Stabilization of carboxyl esterase

Chemistry: molecular biology and microbiology – Micro-organism – tissue cell culture or enzyme using process... – Preparing oxygen-containing organic compound

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435136, 435197, 4352523, 4353201, 935 14, 935 10, 536 232, C12N 1555, C12N 918

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055388760

ABSTRACT:
Carboxyl esterase is inactivated by several chemical compounds such as naproxen or diclofop. By substituting or modifying certain basic residues of the carboxyl esterase, this enzyme shows improved stability properties during application. In this way it is possible to perform stereospecific hydrolysis reactions on industrial scale even at high substrate concentrations.

REFERENCES:
patent: 4101380 (1978-07-01), Rubinstein et al.
patent: 4760025 (1988-07-01), Estell et al.
patent: 4886750 (1989-12-01), Bertola et al.
Royer et al. FEBS Letters, 80 (1): 89-94, Aug. 1977.
Schmid, "Stabilized Soluble Enzymes" Advances in Biochemical Engineering 12, Ghose, Fiechler & Blakebrough (Eds), Springer, Berlin (1979) pp. 41-115.
Boudrant et al., "Continuous Proteolysis with a Stabilized Protease", Biotechnol. Bioeng. 18 (1976) pp. 1719-1734.
Reese et al., "Stability of the Cellulase of Trichoderma reesei under Use Conditions", Biotechnol. Bioeng. 22(2) 1980 323-335.
Ugarova, "Influence of Chemical Modification on the Thermal Stability of Horseradish Peroxidase", Biokhimiya 42(7) 1977 1212-1220.

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