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Protease covalently coupled to porous glass: Preparation and characterization
Author(s) -
Mason R. D.,
Detar C. C.,
Weetall H. H.
Publication year - 1975
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.260170706
Subject(s) - covalent bond , casein , porous glass , solubility , protease , chemistry , porosity , thermal stability , immobilized enzyme , chromatography , substrate (aquarium) , chemical engineering , enzyme , hydrolysate , hydrolysis , organic chemistry , materials science , oceanography , engineering , geology
Abstract A microbial protease was immobilized by covalent attachment, to porous glass. This material was characterized for pH optimum, thermal stability, and operational half–life using casein as substrate. The immobilized enzyme was used for preparation of soya hydrolysates, low in free amino acids with high solubility.