Enhanced enzymatic activity and stability of trypsin by reductive alkylation in solid phase

Biotechnology and Bioengineering
R F Tsuji


Amino groups of trypsin (EC were reductively alkylated in solid phase to obtain a surface-active and biologically active enzyme in an o/w emulsion system. Trypsin adsorbed on a benzamidine-sepharose column was reductively alkylated with n-octanal in the presence of sodium borohydride, i.e., trypsin-C8. Activity of trypsin-C8 against Nalpha-benzoyl-L-arginine-p-nitroanilide was three times higher than that of native trypsin. Activities of trypsin and trypsin-C8 against casein were almost the same. After incubating the trypsin solution at 40 degrees C for 1 h, residual activities in the emulsion and solution systems were 64.2 and 57.4%, respectively. On the other hand, residual activities of native trypsin following incubation were 21.8% in the emulsion system and 33.2% in the solution system. Enhancement of trypsin-C8 stability in the emulsion system may derive from interaction between the hydrophobic areas of trypsin-C8 molecules and the hydrophobic phase of the emulsion.


May 23, 1979·Biochimica Et Biophysica Acta·A Abuchowski, F F Davis
Jan 1, 1979·International Journal of Peptide and Protein Research·K FretheimR E Feeney
Feb 1, 1973·Archives of Biochemistry and Biophysics·H F Hixson, A H Nishikawa
Aug 12, 1966·Biochemical and Biophysical Research Communications·O MikesF Sorm
Nov 1, 1961·Archives of Biochemistry and Biophysics·B F ERLANGERW COHEN
Nov 30, 1967·Biochemical and Biophysical Research Communications·T Chase, E Shaw
Aug 20, 1988·Biotechnology and Bioengineering·K Ampon, G E Means

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Jan 1, 1991·Biotechnology Advances·C O Fágáin, R O'Kennedy
Apr 1, 2009·Journal of Bioscience and Bioengineering·Steven S-S WangHwai-Shen Liu

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