Journal
APPLIED CATALYSIS A-GENERAL
Volume 478, Issue -, Pages 175-185Publisher
ELSEVIER
DOI: 10.1016/j.apcata.2014.03.034
Keywords
Lipase; Immobilization; Catalytic efficiency; Fe-MCM-41; Biodiesel
Categories
Funding
- National twelfth five-year science and technology [2011BAD14805, 2013BAD10B01, 2014BAD02B02]
- Sichuan Science and Technology Bureau [2013GZ0058, 2012GZ0008]
- National Natural Science Foundation of China [31171447, J1103518]
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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 4h). 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. (C) 2014 Elsevier B.V. All rights reserved.
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