Abstract：
:Proleather from Bacillus sp. was chemically modified with decanoyl chloride for enhanced activity for the preparation of poly(lactic acid) in organic solvents. The modified enzyme was highly soluble (up to 44 mg-protein/ml) and active in various organic solvents including chloroform, tetrahydrofuran (THF), pyridine and acetone. The organic-soluble proleather efficiently catalyzed the polymerization of ethyl lactate. The reaction rate was 4-22 times that of native proleather, depending upon the solvent applied. The solubilized enzyme showed a highest activity at 50 degrees C, the same optimum temperature for both the native proleather and an immobilized enzyme, Novozyme-435. Denaturation of the enzymes' protein structures appeared to be the critical factor regulating the optimum activity temperature. Differential scanning calorimetry (DSC) analyses of the enzymes showed endothermic peaks around 55 degrees C, indicating the proteins' structures altered in that temperature range. Interestingly, the activity of the solubilized enzyme showed a more complicated water dependence as compared to native proleather.
journal_name
Bioresour Technoljournal_title
Bioresource technologyauthors
Distel KA,Zhu G,Wang Pdoi
10.1016/j.biortech.2004.06.005subject
Has Abstractpub_date
2005-03-01 00:00:00pages
617-23issue
5eissn
0960-8524issn
1873-2976pii
S0960-8524(04)00228-7journal_volume
96pub_type
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