Please use this identifier to cite or link to this item: http://hdl.handle.net/11455/41165
標題: Production of D-amino acid precursors with permeabilized recombinant Escherichia coli with D-hydantoinase activity
作者: Yin, B.D.
林松池
Chen, Y.C.
Lin, S.C.
Hsu, W.H.
關鍵字: Escherichia coli;immobilization;permeabilization;D-hydantoinase;calcium alginate;microbial transformation;pseudomonas-putida;calcium alginate;agrobacterium sp;microorganisms;immobilization;expression;gene
Project: Process Biochemistry
期刊/報告no:: Process Biochemistry, Volume 35, Issue 9, Page(s) 915-921.
摘要: 
Recombinant Escherichia coil cells expressing D-hydantoinase were used as the biocatalysts for the production of N-carbamoyl-D-hydroxyphenylglycine from DL-p-hydroxyphenylhydantoin. Although high concentrations of DMSO could lead to enzyme denaturation, in the presence of 1.5% DMSO, the rate of product formation increased by more than 80% due to enhanced permeability of the cell membrane and increased substrate concentration. Reduced mass transfer resistance, achieved by the permeabilization of cell membrane with CTAB and glutaraldehyde, led to a 60% increase in the rate of production. However, in addition to causing a shift of optimal pH toward lower pH, permeabilization of the cell membrane resulted in reduced enzyme stability toward thermal and organic denaturation. Nevertheless, the stability of the D-hydantoinase of the recombinant cells toward pH, temperature and organic solvents can be significantly enhanced by immobilization. (C) 2000 Elsevier Science Ltd. All rights reserved.
URI: http://hdl.handle.net/11455/41165
ISSN: 0032-9592
DOI: 10.1016/s0032-9592(99)00157-0
Appears in Collections:化學工程學系所

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