2018
DOI: 10.1016/j.enzmictec.2017.09.004
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Enzymatic esterification of eugenol and benzoic acid by a novel chitosan-chitin nanowhiskers supported Rhizomucor miehei lipase: Process optimization and kinetic assessments

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Cited by 42 publications
(25 citation statements)
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“…Literature has shown that this additional treatment transforms the lipase into a 'frozen' active state (open conformation) on the surface of the support [14]. Our observation is in agreement with similar studies of earlier researchers [34][35][36]. Subsequent protein loadings were lower as the supports were not pretreated with toluene.…”
Section: Effect Of Glutaraldehyde Concentrationsupporting
confidence: 91%
See 1 more Smart Citation
“…Literature has shown that this additional treatment transforms the lipase into a 'frozen' active state (open conformation) on the surface of the support [14]. Our observation is in agreement with similar studies of earlier researchers [34][35][36]. Subsequent protein loadings were lower as the supports were not pretreated with toluene.…”
Section: Effect Of Glutaraldehyde Concentrationsupporting
confidence: 91%
“…Toluene molecules bind to the hydrophobic lid of CRL and trigger the lid to open. This facilitates access of the substrates into the active site of the lipase, thereby resulting in higher lipase activity and immobilization efficiency [36]. The outcome seen in this study is consistent with the findings reported in the literature [37][38] for lipase immobilization that also uses a hydrophobic solvent to activate the lipase.…”
Section: Effect Of Glutaraldehyde Concentrationsupporting
confidence: 90%
“…This is because the temperature threshold was exceeded, hence the surplus breaking of the ionic, intramolecular hydrogen bonds, van der Waals forces and hydrophobic interactions that stabilizes the enzyme tertiary structure is heightened. These changes increase structural over-flexibility and disrupt the active conformation of the enzyme which lower activity of DehSN1 (Manan et al, 2018). On contrary, dehalogenase activity of DehSN1 was at its lowest at 50 °C (with enzyme specific activity 0.061 µmol CI¯/min/mg), which is probably because of the thermal deactivation of the DehSN1 dehalogenase protein structure.…”
Section: Characterization Of Dehsn1mentioning
confidence: 99%
“…Suitability of this mathematical and statistical tool has been established in a myriad of experimental trials for different processes. In fact, the BBD has been proven excellent for evaluating and observing influences, as well as interactions of multiple factors in any given process; benefits that are unseen in the one-variable-at-a-time technique [26][27]. Thus, the objective of this study was to seek the best aforementioned UAE conditions for maximizing the extraction yield and total phenolic content of E. guineensis leaves extract.…”
Section: ■ Introductionmentioning
confidence: 99%