Abstract：
:Rhizopus chinensis produces two lipases that catalyze ester synthesis when cultured under solid-state fermentation. The Lip2 was purified to homogeneity by ammonium sulphate precipitation, hydrophobic interaction chromatography and gel filtration chromatography. It has an apparent molecular weight of 33 kDa estimated from SDS-PAGE and 32 kDa calculated from analytical gel permeation, with synthetic activity and purification fold of 96.8 U/mg and 138.3, respectively. Maximum hydrolytic activity was obtained at pH 8.0-8.5 and 40 degrees C using pNPP as substrate. Slight activation of the enzyme was observed when Mn(2+) is present. The enzyme was most active on p-nitrophenyl laurate (C12). The purified lipase exhibited maximum synthetic activity at pH memory of 6.0 and 30 degrees C. Most of ethyl esters synthesized by lyophilized enzyme achieved good yields (>90%), and caprylic acid served as the best acyl donor. The enzyme presented a particular affinity for ethanol, n-propanol and n-hexanol, with conversion of 92%, 93% and 92%, respectively, after 20 h incubation.
journal_name
Bioresour Technoljournal_title
Bioresource technologyauthors
Sun SY,Xu Y,Wang Ddoi
10.1016/j.biortech.2008.11.006subject
Has Abstractpub_date
2009-05-01 00:00:00pages
2607-12issue
9eissn
0960-8524issn
1873-2976pii
S0960-8524(08)00962-0journal_volume
100pub_type
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