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Pepsin immobilized on inorganic supports for the continuous coagulation of skim milk
Author(s) -
Taylor M. J.,
Cheryan M.,
Richardson T.,
Olson N. F.
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.260190506
Subject(s) - glutaraldehyde , pepsin , adsorption , skimmed milk , catalysis , chemistry , immobilized enzyme , covalent bond , chromatography , coagulation , desorption , rennet , chemical engineering , inorganic chemistry , organic chemistry , casein , enzyme , food science , psychology , psychiatry , engineering
The milk‐clotting enzyme pepsin was immobilized onto beads of alumina, titania, glass, stainless steel, iron oxide, and Teflon for treating skim milk in a fluidized‐bed reactor. Two covalent attachment procedures using silanized supports and glutaraldehyde and two adsorption procedures were evaluated. The three best catalysts were titania and glass, using the covalent attachment procedure, and alumina, using the adsorption procedure at pH 1.2. The pepsin adsorbed on alumina catalyst has commercial potential compared to the previously used glass catalyst. Attempts to increase the stability of pepsin adsorbed on alumina by cross‐linking with glutaraldehyde were unsuccessful owing to the low pH necessary for optimum pepsin adsorption. Desorption of pepsin from alumina during reactor operation was determined. Regeneration of spent catalysts was only partially successful.