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Immobilization of β-Tyrosinase Cells with Collagen

  • H. Yamada
  • K. Yamada
  • H. Kumagai
  • T. Hino
  • S. Okamura

Abstract

β-Tyrosinase (tyrosine phenol-lyase: EC 4.1.99.2) catalyzes the stoichiometric conversion of L-tyrosine to pyruvate, ammonia and phenol, and requires pyridoxal phosphate (PLP) as a cofactor (1–3). Apparently homogeneous preparations of the enzyme were prepared by us from cells of Escherichia intermedia (4,5) and Erwinia herbicola (6) grown in media supplemented with L-tyrosine (7). We have reported that crystalline preparations of the enzyme catalyze a series of α,β-elimination (Eq. 1 and 2) β-replacement and racemization (Eq.6) reactions (8–11). The reverse of the α,β-elimination reaction to synthesize L-tyrosine or L-dopa (Eq. 7,8) was also catalyzed by crystalline preparations of the enzyme (12).

Keywords

Immobilize Cell Pyruvic Acid Collagen Membrane Sodium Sulfite Starch Solution 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Springer Science+Business Media New York 1978

Authors and Affiliations

  • H. Yamada
    • 1
  • K. Yamada
    • 1
  • H. Kumagai
    • 1
  • T. Hino
    • 2
  • S. Okamura
    • 3
  1. 1.Research Institute for Food ScienceKyoto UniversityKyotoJapan
  2. 2.Research Institute for Production DevelopmentKyotoJapan
  3. 3.Department of Polymer ChemistryKyoto UniversityKyotoJapan

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