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n‐Hexanol Formation from n‐Hexanal by Enzyme Action in Soybean Extracts
Author(s) -
MATOBA TERUYOSHI,
SAKURAI ATSUKO,
TANINOKI NARIKO,
SAITOH TOMOKO,
KARIYA FUYU,
KUWAHATA MARI,
YUKAWA NATSUKO,
FUJINO SACHIYO,
HASEGAWA KIYOZO
Publication year - 1989
Publication title -
journal of food science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.772
H-Index - 150
eISSN - 1750-3841
pISSN - 0022-1147
DOI - 10.1111/j.1365-2621.1989.tb05171.x
Subject(s) - hexanal , cofactor , nad+ kinase , chemistry , incubation , nicotinamide adenine dinucleotide , enzyme , nicotinamide adenine dinucleotide phosphate , nicotinamide , dehydrogenase , biochemistry , flavoprotein , alcohol dehydrogenase , chromatography , oxidase test
n‐Hexanal in soybean homogenates decreased during incubation at alkaline pH. When soybean extracts were dialyzed and then incubated with n‐hexanal and cofactors [nicotinamide adenine dinucleotide (NAD + ), the reduced form (NADH), nicotinamide adenine dinucleotide phosphate (NADP+), and the reduced form (NADPH)], NADH and NADPH stimulated the enzymatic reduction of n‐hexanal with NADH being more effective than NADPH. When undialyzed preparations were incubated, all the cofactors stimulated enzymatic activity, with NADH being the most effective. The reaction product in all the incubation mixtures was n‐hexanol; n‐hexanal was reduced to n‐hexanol stoichiometrically. It was suggested that alcohol dehydrogenase was responsible for the decrease of n‐hexanal in soybean homogenate at alkaline pH.