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Rationally designed Fe-MCM-41 by protein size to enhance lipase immobilization, catalytic efficiency and performance

Paper ID Volume ID Publish Year Pages File Format Full-Text
39686 45831 2014 11 PDF Available
Title
Rationally designed Fe-MCM-41 by protein size to enhance lipase immobilization, catalytic efficiency and performance
Abstract

•Modification of adsorbents based on enzyme protein properties is promising.•The relative activity of immobilized lipase reached 197% compared to free enzyme.•Biofuel production catalyzed by immobilized lipase yields 98% conversion at 4 h.•The incorporation of Fe improves the catalytic performance of immobilized lipase.

A three-dimensional structure of lipase protein was constructed by using homology modeling. Six different Fe-MCM-41 carriers were synthesized with different pore size based on the properties of the lipase examined. The relative activity of lipase from Yarrowia lipolytica (YYL) immobilized on Fe-MCM-41 with a pore size of 4.27 nm (FM-4-YYL) reached 197% when compared with free lipase. This result was notably higher than that of YYL encapsulated in other forms of Fe-MCM-41. Moreover, FM-4-YYL has excellent thermal stability in that it can preserve nearly 80% of the initial activity after incubation at 60 °C for 1 h. In addition, immobilized lipases were used as catalysts for the transesterification of olive oil with methanol. The highest conversion yield (98%) was observed when FM-4-YYL was used as a biocatalyst for biodiesel (10 mL olive oil, 1.66 mL methanol, and 1.5 mL water at 30 °C for 4 h). FM-4-YYL can be reused for nine cycles without significant loss in activity. The work demonstrates that the selection and modification of adsorbents based on enzyme protein properties is a very promising strategy for increasing stability and enhancing active the performance of biocatalysts for industrial production.

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Keywords
Lipase; Immobilization; Catalytic efficiency; Fe-MCM-41; Biodiesel
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Rationally designed Fe-MCM-41 by protein size to enhance lipase immobilization, catalytic efficiency and performance
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Publisher
Database: Elsevier - ScienceDirect
Journal: Applied Catalysis A: General - Volume 478, 20 May 2014, Pages 175–185
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Catalysis
Get Full-Text Now
Don't Miss Today's Special Offer
Price was $35.95
You save - $31
Price after discount Only $4.95
100% Money Back Guarantee
Full-text PDF Download
Online Support
Any Questions? feel free to contact us