Abstract:
:Alginate was evaluated as an immobilization matrix for enzyme-catalyzed reactions in organic solvents. In contrast to most hydrogels, calcium alginate was found to be stable in a range of organic solvents and to retain the enzyme inside the gel matrix. In hydrophobic solvents, the alginate gel (greater than 95% water) thus provided a stable, two-phase liquid system. The lipase from Candida cylindracea, after immobilization in alginate beads, catalysed esterification and transesterification in n-hexane under both batch and continuous-flow conditions. The operational stability of the lipase was markedly enhanced by alginate entrapment. In the esterification of butanoic acid with n-butanol, better results were obtained in the typical hydrophilic calcium alginate beads than in less hydrophilic matrices. The effects of substrate concentration, matrix area, and polarity of the substrate alcohols and of the organic solvent on the esterification activity were examined. The transesterification of octyl 2-bromopropanoate with ethanol was less efficient than that of ethyl 2-bromopropanoate with octanol. By using the hydrophilic alginate gel as an immobilization matrix in combination with a mobile hydrophobic phase, a two-phase liquid system was achieved with definite advantages for a continuous, enzyme-catalysed process.
journal_name
Enzyme Microb Technoljournal_title
Enzyme and microbial technologyauthors
Hertzberg S,Kvittingen L,Anthonsen T,Skjåk-Braek Gdoi
10.1016/0141-0229(92)90024-ikeywords:
subject
Has Abstractpub_date
1992-01-01 00:00:00pages
42-7issue
1eissn
0141-0229issn
1879-0909pii
0141-0229(92)90024-Ijournal_volume
14pub_type
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journal_title:Enzyme and microbial technology
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journal_title:Enzyme and microbial technology
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更新日期:2000-05-01 00:00:00
abstract::The primary aim of this study was to decipher the catalytic functions of the NHase with wide substrate spectra from Rhodococcus ruber CGMCC3090 by computer modeling and substrate docking. 3D structure model of the enzyme was built by computer modeling to obtain the optimal structure. The larger binding site cavity (55...
journal_title:Enzyme and microbial technology
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doi:10.1016/j.enzmictec.2012.11.004
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journal_title:Enzyme and microbial technology
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journal_title:Enzyme and microbial technology
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journal_title:Enzyme and microbial technology
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abstract::2,5-Bis(hydroxymethyl)furan (BHMF) is a versatile building block in the synthesis of polymers, fuels, and macrocycle polyethers. In this work, alcohol dehydrogenases (ADHs) were identified from Meyerozyma guilliermondii SC1103 and were heterologously expressed in Saccharomyces cerevisiae for the synthesis of BHMF from...
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journal_title:Enzyme and microbial technology
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journal_title:Enzyme and microbial technology
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journal_title:Enzyme and microbial technology
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journal_title:Enzyme and microbial technology
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abstract::Horseradish peroxidase (HRP) was successfully purified from horseradish roots by a two-stage reverse-micellar extraction from the dialyzed aqueous extract. The anionic surfactant AOT dissolved in isooctane was used to produce the reverse-micellar phases. The narrow pH range at which HRP solubilization occurred was exp...
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