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Preparation and properties of proteases immobilized on anion exchange resin with glutaraldehyde
Author(s) -
Ohmiya Kunio,
Tanimura Shuya,
Kobayashi Takeshi,
Shimizu Shoichi
Publication year - 1978
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.260200102
Subject(s) - chemistry , proteases , immobilized enzyme , glutaraldehyde , chromatography , enzyme , protease , biochemistry , alkaline protease , casein
High activity alkaline protease was obtained when the enzyme was immobilized on Dowex MWA‐1 (mesh 20–50) with 10% glutaraldehyde in chilled phosphate buffer ( M /15, pH 6.5). Activity yields of the protease and rennet were 27 and 29, respectively. The highest activities appeared at 60°C, pH 10 for alkaline protease and 50°C, pH 4.0 for rennet. The properties of both proteases were not essentially changed by the immobilization except that the K m values of both enzymes were increased about tenfold as a result of immobilization. Both proteases in the immobilized state were more stable than those in the free state at 60°C. Other peptide hydrolases, β‐galactosidase, invertase, and glucoamylase, were successfully immobilized with high activities, but lipase, hexokinase, glucose‐6‐phosphate dehydrogenase, and xanthine oxidase became inactive.