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Development of a silica monolith microbioreactor entrapping highly activated lipase and an experiment toward integration with chromatographic separation of chiral esters
Author(s) -
Kawakami Koei,
Abe Daisuke,
Urakawa Taiki,
Kawashima Ayako,
Oda Yasuhiro,
Takahashi Ryo,
Sakai Shinji
Publication year - 2007
Publication title -
journal of separation science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.72
H-Index - 102
eISSN - 1615-9314
pISSN - 1615-9306
DOI - 10.1002/jssc.200700309
Subject(s) - monolith , methyltrimethoxysilane , lipase , chromatography , chemistry , monolithic hplc column , immobilized enzyme , transesterification , organic chemistry , high performance liquid chromatography , coating , catalysis , enzyme
Microbioreactors are effective for high‐throughput production of expensive products from small amounts of substrates. Lipases are versatile enzymes for chiral syntheses, and are highly activated when immobilized in alkyl‐substituted silicates by the sol–gel method. For practical application of sol–gel immobilized lipases to a flow system, a microbioreactor loaded with a macroporous silica monolith is well suited, because it can be easily integrated with a chromatographic separator for optical resolution. We attempted to develop a microbioreactor containing a silica monolith‐immobilized lipase. A nonshrinkable silica monolith was first formed from a 4:1 mixture of methyltrimethoxysilane (MTMS) and tetramethoxysilane (TMOS). It was then coated with silica precipitates entrapping lipase, derived from a 4:1 mixture of n ‐butyltrimethoxysilane (BTMS) and TMOS. As a result, monolith treated with the BTMS‐based silicate entrapping lipase exhibited approximately ten times higher activity than nontreated monolith‐immobilized lipase derived from the MTMS‐based silicate, in transesterification between glycidol and vinyl n ‐butyrate in isooctane. A commercially available chiral column was connected in series to the monolith microbioreactor, and a pulse of substrate solution was supplied at the inlet of the reactor. Successful resolution of the racemic ester produced was achieved in the chromatographic column.