• Biotechnology and Bioprocess Engineering:BBE
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• v.7 no.3
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• pp.130-137
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• 2002

Microbial lactonohydrolases (intramolecular ester bond-hydrolyzing enzymes) with unique properties were found. The lactonohydrolase from Fusarium oxysporum catalyzes enantiose-lective hydrolysis of aldonate lactones and D-pantoyl lactone (D-PL). This enzyme is useful for the large-scale optical resolution of racemic PL. The Agrobacterium tumefaciens enzyme catalyzes asymmetric hydrolysis of PL, but the stereospecificity is opposite to that of the Fusarium enzyme. Dihydrocoumarin hydrolase (DHase) from Acinetobacter calcoaceticus is a bifunctional enzyme, which catalyzes not only hydrolysis of aromatic lactones but also bromination of monochlorodi-medon in the presence of H$_2$O$_2$and dihydrocoumarin. DHase also hydrolyzes several linear esters, and is useful for enantioselective hydrolysis of methyl DL-$\beta$-acetylthioisobutyrate and regioselective hydrolysis of methyl cetraxate.

• Bulletin of the Korean Chemical Society
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• v.32 no.1
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• pp.65-70
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• 2011

Coumarins are ubiquitous in plant kingdom and have been used as antitumor, antifungals, anticoagulants, insecticides. Chalcones are also widespread in plant kingdom and have been known to possess diverse biological activities; antibacterial, antifungal, antitumor and anti-inflammatory, etc. As they are considered as important natural products, numerous synthetic approaches have been reported up to the present. We devise a new selective method of preparing dihydrocoumarins and chalcones from aryl cinnamates by the selection of reagents. Dihydrocoumarin derivatives were prepared selectively by using intramolecular cyclization catalyzed by p-toluene sulfonic acid. Also, chalcones were prepared by Fries-rearrangement catalyzed by $TiCl_4$. This method can be used for preparing various coumarin & chalcone compounds.

• Journal of Microbiology and Biotechnology
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• v.22 no.6
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• pp.832-837
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• 2012

The oxidative potential of the fungus Penicillium brasilianum, a strain isolated as endophytic from a Meliaceae plant (Melia azedarach), was investigated using 1-indanone as substrate to track the production of monooxygenases. The fungus produced the dihydrocoumarin from 1-indanone with the classical Baeyer-Villiger reaction regiochemistry, and (-)-(R)-3-hydroxy-1-indanone with 78% ee. Minor compounds that had resulted from lipase and SAM activities were also detected. The biotransformation procedures were also applied using a collection of Penicillium and Aspergillus fungi obtained from M. azedarach and Murraya paniculata. The results showed that Baeyer-Villiger were mostly active in fungi isolated from M. azedarach. Almost all fungi tested produced 3-hydroxy-1-indanone.