Biochemical and biophysical characterisation of a small purified lipase from Rhizopus oryzae ZAC3

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dc.contributor.authorAyinla, Zainab Adenike
dc.contributor.authorAdemakinwa, Adedeji Nelson
dc.contributor.authorGross, Richard A.
dc.contributor.authorAgboola, Femi K.
dc.date.accessioned2021-02-17T11:52:29Z
dc.date.available2021-02-17T11:52:29Z
dc.date.issued2021-02-08
dc.descriptionStaff Publicationsen_US
dc.description.abstractThe characteristics of a purified lipase from Rhizopus oryzae ZAC3 (RoL-ZAC3) were investigated. RoL-ZAC3, a 15.8 kDa protein, which was optimally active at pH 8 and 55 °C had a half-life of 126 min at 60 °C. The kinetic parameters using p-nitrophenylbutyrate as substrate were 0.19 ± 0.02 mM, 126 ± 5.6 U/ml and 122 s−1 for Km , V max and k cat respectively. RoL-ZAC3 showed stability in methanol and isopropanol with Na+ enhancing the activity. p-nitrophenyloleate and castor oil were the best preferred substrates among the p-nitrophenyl esters and vegetable oils tested respectively. About 43% residual activity was observed after incubation for 30 min at 75 °C. Circular dichroism thermal scan showed that the lipase displayed intense negative ellipticities even at high temperature. Perturbation of the tertiary structure with increasing temperature caused the exposure of hydrophobic side chains to the aqueous environment as revealed by tryptophan fluorescence, with a t−Tm of 50 °C. Differential scanning calorimetry analysis showed melting temperature and calorimetric enthalpy of 55.5 °C and 444 kJ/mol respectively. Dynamic light scattering analysis indicated that the lipase was prone to aggregation upon unfolding at high temperature. It can be concluded that RoL-ZAC3 possesses promising potential for numerous biotechnological applications.en_US
dc.identifier.citationZainab A. Ayinla, Adedeji N. Ademakinwa, Richard A. Gross & Femi K. Agboola (2021) Biochemical and biophysical characterisation of a small purified lipase from Rhizopus oryzae ZAC3, Biocatalysis and Biotransformation, DOI: 10.1080/10242422.2021.1883006en_US
dc.identifier.urihttps://doi.org/10.1080/10242422.2021.1883006
dc.identifier.urihttp://repository.elizadeuniversity.edu.ng/handle/20.500.12398/866
dc.language.isoenen_US
dc.publisherTaylor and Francis Onlineen_US
dc.subjectLipase,en_US
dc.subjectRhizopus oryzaeen_US
dc.subjecttryptophan fluorescenceen_US
dc.subjectcircular dichroismen_US
dc.subjectcalorimetric enthalpyen_US
dc.titleBiochemical and biophysical characterisation of a small purified lipase from Rhizopus oryzae ZAC3en_US
dc.typeArticleen_US
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