Effect of carboxymethylcellulose on the proteolysis of alphas-casein by immobilized pepsin

Valaris, M.; Harper, W.J.

Journal of Food Science 38(3): 477-480

1973


ISSN/ISBN: 0022-1147
DOI: 10.1111/j.1365-2621.1973.tb01459.x
Accession: 000068625

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Abstract
Effect of the presence of carboxymethylcellulose (CMC) on activity of pepsin covalently attached on alkylamino-glass derivatives was investigated. CMC above 0.01% concn. was found to inhibit action of pepsin on alpha s-casein, inhibition being independent of substrate concn. Further experimentation with [carboxy-14C]CMC showed that the inhibitor binds directly onto the enzyme and not onto the porous glass beads. CMC binding capacity of immobilized pepsin was unaffected by the presence of the substrate alpha s-casein. Treatment of this column with HCl resulted in some dissociation of enzyme-inhibitor (EI) complex but did not restore any of the proteolytic activity. Subsequent washing of acid-treated immobilized pepsin with pH 5.0 acetate buffer had no effect on either the EI complex or enzymic activity. Activity of the bound enzyme, however, was almost doubled after treatment with 1M NaCl although no further release of inhibitor from the column was detected.

Effect of carboxymethylcellulose on the proteolysis of alphas-casein by immobilized pepsin