TRANSAMINASES IN A HALOPHILIC BACTERIUM No. 101

Abstract

1. Water-lysed extracts of a halophilic Pseudomonas strain No. 101 catalyzed the transamination reactions between α-ketoglutaric acid and L-aspartic acid, L-phenylalanine and L-tyrosine (maximum QTN: 1, 640, 2, 170 and 388, respectively).
2. These transaminases were not halophilic unlike alkaline phosphomonoesterase of this halophilic bacterium.
3. From the activity changes during heat-treatment and growth of the culture, it was suggested that at least two transaminases existed in the lysed extracts, one corresponding to aspartic acid and the other to phenylalanine.
The authors are indebted to Prof. F. Egami, Chemical Institute, Faculty of Science, Nagoya University, for the gift of the bacterial strain and also to Mr. M. Shiroishi, Food Research Institute, the Department of Agriculture and Forestry, for the preparation of pyridoxal phosphate.