دورية أكاديمية
The Tyrosinase Produced by Lentinula boryana (Berk. & Mont.) Pegler Suffers Substrate Inhibition by L-DOPA
| العنوان: | The Tyrosinase Produced by Lentinula boryana (Berk. & Mont.) Pegler Suffers Substrate Inhibition by L-DOPA |
|---|---|
| المؤلفون: | Rodrigo Otávio de Faria, Vivian Rotuno Moure, Wellington Balmant, Maria Angela Lopes de Almeida Amazonas, Nadia Krieger, David Alexander Mitchell |
| المصدر: | Food Technology and Biotechnology, Vol 45, Iss 3, Pp 334-340 (2007) |
| بيانات النشر: | University of Zagreb Faculty of Food Technology and Biotechnology, 2007. |
| سنة النشر: | 2007 |
| المجموعة: | LCC:Biotechnology LCC:Food processing and manufacture |
| مصطلحات موضوعية: | tyrosinase, Lentinula boryana, substrate inhibition, 3,4-dihydroxy-L-phenylalanine, L-DOPA, Biotechnology, TP248.13-248.65, Food processing and manufacture, TP368-456 |
| الوصف: | We undertook a preliminary characterization of the tyrosinase produced by a strain of Lentinula boryana from Brazil, with a view to evaluate its potential for biotechnological applications. The enzyme was similar to other fungal tyrosinases in many respects. When the crude extract was characterized, the tyrosinase activity was optimal at pH=6 and was not particularly thermostable, with half-lives of about 10 min and 1 min at 50 and 60 °C, respectively. We purified the enzyme with ammonium sulfate precipitation followed by ion exchange chromatography on a DEAE Sepharose column, obtaining a yield of 33 % and a 5.3-fold enrichment. The purified preparation gave three bands on SDS-PAGE, with molecular masses of 20, 27 and 47 kDa. This preparation showed substrate inhibition kinetics with L-DOPA (3,4-dihydroxy-L-phenylalanine), with a KM of 1.9 mM and a KI of 72 mM. Under the same reaction conditions, a commercial mushroom tyrosinase followed Michaelis-Menten kinetics, with a KM of 0.51 mM. Although the present study did not identify properties that would make the tyrosinase of L. boryana more suitable in biotechnological applications than tyrosinases from other mushrooms, it has made a contribution by showing that the enzyme suffers substrate inhibition by L-DOPA, something that has not previously been reported for mushroom tyrosinases. |
| نوع الوثيقة: | article |
| وصف الملف: | electronic resource |
| اللغة: | English |
| تدمد: | 1330-9862 1334-2606 |
| Relation: | http://hrcak.srce.hr/file/38139; https://doaj.org/toc/1330-9862; https://doaj.org/toc/1334-2606 |
| URL الوصول: | https://doaj.org/article/2715453b7cd2403a82efea0a8b3c7433 |
| رقم الأكسشن: | edsdoj.2715453b7cd2403a82efea0a8b3c7433 |
| قاعدة البيانات: | Directory of Open Access Journals |
Full Text Finder | تدمد: | 13309862 13342606 |
|---|