Optimization of the immobilization of sweet potato amylase using glutaraldehyde-agarose support. Characterization of the immobilized enzyme

被引：51

作者：

Tavano, Olga Luisa ^{[1
]}

Fernandez-Lafuente, Roberto ^{[2
]}

Goulart, Antonio Jose ^{[3
]}

Monti, Rubens ^{[3
]}

机构：

[1] Univ Fed Triangulo Mineiro, ICS, Dept Nutr, BR-38025360 Uberaba, MG, Brazil

[2] CSIC, ICP, Dept Biocatalysis, Canto Blanco 28049, Madrid Zc, Spain

[3] UNESP Sao Paulo State Univ, Fac Pharmaceut Sci, Dept Food Nutr, BR-14840000 Araraquara, SP, Brazil

来源：

PROCESS BIOCHEMISTRY | 2013年 / 48卷 / 07期

关键词：

Beta-amylase; Immobilization; Sweet potato; Agarose; Glutaraldehyde; BETA-AMYLASE; ACTIVATED SUPPORTS; PROTEIN IMMOBILIZATION; GLYOXYL-AGAROSE; ALPHA-AMYLASE; STABILIZATION; STABILITY; STARCH; PERFORMANCE;

D O I：

10.1016/j.procbio.2013.05.009

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：

A simplified procedure for the preparation of immobilized beta-amylase using non-purified extract from fresh sweet potato tubers is established in this paper, using differently activated agarose supports. Beta-amylase glutaraldehyde derivative was the preparation with best features, presenting improved temperature and pH stability and activity. The possibility of reusing the amylase was also shown, when this immobilized enzyme was fully active for five cycles of use. However, immobilization decreased enzyme activity to around 15%. This seems to be mainly due to diffusion limitations of the starch inside the pores of the biocatalyst particles. A fifteen-fold increase in the Km was noticed, while the decrease of Vmax was only 30% (10.1 U mg(-1) protein and 7.03 U mg(-1) protein for free and immobilized preparations, respectively). (C) 2013 Elsevier Ltd. All rights reserved.

引用

页码：1054 / 1058

页数：5

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