Kinetic study of tyrosinase immobilized on polymeric membrane

被引：35

作者：

Donato, L. ^{[1
]}

Algieri, C. ^{[1
]}

Rizzi, A. ^{[1
]}

Giorno, L. ^{[1
]}

机构：

[1] Univ Calabria, Natl Res Council, Inst Membrane Technol, CNR, I-87036 Arcavacata Di Rende, Italy

来源：

JOURNAL OF MEMBRANE SCIENCE | 2014年 / 454卷

关键词：

Mushroom tyrosinase; Immobilization; Polyamide membranes; Membrane reactor; Kinetic properties; ENZYME-IMMOBILIZATION; L-DOPA; INVERTASE; CHITOSAN; LIPASE; BEADS; STABILITY; OXIDASE; REACTOR;

D O I：

10.1016/j.memsci.2013.12.029

中图分类号：

TQ [化学工业];

学科分类号：

0817 ;

摘要：

Kinetic properties of tyrosinase immobilized on a polymeric membrane for the production of 4-dihydroxyphenylalanine (L-DOPA) were investigated. A comparison with the properties shown by the free enzyme used in a stirred tank reactor was also carried out. The values of the Michaelis-Menten constant indicated that the immobilized tyrosinase exhibited better affinity for the substrate (K-m = 1.56 mM and 2.10 mM for the immobilized and free enzyme, respectively). The stability (pH, thermal, storage and operational) of both free and immobilized tyrosinase was also evaluated. Results showed that the immobilization enhanced the enzyme stability. The optimum pH and temperature for the activity of both free and immobilized enzyme were found at pH 7.0 and 35 degrees C, respectively. However, the immobilized tyrosinase was more stable in the whole range of pH and temperature. These advantages of the immobilized enzyme make it a good candidate for its use in different industrial processes. (C) 2013 Elsevier B.V. All rights reserved.

引用

页码：346 / 350

页数：5

共 29 条

[1] Immobilised tyrosinase-based biosensor for the detection of tea polyphenols [J].