Activity stabilization of Aspergillus niger and Escherichia coli phytases immobilized on allophanic synthetic compounds and montmorillonite nanoclays

被引:65
作者
Menezes-Blackburn, Daniel
Jorquera, Milko [1 ]
Gianfreda, Liliana [2 ]
Rao, Maria [2 ]
Greiner, Ralf [3 ]
Garrido, Elizabeth [1 ]
de la Luz Mora, Maria [1 ]
机构
[1] Univ La Frontera, Sci & Technol Bioresource Nucleus BIOREN, Temuco 01145, Chile
[2] Univ Naples Federico II, Dipartimento Sci Suolo Pianta & Ambiente & Prod A, Portici, Italy
[3] Fed Res Inst Nutr & Food, Max Rubner Inst, Dept Food Technol & Bioproc Engn, Karlsruhe, Germany
关键词
Phytase; Enzyme immobilization; Nanoclay; Phytate; Phosphorus; ACID-PHOSPHATASE; ENZYME-ACTIVITY; PH; DEGRADATION; ADSORPTION; STABILITY; MANGANESE; KINETICS;
D O I
10.1016/j.biortech.2011.07.054
中图分类号
S2 [农业工程];
学科分类号
0828 ;
摘要
The aim of this work was to study the stabilization of the activity of two commercial microbial phytases (Aspergillus niger and Escherichia coli) after immobilization on nanoclays and to establish optimal conditions for their immobilization. Synthetic allophane, synthetic iron-coated allophanes and natural montmorillonite were chosen as solid supports for phytase immobilization. Phytase immobilization patterns at different pH values were strongly dependent on both enzyme and support characteristics. After immobilization, the residual activity of both phytases was higher under acidic conditions. Immobilization of phytases increased their thermal stability and improved resistance to proteolysis, particularly on iron-coated allophane (6% iron oxide), which showed activation energy (E-a) and activation enthalpy (Delta H-#) similar to free enzymes. Montmorillonite as well as allophanic synthetic compounds resulted in a good support for immobilization of E. coli phytase, but caused a severe reduction of A. niger phytase activity. (C) 2011 Published by Elsevier Ltd.
引用
收藏
页码:9360 / 9367
页数:8
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