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Use of mono- and diacylglycerol lipase as immobilized fungal whole cells to convert residual partial glycerides enzymatically into fatty acid methyl esters
 

Use of mono- and diacylglycerol lipase as immobilized fungal whole cells to convert residual partial glycerides enzymatically into fatty acid methyl esters

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Use of mono- and diacylglycerol lipase as immobilized fungal whole cells to

Use of mono- and diacylglycerol lipase as immobilized fungal whole cells to
convert residual partial glycerides enzymatically into fatty acid methyl esters

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    Use of mono- and diacylglycerol lipase as immobilized fungal whole cells to convert residual partial glycerides enzymatically into fatty acid methyl esters Use of mono- and diacylglycerol lipase as immobilized fungal whole cells to convert residual partial glycerides enzymatically into fatty acid methyl esters Presentation Transcript

    • Speaker:XineYeah,Tang
    • Rhizopusoryzae producing triacylglycerollipase
      mono- and diacylglycerol lipase (mdlB) derived from Aspergillusoryzae.
    • Introduction
      R. oryzae, which originally produces a 1,3-position-specific triacylglycerol lipase, is one of the most studied fungi in lipase-catalyzed methanolysis
    • Studies by our group revealed that BSP-immobilized R. oryzae can efficiently catalyze the methanolysis with the addition of a certain amount of water , and that a packed-bed reactor (PBR) using BSPimmobilizedR. oryzae can be used for long-term repeated-batch methanolysis, with the methyl ester (ME) content around 80–90% during 10 batch cycles .
    • Mono- and diacylglycerol lipase is an enzyme that hydrolyzes MGandDG, but doesnothydrolyzetriglyceride (TG). Themono-and diacylglycerollipase-encoding genes have been cloned fromthefilamentous fungi, Penicilliumcamembertii (mdlA) and A. oryzae
      (mdlB) .
    • Materials and methods
      Two fungal strains, R. oryzae IFO4697 and A. oryzaeniaD300,were used.
      Reticulated polyurethane foam (Bridgestone Co. Ltd., Osaka, Japan) with a particle voidageofmore than 97% and a pore size of 50 pores per linear inch (ppi) was cut into 6mm×6mm×3mm cuboids for use asBSPs.
    • Construction of lipase expression vector and transformation of A. oryzae(skip)
    • Results and discussion
      Substrate specificity of mdlB
    • Effect of water content on methanolysis usingmdlB-producing A. oryzae
    • Composition of reaction mixtures in methanolysis usingmdlB-producing A. oryzae
    • Two-step batch methanolysis in PBR
    • Two-step batch methanolysis in PBR
    • Two-step batch methanolysis in PBR
    • Conclusions
      In this study, we attempted to use a mono- and diacylglycerol lipase to convert residual partial glycerides efficiently into their corresponding MEs. The newly developed mdlB-producing A.
    • The newly developed mdlB-producing A. oryzaeshowed an effective methanolysis activity toward MG and DG. In the presence of 5% water, the methanolysis of intermediate products using mdlB-producing A. resulting in less than 0.1% of MG and DG.
    • Ten repeated-batch methanolysiscycles in the PBR, containing both R. oryzae and mdlBproducing A. oryzae, maintained a high ME content of over 90% with MG and DG at 0.08–0.69 and 0.22–1.45%, respectively. These results indicate that the use of mdlB-producing A. oryzaeallows maintaining MG and DG at low levels during long-term repeatedbatchmethanolysis. We thus conclude that the proposed method is effective for improving enzymatic biodiesel production.