Performance evaluation of a silk protein-based matrix for the enzymatic conversion of tyrosine to L-DOPA

被引：25
作者：
Acharya, Chitrangada [1 ]
Kumar, Veerendra [1 ]
Sen, Ramkrishna [1 ]
Kundu, Subhas C. [1 ]
机构：
[1] Department of Biotechnology, Indian Institute of Technology
来源：
Biotechnology Journal | 2008年 / 3卷 / 02期
关键词：
Fourier transform infra red spectroscopy; Immobilized tyrosinase; L-DOPA; Silk fibroin;
D O I：
10.1002/biot.200700120
中图分类号：
学科分类号：
摘要：
L-DOPA (3, 4-dihydroxyphenyl-L-alanine), one of the most important intermediates in the melanin biosynthesis pathway, is used for the treatment of Parkinson's disease. With a view of developing a cheaper and more effective method for the bioconversion of tyrosine to L-DOPA, the potential and performance of a novel fibrous matrix prepared from Bombyx mori silk protein fibroin were evaluated for the immobilization of tyrosinase. Cross-linkage between fibroin and tyrosinase using glutaraldehyde was evident from Fourier transform infra red spectroscopy. Maximum product formation occurred when 1000 U enzyme was immobilized on 20 mg fibroin. The optimum conditions for maximal L-DOPA production using immobilized tyrosinase were 40°C and pH 5.5, conditions that caused a 50% loss of free enzyme activity. Immobilized tyrosinase also showed to have a higher degree of stability during storage and it retained 80% of its original activity after repeated reuses. The efficiency of this immobilized tyrosinase system to produce L-DOPA was high, as evident from a high effectiveness factor, between 0.7 and 0.8, thereby making this method feasible for the large-scale production of L-DOPA. © 2008 Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim.
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页码：226 / 233
页数：7
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