The production of beta-fructofuranosidases by Aspergillus niveus, cultivated under submerged fermentation using agroindustrial residues, was investigated. The highest productivity of beta-fructofuranosidases was obtained in Khanna medium supplemented with sugar cane bagasse as carbon source. Glucose enhanced the production of the intracellular enzyme, whereas that of the extracellular one was decreased. The intracellular beta-fructofuranosidase was a trimeric protein of approximately 141 kDa (gel filtration) with 53.5% carbohydrate content, composed of 57 kDa monomers (SDS-PAGE). The optimum temperature and optimum pH were 60 degrees C and 4.5, respectively. The purified enzyme showed good thermal stability and exhibited a half-life of 53 min at 60 degrees C. beta-Fructofuranosidase activity was slightly activated by Cu(2+), Mn(2+), Mg(2+), and Na(+) at 1 mM concentration. The enzyme hydrolyzed sucrose, raffinose, and inulin, with K(d) values of 5.78 mM, 5.74 mM, and 1.74 mM, respectively. (C) 2008 Elsevier Ltd. All rights reserved.

引用

页码：237 / 241

页数：5