A purified thermo-tolerant lipase of Streptomyces STL-D8 was immobilized onto the natural fibres namely
‘Bombax’. Hydrolytic activity of this fibre-bound lipase was determined for hydrolysis of p-NPP in a 0.05 M Tris buffer
(pH 8.5) at 55°C. This fibre-bound lipase was used to synthesize methyl succinate using methanol and succinic acid as
reactants in DMSO at 55°C under shaking. Although a low yield of methyl succinate was observed in reaction mixture at
16 h (14.3 mM) yet the yield of methyl succinate was improved by optimizing molar ratio of reactants to 75 mM: 100 mM
(succinic acid: methanol) in DMSO. Molecular sieves added to the reaction system at a concentration of 30 mg/2 mL
increased the synthesis of methyl succinate from 30.0 mM to 31.4 mM. The volumetric scale up of the reaction system to
10 and 50 mL produced more or less a similar yield (29.1 mM to 27.9 mM) of methyl succinate after 16 h of reaction.
Methyl succinate is a therapeutic molecule that has insulin sensitizing property comparable to that of glucose.
Keywords: Streptomyces sp. STL-D8, lipase, natural fibres, methyl succinate, immobilized biocatalyst, DMSO.
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