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Immobilizing Systems Biocatalysis for the Selective Oxidation of Glycerol Coupled to In Situ Cofactor Recycling and Hydrogen Peroxide Elimination
Author(s) -
RochaMartin Javier,
Acosta Andreína,
Guisan Jose M.,
LópezGallego Fernando
Publication year - 2015
Publication title -
chemcatchem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.497
H-Index - 106
eISSN - 1867-3899
pISSN - 1867-3880
DOI - 10.1002/cctc.201500210
Subject(s) - chemistry , cofactor , nad+ kinase , glycerol , biocatalysis , glycerol 3 phosphate dehydrogenase , redox , dehydrogenase , hydrogen peroxide , alcohol dehydrogenase , oxidizing agent , dihydroxyacetone , formate dehydrogenase , oxidase test , disproportionation , enzyme , organic chemistry , catalysis , reaction mechanism
The combination of three different enzymes immobilized rationally on the same heterofunctional carrier allowed the selective oxidation of glycerol to 1,3‐dihydroxyacetone (DHA) coupled to in situ redox‐cofactor recycling and H 2 O 2 elimination. In this cascade, engineered glycerol dehydrogenase with reduced product inhibition oxidized glycerol selectively to DHA with the concomitant reduction of NAD + to NADH. NADH oxidase regenerated the NAD + pool by oxidizing NADH to NAD + to form H 2 O 2 as the byproduct. Finally, catalase eliminated H 2 O 2 to yield water and O 2 as innocuous products, which avoided the spontaneous DHA oxidation triggered by H 2 O 2 . The co‐immobilization of the three enzymes on the same porous carrier allowed the in situ recycling and disproportionation of the redox cofactor and H 2 O 2 , respectively, to produce up to 9.5 m M DHA, which is 18‐ and 6‐fold higher than glycerol dehydrogenase itself and a soluble multienzyme system, respectively.