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Lipase Immobilization
Published in Sulaiman Al-Zuhair, Hanifa Taher, Supercritical Fluids Technology in Lipase Catalyzed Processes, 2016
Sulaiman Al-Zuhair, Hanifa Taher
Selectivity improvement is a critical requirement for industrial applications of lipase. This includes substrate selectivity, stereoselectivity, regioselectivity, and enantio-selectivity. Adsorption of Candida rugosa on celite was reported to enhance the stability of lipase and improve its enantioselectivity up to 3-fold (Ogino, 1970). Entrapment in cellulose acetate–TiO2 gel fiber improved the selectivity of Rhizomucor miehei lipase in the hydrolysis of 1,2-diacetoxypropane (Ikeda and Kurokawa, 2001). Also the enantioselectivity of pegylated P. cepacea lipase was increased 3-fold by entrapment in Ca-alginate gel beads (Palomo et al., 2003). Physical immobilization of C. antarctica lipase B by adsorption onto octadecyl-Sepabeads (hydrophobic support) did not show any appreciable enantioselectivity. However, the covalent immobilization onto the glutaraldehyde (hydrophilic support) derivative showed high enantioselectivity (Palomo et al., 2002b). This is mainly because glutaraldehyde is soluble in an aqueous media and can form inter- and intrabonds. If immobilized, it alters the rigidity of the lipase resulting in a conformational change from closed form to open form.
Transesterification of vegetable oils into biodiesel by an immobilized lipase: a review
Published in Biofuels, 2023
Akossi Moya Joëlle Carole, Kouassi Konan Edmond, Abolle Abollé, Kouassi Esaie Kouadio Appiah, Yao Kouassi Benjamin
Encapsulation of an enzyme requires synthesis of the material in the presence of the enzyme. The drawbacks of this technique are intrinsic to the synthesis of the support. The localization of the enzyme inside the polymer poses steric problems. It is necessary to control, before immobilization, the size of the membrane pores to prevent enzyme leakage [114]. High temperatures may be required which might render the enzyme inactive. The use of solvent can also be a reason for the denaturation of the enzyme. Galarneau et al. [131] synthesized a spongy mesoporous material into which a very fragile enzyme was introduced during synthesis by adding lactose to protect the enzyme during network formation. This encapsulation in silicate sponge materials leads to significantly higher enzyme activities than those obtained with a solid-gel encapsulation method. Macario et al. encapsulated the lipase Rhizomucor miehei during the synthesis of silica nanospheres [132, 133].
Synthesis of biocatalyst in microfluidic reactor for β-sitosterol esterification
Published in Chemical Engineering Communications, 2023
Fiona W.M Ling, Hayder A. Abdulbari, Chin Sim-Yee, Wafaa K. Mahmood
From the results, catalyst loading of 2.5 mg/ml showed a better esterification rate, thus the result was used for comparison with the catalytic performance of free lipase under the same reaction conditions. When the esterification was carried out with a 2.5 mg/ml catalyst loading, Figure 12 showed the DE of immobilized lipase relative to free lipase. The results show that the DE of free lipase reached a maximum of 88.7%, compared to 97.3% for immobilized lipase. By using immobilized Rhizomucor miehei lipase on silica NPs, the catalytic performance was enhanced by 8.84% compared to the free lipase. Lipase immobilization through physical adsorption on a matrix material is believed to improve the catalytic efficiency through enhancing the interfacial specificities and substrate binding ability while enhancing the stability of the enzyme (Adlercreutz 2013). The high DE achieved in this study proven the possibility of using the Rhizomucor miehei as the biocatalyst in esterification process which the results are contradicted with previous studies where the DE was only 9.9% after 24 h of esterification (Villeneuve et al. 2005). However, the resulting DE is affected by different conditions and it is believed that extensive studies should be conducted in the future to obtain the optimum conditions using Rhizomucor miehei as biocatalyst in esterification process.
Crude glycerol impurities improve Rhizomucor miehei lipase production by Pichia pastoris
Published in Preparative Biochemistry & Biotechnology, 2021
Miao Tian, Zhi-Yuan Wang, Jun-Ying Fu, Hui-Wen Li, Jun Zhang, Xu-Feng Zhang, Wen Luo, Peng-Mei Lv
The recombinant Rhizomucor miehei lipase (RML, Genebank: A02536) was constructed in P. pastoris GS115 by Luo et al.[22]Pichia pastoris GS115 were used for protein expression. Glycerol (≥99.5%) was purchased from Shanghai Macklin Biochemical Co., Ltd. Crude glycerol received during biodiesel production from waste oil in a biodiesel plant (Maoming Hongyu Energy Technology Co., Ltd., China). The crude glycerol contained: 60% (w/w) glycerol, <1% (v/v) methanol, 20.6% (w/w) methyl ester and grease, and 14.2% metal saponification including 0.53‰ (w/w) Fe3+, 9.65‰ (w/w) Na+, 1.37‰ (w/w) K+, and 0.05‰ (w/w) Ca2+. The methyl ester, grease and methanol were measured by Gas Chromatography − Mass Spectrometry (GC-MS), the Fe3+, Na+, K+, and Ca2+ by inductively coupled plasma optical emission spectrometry (ICP-OES, PerkinElmer Optima 2100 DV, USA), Glycerol by Iodometric − Periodic Acid Method (GB/T 13216.6-91).