Investigation of Lipozyme TL IM-catalyzed transesterification using ultraviolet spectrophotometric assay

付显锋,; 郑建永,; 应向贤,; 鄢洪德,; 汪钊,

doi:10.1016/s1872-2067(14)60053-x

Cited by 11 publications

(5 citation statements)

References 36 publications

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“…The relative activity was decreased up to 80% on acetonitrile compared with that of n-hexane, moreover on acetone the enzymes exhibited 50% activity. Similar result was reported for Thermomyces lanuginosus lipase [ 43 ]. Some lipases were reported to lose its activity on acetone [ 21 ].…”

Section: Resultssupporting

confidence: 91%

Molecular characterization of transesterification activity of novel lipase family I.1

et al. 2022

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Lipase's thermostability and organic solvent tolerance are two crucial properties that enable it to function as a biocatalyst. This study examined the characteristics of two recombinant thermostable lipases (Lk2, Lk3) based on transesterification activity. Conversion of C12-C18 methyl ester with paranitrophenol was investigated in various organic solvent. Both lipases exhibited activity on difference carbon chain length (C12 – C18, C18:1, C18:2) of substrates. The activity of Lk2 was higher in each of substrate compared to that the Lk3. Experimental findings showed that the best substrates for Lk2 and Lk3 are C18:1 and C18:2 respectively, in agreement with the computational analysis. The activity of both enzymes prefers on nonpolar solvent. On nonpolar solvent the enzymes are able to keep its native folding shown by the value of radius gyration, solvent-enzyme interaction and orientation of triad catalytic residues. Lk3 appeared to be more thermostable, with maximum activity at 55°C. The presence of Fe3+ increased the activity of Lk2 and Lk3. However, the activity of both enzymes were dramatically decreased by the present of Ca2+ despite of the enzymes belong to family I.1 lipase known as calcium dependent enzyme. Molecular analysis on His loop of Lk2 and Lk3 on the present of Ca2+ showed that there were shifting on the orientation of catalytic triad residues. All the data suggest that Lk2 and Lk3 are novel lipase on the family I.1 and both lipase available as a biocatalyst candidate.

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Section: Resultssupporting

confidence: 91%

Molecular characterization of transesterification activity of novel lipase family I.1

et al. 2022

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“…2 showed that the highest yield of 1,2-acetonide-3-lauryl glycerol was achieved in n-hexane, namely 78.4％. n-hexane as a hydrophobic solvent interacts more effectively with lipozyme TL IM which is also hydrophobic 23) and increases the catalytic activity between methyl laurate and glycerol 1,2-acetonide. Furthermore, the interaction between the reactants and the catalyst is less effective in the reaction system without solvent, and the yield of 1,2-acetonide-3-lauryl glycerol is lower than the reaction system in n-hexane solvent.…”

Section: Effect Of Solventmentioning

confidence: 99%

“…Accordingly, the selection of a catalyst from Lipozyme TL IM is an excellent alternative to replace K 2 CO 3 and Na 2 CO 3 in the synthesis reaction of α-Glycerol Monolaurate. Some literature showed that Lipozyme TL IM has excellent catalytic activity in a transesterification reaction between a fatty acid ester and an alcohol to produce new fatty acid esters 23,24) . In addition, it is a cheap and commercial lipase from Novozym and also has an active site formed by Ser-His-Asp residues 21,23) .…”

Section: Deprotection Of 12-acetonide-3-lauryl Glycerolmentioning

confidence: 99%

“…Some literature showed that Lipozyme TL IM has excellent catalytic activity in a transesterification reaction between a fatty acid ester and an alcohol to produce new fatty acid esters 23,24) . In addition, it is a cheap and commercial lipase from Novozym and also has an active site formed by Ser-His-Asp residues 21,23) . The reaction for the synthesis of α-glycerol monolaurate from methyl laurate consists of 2 steps and follows the scheme in (Fig.…”

Section: Deprotection Of 12-acetonide-3-lauryl Glycerolmentioning

confidence: 99%

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Improved Synthesis of α-Glycerol Monolaurate Using Lipozyme TL IM

et al. 2022

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This study aimed to synthesize α-Glycerol Monolaurate from protected glycerol (glycerol 1,2-acetonide) using Lipozym TL IM as a catalyst. In the first step, transesterification of methyl laurate and glycerol 1,2-acetonide with Lipozyme TL IM produced 1,2-acetonide-3-lauryl glycerol. In the second step, deprotection of 1,2-acetonide-3-lauryl glycerol with Amberlyst-15 produced α-Glycerol Monolaurate. Furthermore, the optimum yield (82.1%) of 1,2-acetonide-3-lauryl glycerol (light yellow liquid, purity of 92%) was achieved at a reactant mole ratio of 1, n-hexane (4 mL) with a reaction time of 12 hours, and total Lipozyme TL IM of 5% (w/w of the total weight of reactants) at a temperature of 35℃. Deprotection of 1,2-acetonide-3-lauryl glycerol with Amberlyst-15 was conducted at room temperature for 24 hours. At a melting point of 62.8℃, and purity of 100% α-Glycerol Monolaurate in the form of a white solid was obtained with a yield of 74.6% after the recrystallization of the crude product. This α-glycerol monolaurate synthesis reaction pathway can be referred to as a green α-monoacylglyceride synthesis method.

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“…High temperature can reduce the viscosity of the reaction medium, enhance mutual solubility, improve the diffusion process of the substrate, and enhance the interaction between enzyme and substrate. However, high temperatures destroy the active conformation of the enzyme and resulting in loss of the activity in the biocatalytic process (Yadav and Dhoot 2009;Zheng et al 2011;Fu et al 2014).…”

Section: Effect Of Reaction Temperaturementioning

confidence: 99%

Immobilization of Lipozyme TL 100L for methyl esterification of soybean oil deodorizer distillate

et al. 2020

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An immobilization method for binding cross-linked enzyme aggregates of Lipozyme TL 100L on macroporous resin NKA (CLEA-TLL@NKA) was developed in this study. The esterification activity of CLEA-TLL@NKA reached 6.4 U/mg. The surface structure of immobilized lipase was characterized by scanning electron microscopy. Methyl esterification reaction of soybean oil deodorizer distillate (SODD) was catalyzed by CLEA-TLL@NKA, which the conversion rate reached 98% and its activity retained over 90% after 20 batches of reaction. Compared with the commercial enzyme Lipozyme TLIM, half-life (t 1/2 ) of CLEA-TLL@NKA increased by 25 times and the catalytic activity increased by approximate 10 times. Thus, CLEA-TLL@NKA had high catalytic activity, good operational stability, and potential industrial application in the field of oil processing.

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Investigation of Lipozyme TL IM-catalyzed transesterification using ultraviolet spectrophotometric assay

Cited by 11 publications

References 36 publications

Molecular characterization of transesterification activity of novel lipase family I.1

Molecular characterization of transesterification activity of novel lipase family I.1

Improved Synthesis of α-Glycerol Monolaurate Using Lipozyme TL IM

Immobilization of Lipozyme TL 100L for methyl esterification of soybean oil deodorizer distillate

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