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Chiral Resolution Function with Immobilized Food Proteins
Author(s) -
Nagaoka Hiroyuki
Publication year - 2008
Publication title -
biotechnology progress
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 129
eISSN - 1520-6033
pISSN - 8756-7938
DOI - 10.1021/bp034059w
Subject(s) - nad+ kinase , chemistry , reagent , substrate (aquarium) , stereoselectivity , alcohol dehydrogenase , kinetic resolution , catalysis , calcium alginate , regioselectivity , aryl , alcohol , organic chemistry , stereochemistry , enzyme , enantioselective synthesis , calcium , biology , ecology , alkyl
We confirmed that an NAD(P)+‐dependent secondary alcohol dehydrogenase (NAD(P)‐E) can be easily and effectively isolated from pea, soybean, and wheat proteins immobilized with calcium alginate gel (IPP, ISP, and IWP, respectively). The estimated molecular mass of NAD(P)‐E is 138.7 kDa, and the concentrations of NAD(P)‐E in solution are 36.2 (IPP), 53.9 (ISP), and 93.7 (IWP) μg/mL. The NAD(P)‐E oxidizes only ( R )‐isomers highly enantioselectively; thus, greater than 99% ee(s) of ( S )‐isomers can be obtained from corresponding rac ‐aryl methyl carbinols ( 1 , 2a – 6a , and 2b – 7b ). The amount of food protein needed for 1 g of substrate (B/S ratio) is approximately 20. Thus, in comparison to current biocatalysts, certain food proteins can serve as asymmetric reagent bases, providing easily obtained, low‐cost natural catalysts with stereoselectivity, regioselectivity, and substrate specificity that work under mild conditions for asymmetric synthesis of organic compounds. Moreover, this “fourth” function of food may help build a sustainable society by synthesizing optically active secondary alcohols in an environmentally friendly manner.