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      Improving Stability and Activity of Cross-linked Enzyme Aggregates Based on Polyethylenimine in Hydrolysis of Fish Oil for Enrichment of Polyunsaturated Fatty Acids

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          Abstract

          Cross-linking of enzyme aggregates from recombinant Geotrichum sp. lipase based on polyethylenimine (PEI) was applied to hydrolyze fish oil for enrichment of polyunsaturated fatty acids successfully. Through acetone precipitation and cross-linking of physical aggregates using glutaraldehyde in the presence of PEI, firmly cross-linked enzyme aggregates (PEI-CLEAs) were prepared. They could maintain more than 65% of relative hydrolysis degree after incubation in the range of 50-55 °C for 4 h and maintain more than 85% of relative hydrolysis degree after being treated by acetone, tert-butyl alcohol and octane for 4 h. PEI-CLEAs increased hydrolysis degree to 42% from 12% by free lipase. After five batch reactions, PEI-CLEAs still maintained 72% of relative hydrolysis degree. Hydrolysis of fish oil by PEI-CLEAs produced glycerides containing concentrated EPA and DHA in good yield. PEI-CLEAs had advantages over general CLEAs and free lipase in initial reaction rate, hydrolysis degree, thermostability, organic solvent tolerance and reusability.

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          Cross-linked enzyme aggregates: a simple and effective method for the immobilization of penicillin acylase.

          [reaction--see text] Penicillin G acylase (penicillin amidohydrolase, E.C. 3.5.1.11) was immobilized in a simple and effective way by physical aggregation of the enzyme, using a precipitant, followed by chemical cross-linking to form insoluble cross-linked enzyme aggregates (CLEAs). These had the same activity in the synthesis of ampicillin as cross-linked crystals of the same enzyme, but the accompanying hydrolysis of the side-chain donor was much less. Penicillin G acylase CLEAs also catalyzed the synthesis of ampicillin in a broad range of organic solvents.
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            Preparation, optimization, and structures of cross-linked enzyme aggregates (CLEAs).

            The broad applicability of the cross-linking of enzyme aggregates to the effective immobilisation of enzymes is demonstrated and the influence of many parameters on the properties of the resulting CLEAs is determined. The relative simplicity of the operation ideally lends itself to high-throughput methodologies. The aggregation method was improved up to 100% activity yield for any enzyme. For the first time, the physical structures of CLEAs are elucidated. Copyright 2004 Wiley Periodicals, Inc.
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              Cross-linked enzyme aggregates (CLEAs): A novel and versatile method for enzyme immobilization (a review)

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                Author and article information

                Journal
                Applied Biochemistry and Biotechnology
                Appl Biochem Biotechnol
                Springer Nature America, Inc
                0273-2289
                1559-0291
                February 2012
                December 15 2011
                February 2012
                : 166
                : 4
                : 925-932
                Article
                10.1007/s12010-011-9480-z
                6dcec409-8cde-428a-83fb-bde07763dab4
                © 2012
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