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You searched for: Journal name Process biochemistry Remove constraint Journal name: Process biochemistry Publication Year 2019 Remove constraint Publication Year: 2019 Subject epoxides Remove constraint Subject: epoxides
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1. Immobilized feruloyl esterase from Humicola insolens catalyzes the synthesis of feruloylated oligosaccharides

Author:
Juan Tamayo-Cabezas; Salwa Karboune
Source:
Process biochemistry 2019 v.79 pp. 81-90
ISSN:
1359-5113
Subject:
Humicola insolens; acylation; catalytic activity; emulsions; epoxides; ferulic acid; feruloyl esterase; magnetism; microparticles; nanoparticles; raffinose; substrate specificity
Abstract:
... Ferulic acid acylation of oligosaccharides catalyzed by feruloyl esterases (FAE) is a promising route to produce feruloylated oligosaccharides. However, modulation of FAE synthetic properties is a key step to improve the acylation. The efficiency of H. insolens FAE to catalyze the feruloylation in six different surfactantless microemulsions reaction systems was evaluated. The highest yield (57%) w ...
DOI:
10.1016/j.procbio.2018.12.013

2. Modulation of Lecitase properties via immobilization on differently activated Immobead-350: Stabilization and inversion of enantiospecificity

Author:
Maísa P. Pinheiro; Rodolpho R.C. Monteiro; Francisco F.M. Silva; Telma L.G. Lemos; Roberto Fernandez-Lafuente; Luciana R.B. Gonçalves; José C.S. dos Santos
Source:
Process biochemistry 2019 v.87 pp. 128-137
ISSN:
1359-5113
Subject:
acetates; acetonitrile; biocatalysts; butyrates; catalytic activity; enzymes; epoxides; hydrolysis; pH
Abstract:
... Lecitase Ultra (Leci) was immobilized on Immobead-350 (IB-350) activated with epoxy (EPO), amino-divinylsulfone (DVS) or amino-glutaraldehyde (GLU) groups. Leci-GLU had 27% more activity versus p-nitro-phenyl butyrate (p-NPB) than Leci-EPO, after 3 h of immobilization using 100 mg of enzyme/g of support (immobilization yield was 84.1%, expressed activity versus p-NPB was around 10%), the covalent ...
DOI:
10.1016/j.procbio.2019.08.016

3. Overexpression of epoxide hydrolase in Rhodococcus ruber with high robustness for the synthesis of chiral epichlorohydrin

Author:
Youxiang Liang; Song Jiao; Miaomiao Wang; Huimin Yu; Zhongyao Shen
Source:
Process biochemistry 2019 v.79 pp. 49-56
ISSN:
1359-5113
Subject:
Agrobacterium radiobacter; Escherichia coli; Rhodococcus ruber; biocatalysts; enantiomers; epichlorohydrins; epoxide hydrolase; epoxides; glycols; pH; proteins; thermal stability
Abstract:
... Epoxide hydrolases (EHs) are attractive enzymes for producing enantiopure epoxides and diols, but do not display enough stability when lysates or Escherichia coli whole cells are used as biocatalysts. In this work, an organic-solvent tolerant strain Rhodococcus ruber THdAdN was utilized to overexpress an epoxide hydrolase from Agrobacterium radiobacter (ArEH), using E. coli BL21(DE3) as a control. ...
DOI:
10.1016/j.procbio.2018.12.023