Characterization of immobilized tyrosinase – an enzyme that is stable in organic solvent at 100 °C. Issue 69 (27th November 2018)

• Record Type: Journal Article
• Authors: Wu, Lidong; Rathi, Brijesh; Chen, Yi; Wu, Xiuhong; Liu, Huan; Li, Jincheng; Ming, Anjie; Han, Gang
• Is Part Of: RSC advances. Volume 8:Issue 69(2018)
• Page Start: 39529
• Page End: 39535
• Publication Date: 2018-11-27
• Subjects: Chemistry -- Periodicals; 540.5
• DOI: 10.1039/c8ra07559j
• Languages: English
• ISSNs: 2046-2069

Abstract

Abstract : Immobilized tyrosinase in hexane can withstand 100 °C over one week, and the half-life of the dry immobilized tyrosinase in organic solvent is strongly related to the polarity of the organic solvent. Abstract : Tyrosinase is a copper-containing enzyme present in plant and animal tissues, which catalyzes the production of melanin and other pigments. In organic solvent, tyrosinase can convert N -acetyl-l -tyrosine ethyl ester (insoluble in aqueous) to a derivative ofl -dopamine (a drug used for the treatment of Parkinson's disease). Thus, the performances of tyrosinase in organic solvent have attracted scientific attention since 1980. In this work, we investigated the stability of immobilized tyrosinase at high temperature in anhydrous organic solvent. Triethylaminoethyl cellulose (TEAE-Cellulose) performed the best out of six immobilization platforms. The dry immobilized tyrosinase became extremely thermostable in organic solvent, and the half-life of the dry immobilized tyrosinase in organic solvent is strongly related to the polarity of the organic solvent than their log P value. The immobilized tyrosinase loses its activity instantaneously in aqueous solution at 100 °C, but it keeps enzymatic activity within 10 min in hydrophilic methanol and over one month in hydrophobic hexane (log P : 4.66, non-polar) even incubating at 100 °C. This research provides valuable information for the design of new biocatalysts.