1998
DOI: 10.1023/a:1008867901427
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Cited by 13 publications
(32 citation statements)
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“…Formate ion does not influence activities of enzymes used in the proposed process. At present, only one enzyme is known (xylitol reductase [92]) that is inhibited by formate, and the inhibition constant (182 mM) is comparable with formate concentrations used in practice.…”
Section: Application Of Formate Dehydrogenasementioning
confidence: 94%
“…Formate ion does not influence activities of enzymes used in the proposed process. At present, only one enzyme is known (xylitol reductase [92]) that is inhibited by formate, and the inhibition constant (182 mM) is comparable with formate concentrations used in practice.…”
Section: Application Of Formate Dehydrogenasementioning
confidence: 94%
“…XRs from the yeasts Pichia stipitis and Candida tenuis are most popular for xylitol production; however, these enzymes have higher catalytic efficiencies toward L ‐arabinose than D ‐xylose (Table 1). 6, 7 Consequently, we decided that the recently isolated fungal XR from Neurospora crassa (NcXR) was a better choice for engineering due to its innate 2.4‐fold preference for D ‐xylose, high activity, and high expression level in E. coli 8. Semirational‐design approaches, targeted site‐saturation mutagenesis (TSSM), and combinatorial active‐site saturation testing (CASTing) have been successfully applied to shift the substrate specificity of the human estrogen receptor α LBD,9 and to alter enantioselectivity or substrate scope of lipases, respectively 10.…”
Section: Methodsmentioning
confidence: 99%
“…Under these optimum conditions, the highest conversion of NADH catalyzed by the encapsulated FateDH (both in pure polysaccharide capsules and hydroxyapatite-mineralized capsules) was up to 80.0%, which was a little higher than that of the enzymatic reaction catalyzed by free FateDH (78.0%). The enhancement of NADH conversion catalyzed by encapsulated FateDH could be tentatively attributed to confinement and partition effects, which could increase the local concentration of substrates and then shift the final reaction equilibrium toward the product [21]. The enzyme activity of both free and encapsulated FateDH was studied at various temperatures at pH 7.0, taking the highest activity of FateDH under its optimum condition to be 100% and the relative activity of FateDH defined as the ratio of its activity to the highest activity.…”
Section: Optimum Conditions For Enzyme Activitymentioning
confidence: 99%
“…In this work, hydroxyapatite-polysaccharide-FateDH composite capsules were utilized for efficient conversion of CO 2 into formic acid [19][20][21]. The capsules were produced by a one-step method in which the deposition of a semi-permeable alginate/chitosan membrane around droplets of sodium alginate was coupled with in …”
Section: Introductionmentioning
confidence: 99%