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The enzymatic conversion of L ‐histidine to urocanic acid by whole cells of Micrococcus luteus immobilized on carbodiimide activated carboxymethylcellulose
Author(s) -
Jack T. R.,
Zajic J. E.
Publication year - 1977
Publication title -
biotechnology and bioengineering
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.136
H-Index - 189
eISSN - 1097-0290
pISSN - 0006-3592
DOI - 10.1002/bit.260190503
Subject(s) - micrococcus luteus , carbodiimide , chemistry , urocanic acid , histidine , chromatography , cellulose , biochemistry , immobilized enzyme , enzyme , escherichia coli , gene
Whole cells of Micrococcus luteus (formerly Sarcina lutea ATCC 9341) have been covalently linked to a carboxymethylcellulose support system, with the retention of histidine ammonia–lyase activity. The dependence of the rate of urocanic acid formation on pH, temperature, and added surfactant concentration was similar for the free and the immobilized cells. The immobilization procedure used is based on the carbodiimide activation of carboxymethylcellulose and has been optimized for the histidine ammonia–lyase activity of the immobilized cells on a given weight of cellulose. In a column reactor at 23°C and superficial velocity of 0.044 cm/min, 5 g of cellulose with bound cells gave a 35% conversion of an L ‐histidine solution (0.25 M , pH 9.0) to urocanic acid for 16 days of continuous operation. The scope of this carbodiimide assisted immobilization procedure has been investigated for a series of microorganisms and a variety of carboxylate functionalized supports.