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Pure Appl. Chem., 2005, Vol. 77, No. 1, pp. 227-236

Gel-immobilized enzymes as promising biocatalysts: Results from Indo-Russian collaborative studies

Elena A. Markvicheva1, Vladimir I. Lozinsky2, Fatima M. Plieva2, Konstantin A. Kochetkov2, Lev D. Rumsh1, Vitali P. Zubov1, Jyotirmoy Maity3, Rajesh Kumar3, Virinder S. Parmar3 and Yury N. Belokon2

1 Shemyakin and Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Miklukho-Maklaya St. 16/10, Moscow 117871, Russia
2 Nesmeyanov Institute of Organoelement Compounds, Russian Academy of Sciences, Vavilov St. 28, Moscow, V-334, 117813, Russia
3 Bioorganic Laboratory, Department of Chemistry, University of Delhi, Delhi 110 007, India

Abstract: Chemo-enzymatic methods constitute a promising approach to obtain various biologically active compounds, including enantiomerically pure substances. Entrapment in gels is one of the most convenient methods to stabilize enzymes for their application in water/organic media. Proteases and lipases are widely used for enantioselective transformations of various organic compounds in water-poor media. In this study, chymotrypsin was entrapped into a composite poly(N-vinyl caprolactam)-calcium alginate (PVCL-CaAlg) and covalently attached to poly(vinyl alcohol) (PVA) cryogel beads. Lipase was immobilized by covalently attaching to aldehyde-bearing PVA cryogel beads. The activities of the entrapped biocatalysts were studied. Both entrapped α-chymotrypsin and lipase retained high activity in acetonitrile/water medium (water content 0.5–20 %) and displayed high storage stability for several months. The high operational stability of immobilized α-chymotrypsin and lipase in a cyclic process (up to 912 h in total) was also demonstrated. Gel-immobilized enzymes were successfully used to obtain optically pure L-phenylalanine (ee 98.6 and 83 % in the case of α‑chymotrypsin and lipase, respectively) by enantioselective hydrolysis of Schiff’s base of amino acid ethyl ester in an acetonitrile/water system.