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Applied Biochemistry and Biotechnology
Volumn 14, Issue 2, 1987, Pages 147-197
Regeneration of nicotinamide cofactors for use in organic synthesis
Author keywords

enzymes, dehydrogenases; nicofinamide cofactors, preparation of; nicotinamide cofactors; nicotinamide cofactors, and organic synthesis; Nicotinamide cofactors, regeneration of; organic synthesis; regeneration; stability
Indexed keywords

NICOTINAMIDE ADENINE DINUCLEOTIDE; NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; OXIDOREDUCTASE;
EID: 0345817539     PISSN: 02732289     EISSN: 15590291     Source Type: Journal    
DOI: 10.1007/BF02798431     Document Type: Review
Times cited : (558)
References (233)
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    • Calculations are based on initial reactor conditions reported in references cited by this paper. Typically, in batch reactors, the total concentration of nicotinamide cofactor is on the order of the sum of the Michaelis constants for NAD(P) and NAD(P)H of the oxidizing and reducing enzymes, respectively. Such concentrations provide an efficient compromise between maximal utilization of enzymatic activity (optimizing V/Vmax) and maximal utilization of cofactor (optimizing TTN). Values for KNAD tend to be on the order of 0.1 mM, and values for Knadh tend to be on the order of 0.01 mM (13,45). Thus, KNAD/KNADH is approximately 10. For coupled enzymes having 5 ≤ Knad/KNadh ≤ 10 and that differ in cost by no more than two orders of magnitude, the calculated total cost of enzyme per unit rate of product formation reaches a minimum when the oxidizing and reducing enzymes are present with relative activities of from 5:1 to 1:5 (71). When the relative enzyme activities are set so as to minimize the cost of enzyme per unit rate of product formation, these systems also give calculated values of [NAD]/([NAD] + [NADH]), which are generally in the range of 0.20-0.95.
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* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.