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Immobilization of enzyme using natural feldspar for use in the synthesis of oleyl oleate

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dc.Conferencecode137127
dc.Conferencedate7 November 2017 through 8 November 2017
dc.ConferencenameInternational Conference on Recent Advancements in Science and Technology 2017, ICoRAST 2017
dc.contributor.affiliationsFaculty of Science and Technology
dc.contributor.affiliationsInstitute of Halal Research and Management (IHRAM)
dc.contributor.affiliationsUniversiti Sains Islam Malaysia (USIM)
dc.contributor.affiliationsUniversiti Putra Malaysia (UPM)
dc.contributor.authorAli B.J.en_US
dc.contributor.authorOthman S.S.en_US
dc.contributor.authorHarun F.W.en_US
dc.contributor.authorJumal J.en_US
dc.contributor.authorRahman M.B.A.en_US
dc.date.accessioned2024-05-28T08:25:43Z
dc.date.available2024-05-28T08:25:43Z
dc.date.issued2018
dc.description.abstractNatural feldspar from Tanah Putih, Gua Musang, Kelantan (Malaysia) was physico-chemically characterized using X-ray Diffraction (XRD), Surface Area and Porosity Analysis (ASAP) and Energy Dispersive X-ray (EDX) techniques. The feldspar was found to be of the potassium (K) type, with major components containing aluminum (Al), and silicon (Si). The feldspar also possesses 38.307 nm mean pore diameter and 18.717 m2/g surface area. Candida rugosa (CRL) was then immobilized onto natural feldspar by physical adsorption method. About 49.96% of protein content was immobilized onto the support. The catalytic activity of the immobilized lipase was determined by the esterification reaction using oleic acid and oleyl alcohol. The effects of various reaction temperatures, stability in organic solvent, and lipase recyclability on the esterification reaction for the native and immobilized lipase were investigated. Feldspar-immobilized lipase exhibited higher activity than that of the native lipase. Immobilized lipase retained its activity ca. 50% even after incubation at high temperature (70°C) with the optimum reaction temperature of 40°C, long incubation in hexane up to 10 days and after ten repeated cycles used. Feldspar-immobilized lipase also showed considerably efficient reusability where it was not easily leached even after being washed with large amount of hexane (20 mL). These results showed that physical adsorption method is suitable for the immobilization of lipase onto feldspar.en_US
dc.description.natureFinalen_US
dc.editorAli E.S.Yatim N.M.Harun F.W.en_US
dc.identifier.doi10.1063/1.5041239
dc.identifier.isbn9780740000000
dc.identifier.issn0094243X
dc.identifier.scopus2-s2.0-85048892445
dc.identifier.urihttps://www.scopus.com/inward/record.uri?eid=2-s2.0-85048892445&doi=10.1063%2f1.5041239&partnerID=40&md5=d05564fdd0855d6c34cdc8197fa75e6f
dc.identifier.urihttps://oarep.usim.edu.my/handle/123456789/8674
dc.identifier.volume1972
dc.languageEnglish
dc.language.isoen_USen_US
dc.publisherAmerican Institute of Physics Inc.en_US
dc.relation.ispartofOpen Accessen_US
dc.relation.ispartofAIP Conference Proceedings
dc.sourceScopus
dc.titleImmobilization of enzyme using natural feldspar for use in the synthesis of oleyl oleateen_US
dc.title.alternativeAIP Conf. Proc.en_US
dc.typeConference Paperen_US
dspace.entity.typePublication

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