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Silanized silica bound trypsin as analytical probe

Bharadwaj, D.; Mukherjee, A.; Roy, M.S.; Hati, R.N.; Mukherjee, R.N.

Indian Journal of Biochemistry and Biophysics 29(4): 375-377

1992

ISSN/ISBN: 0301-1208
PMID: 1330896
Document Number: 395101
Trypsin immobilized by covalent coupling to silanized silica shows significant activity (30-38%) and greater thermostability as compared to soluble trypsin. Proteolytic processing of albumin at varying periods suggest that the enzyme matrix can be used efficiently for limited proteolysis. Repeated use of the immobilized enzyme in protein digestion produces similar products as seen by electrophoretic analysis. Also, digestion of albumin by the immobilized enzyme follows similar pattern as that by soluble enzyme. The enzyme matrix can be easily removed from the incubation mixture. The results indicate the possibility of the immobilized enzyme for its effective application as analytical tool in peptide mapping and limited proteolytic processing.

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