Enantio- & chemo-selective preparation of enantiomerically enriched aliphatic nitro alcohols using Candida parapsilosis ATCC 7330

RSC Advances ◽  
2015 ◽  
Vol 5 (90) ◽  
pp. 73807-73813 ◽  
Author(s):  
Sowmyalakshmi Venkataraman ◽  
Anju Chadha
Keyword(s):  
Candida Parapsilosis ◽  
Asymmetric Reduction ◽  
Reaction Conditions ◽  
Enantiomerically Pure ◽  
Candida Parapsilosis Atcc 7330

Enantiomerically pure β- and γ-nitro alcohols were prepared from their respective nitro ketones by asymmetric reduction using Candida parapsilosis ATCC 7330 under optimized reaction conditions (ee up to >99%; yields up to 76%).

scholarly journals Understanding (R) Specific Carbonyl Reductase from Candida parapsilosis ATCC 7330 [CpCR]: Substrate Scope, Kinetic Studies and the Role of Zinc

Catalysts ◽  
2019 ◽  
Vol 9 (9) ◽  
pp. 702 ◽  
Author(s):  
Karanam ◽  
Chaudhury ◽  
Chadha
Keyword(s):  
Candida Parapsilosis ◽  
Asymmetric Reduction ◽  
Kinetic Studies ◽  
Aromatic Aldehydes ◽  
Carbonyl Reductase ◽  
Rate Of Reaction ◽  
Reaction Change ◽  
Candida Parapsilosis Atcc 7330 ◽  
Reduction Of Ketones

CpCR, an (R) specific carbonyl reductase, so named because it gave (R)-alcohols on asymmetric reduction of ketones and ketoesters, is a recombinantly expressed enzyme from Candida parapsilosis ATCC 7330. It turns out to be a better aldehyde reductase and catalyses cofactor (NADPH) specific reduction of aliphatic and aromatic aldehydes. Kinetics studies against benzaldehyde and 2,4-dichlorobenzaldehyde show that the enzyme affinity and rate of reaction change significantly upon substitution on the benzene ring of benzaldehyde. CpCR, an MDR (medium chain reductase/dehydrogenase) containing both structural and catalytic Zn atoms, exists as a dimer, unlike the (S) specific reductase (SRED) from the same yeast which can exist in both dimeric and tetrameric forms. Divalent metal salts inhibit the enzyme even at nanomolar concentrations. EDTA chelation decreases CpCR activity. However, chelation done after the enzyme is pre-incubated with the NADPH retains most of the activity implying that Zn removal is largely prevented by the formation of the enzyme-cofactor complex.

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