Purification and characterization of a highly stable tyrosinase from Thermomicrobium roseum
- Authors
- Kong, Kwang-Hoon; Hong, Min-Pyo; Choi, Sang-Sook; Kim, Yong-Tae; Cho, Sung-Hye
- Issue Date
- Apr-2000
- Publisher
- WILEY
- Citation
- BIOTECHNOLOGY AND APPLIED BIOCHEMISTRY, v.31, no.2, pp 113 - 118
- Pages
- 6
- Journal Title
- BIOTECHNOLOGY AND APPLIED BIOCHEMISTRY
- Volume
- 31
- Number
- 2
- Start Page
- 113
- End Page
- 118
- URI
- https://scholarworks.bwise.kr/cau/handle/2019.sw.cau/25336
- DOI
- 10.1042/BA19990096
- ISSN
- 0885-4513
1470-8744
- Abstract
- Tyrosinase, with an isoelectric point at pH 4.9, was purified to electrophoretic homogeneity from an extremely thermophilic bacterium, Thermomicrobium roseum. Gel filtration, N-terminal amino acid sequencing and SDS/PAGE analysis indicate that T. roseum tyrosinase is composed of two identical subunits, each with a molecular mass of 43 000 Da, The enzyme exhibited high substrate specificity towards catechol, chlorogenic acid, L-3-(3,4-dihydroxyphenyl)-L-alanine (L-DOPA) and pyrogallol. The K-m value of the enzyme for L-DOPA was 0.18 mM. beta-Mercaptoethanol and sodium diethyldithiocarbamate notably inhibited the enzymic activity. The activity of the enzyme was optimal at pH 9.5 and 70 degrees C, and was increased by addition of I mM Mg2+, K+ or Cu2+. The enzyme was highly stable against high temperature and guanidine hydrochloride. The N-terminal amino acid sequence of the enzyme was determined to be Asp-lle-Asn-Cly-Gly-Gly-Ala-Thr-Leu-Pro-Gln-Lys-Leu-Tyr. These facts indicate that T. roseum tyrosinase appears to be distinct from the tyrosinases so far purified from other sources.
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