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Enzymatic Dipeptide Synthesis by Surfactant‐Coated α‐Chymotrypsin Complexes in Supercritical Carbon Dioxide
Author(s) -
Mishima Kenji,
Matsuyama Kiyoshi,
Baba Masayoshi,
Chidori Masuhiro
Publication year - 2003
Publication title -
biotechnology progress
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 129
eISSN - 1520-6033
pISSN - 8756-7938
DOI - 10.1021/bp010261s
Subject(s) - chymotrypsin , dipeptide , chemistry , pulmonary surfactant , supercritical carbon dioxide , supercritical fluid , organic chemistry , chromatography , amide , enzyme , nuclear chemistry , amino acid , biochemistry , trypsin
Enzymatic dipeptide synthesis by surfactant‐coated α‐chymotrypsin complexes was performed in supercritical CO 2 and liquid CO 2 at 308.2 and 333.2 K at pressures of 6.1 and 10.1 MPa. The enzymatic activity of coated α‐chymotrypsin complexes for dipeptides synthesis at 10.1 MPa in supercritical CO 2 (SC‐CO 2 ) was higher than that in a liquid CO 2 and ethyl acetate solution at 6.1 MPa. The behavior of α‐chymotrypsin in SC‐CO 2 was similar to that in liquid ethyl acetate. And increasing the pressure and temperature increased the maximum conversion and the enzymatic reaction rate in SC‐CO 2 . Furthermore, the control of the water content in the reaction media had a dominant effect on the enzymatic activity. The maximum conversion for the dipeptide synthesis by the surfactant‐coated α‐chymotrypsin was obtained at 4% water content. The α‐chymotrypsin complexes exhibited a higher enzymatic activity than native α‐chymotrypsin in SC‐CO 2 . The nonionic surfactants l ‐glutamic acid dialkyl ester ribitol amide and sorbitan monostearate were more favored than the anionic surfactant sodium bis(2‐ethylhexyl)sulfosuccinate.

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