Properties of Tyrosinase from Pseudomonas melanogenum |
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Authors: | Hajime Yoshida Yoshitake Tanaka Kiyoshi Nakayama |
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Affiliation: | Tokyo Research Laboratory, Kyowa Hakko Kogyo Co., Ltd., Machida-shi, Tokyo |
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Abstract: | The properties of the tyrosinase from Pseudomonas melanogenum was investigated with the crude enzyme preparation. Optimum temperature and pH of the enzyme were 23°C and 6.8, respectively. l-Tyrosine, d-tyrosine, m-tyrosine, N-acetyl-l-tyrosine and l-DOPA were utilized as a substrate by the enzyme. The value for Km obtained were as follows: l-tyrosine 6.90 × 10?4 m, d-tyrosine 1.43 ×10?3 m and l-DOPA 9.90 × 10?4 m. The enzyme was inhibited by chelating agents of Cu2+ l-cysteine, l-homocysteine, thiourea and diethyl-dithiocarbamate and the inhibition was completely reversed by the addition of excess Cu2+ From these results it is concluded that the enzyme is a copper-containing oxidase. |
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Keywords: | Candida boidinii D-amino acid oxidase peroxisome high-level production gene expression |
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