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Plasma‐Modified Polypropylene as Carrier for the Immobilization of Candida antarctica Lipase B and Pyrobaculum calidifontis Esterase
Author(s) -
Vorhaben Torge,
Böttcher Dominique,
Jasinski Dagmar,
Menyes Ulf,
Brüser Volker,
Schröder Karsten,
Bornscheuer Uwe T.
Publication year - 2010
Publication title -
chemcatchem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.497
H-Index - 106
eISSN - 1867-3899
pISSN - 1867-3880
DOI - 10.1002/cctc.201000130
Subject(s) - candida antarctica , lipase , esterase , chemistry , vinyl acetate , transesterification , polypropylene , immobilized enzyme , polymer chemistry , catalysis , enzyme , organic chemistry , copolymer , polymer
In this work, the immobilization of two hydrolases on plasma‐modified polypropylene carriers was investigated. Treating Accurel MP1001 with an oxygen plasma was found most suitable to increase the hydrophilicity and to allow for efficient immobilization. Thus, for lipase B from Candida antarctica and for an esterase from Pyrobaculum calidifontis esterase (PestE) a 5‐fold and 14‐fold increase, respectively, in immobilization yield resulted compared to untreated carrier. In contrast to the oxygen‐modified support, modification of the polypropylene carrier with ammonia plasma showed no positive effect. Furthermore, it could be shown that immobilized PestE catalyzed enantioselective transesterification of α‐phenylethanol in vinyl acetate, whereas the free enzyme showed no activity. Both hydrolases could be recycled five times without significant loss of activity.