Optically pure (

R

)-

γ

- and (

R

)-

δ

-lactones can be prepared by intramolecular cyclization of chiral hydroxy acids/esters reduced asymmetrically from γ- and δ-keto acids/esters using

Saccharomyces cerevisiae

(

S. cerevisiae

) as a whole-cell biocatalyst. However

some of the enzymes catalyzing these reactions in

S. cerevisiae

are still unknown up to date. In this report

two carbonyl reductases

OdCR1 and OdCR2

were successfully discovered

and cloned from

S. cerevisiae

using a genome-mining approach

and overexpressed in

Escherichia coli

(

E. coli

). Compared with OdCR1

OdCR2 can reduce 4-oxodecanoic acid and 5-oxodecanoic acid asymmetrically with higher stereoselectivity

generating (

R

)-

γ

-decalactone (99% ee) and (

R

)-

δ

-decalactone (98%

ee

) in 85% and 92% yields

respectively. This is the first report of native enzymes from

S. cerevisiae

for the enzymatic synthesis of chiral γ- and δ-lactones which is of wide uses in food and cosmetic industries.