Study and deployment of methacrylate-based polymer resins for immobilized lipase catalyzed triglyceride hydrolysis

Anand, Akash; Gnanasekaran, Priyadarshini; Allgeier, Alan M.; Weatherley, L.R.

doi:10.1016/j.fbp.2020.06.016

Cited by 13 publications

(6 citation statements)

References 72 publications

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“…This correlates with the results of contact angle measurement obtained by Anand et al., (2020) showing that ECR8806M was more hydrophobic than ECR1030M. [ 14 ]…”

Section: Resultssupporting

confidence: 89%

“…This correlates with the results of contact angle measurement obtained by Anand et al, (2020) showing that ECR8806M was more hydrophobic than ECR1030M. [14] Immobilization by covalent binding to epoxy-groups (A8285) showed the lowest specific activity for both lipases. During immobilization, multipoint covalent chemical bonds are formed between functional groups on the support and free amino groups on the enzyme.…”

Section: Catalytic Activity Of Immobilized Preparationssupporting

confidence: 87%

“…This is especially common in covalent binding due to multipoint attachment of the enzyme to the support. [7][8][9]14,15] Furthermore, immobilization on different supports has been found to affect the regioselectivity by enhancing acyl migration. [16,17] Evaluation of different supports and their effect on the lipase properties is thus essential in applications utilizing the sn-1,3regioselectivity of lipases, such as the production of STAG.…”

Section: Introductionmentioning

confidence: 99%

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Effects of Lipase Immobilization Conditions and Support Materials for the Production of Structured Triacylglycerols

Causevic

Olofsson²,

Adlercreutz

et al. 2023

Euro J Lipid Sci & Tech

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Structured triacylglycerols (STAG) with desired properties can be synthesized by transesterification using immobilized lipases. Herein, the effect of immobilization conditions and support material on the immobilization yield, specific activity and regioselectivity of lipases from Rhizomucor miehei (RML) and Rhizopus oryzae (ROL) in the production of STAG, are evaluated. Four different support materials utilizing adsorption and one with covalent binding are investigated. Ammonium sulfate is found to significantly increase the activity-based immobilization yield (12% and 38% for RML and ROL, respectively) and specific activity on Accurel MP1000 (MP1000) when used as the immobilization buffer. Furthermore, the immobilization principle and support material influenced both the activity and regiospecificity. Immobilization by adsorption is found to result in higher catalytic activity, while covalent binding resulted in lipase inactivation. For RML, the highest specific activity of 43 µmol STAG min −1 g −1 (U) is obtained on MP1000, while ROL, which exhibited higher activities in general, results in a maximum activity of 120 U on Lifetech ECR8806. The obtained specific activites are comparable to the commercial preparations Novozym 40086 (45 U) and Lipase DF "Amano" IM (147 U) while the regiospecificity of the developed preparations is even higher, forming at least 64% less byproduct. Practical applications: There is an increasing need for lipids with specific nutritional and physical properties in health, nutrition, and food applications. In this context, STAG are highly promising products due to the possibility to tailor the composition to obtain the desired properties. Immobilized lipases are the catalyst of choice for the production of STAG, in which activity and regioselectivity are particularly important parameters for the process performance. In this study, it is shown that these parameters can be affected by the immobilization conditions and support material. Immobilized preparations with high activity and excellent regiospecificity are created on commercially available supports. This shows the possibility of STAG synthesis with high purity and beneficial properties.

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“…This correlates with the results of contact angle measurement obtained by Anand et al., (2020) showing that ECR8806M was more hydrophobic than ECR1030M. [ 14 ]…”

Section: Resultssupporting

confidence: 89%

Section: Catalytic Activity Of Immobilized Preparationssupporting

confidence: 87%

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Effects of Lipase Immobilization Conditions and Support Materials for the Production of Structured Triacylglycerols

Causevic

Olofsson²,

Adlercreutz

et al. 2023

Euro J Lipid Sci & Tech

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“…This is probably due to the high porosity of this support, which results in a large surface area. Similar support of octadecyl methacrylate (Purolite ® Lifetech™ ECR8806M) was used for immobilization of ET2, TLL, and Candida rugosa (CRL) lipases, but the maximum enzyme loading achieved did not exceed 20 mg/g (enzyme/support) in any of the cases [26][27][28]. No other study was found in the literature reporting the immobilization of any enzyme on IB-ADS-3, which may open up possibilities for further research.…”

Section: Immobilization Of Et2 Lipasementioning

confidence: 99%

Strategies for the Immobilization of Eversa® Transform 2.0 Lipase and Application for Phospholipid Synthesis

et al. 2021

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Eversa® Transform 2.0 lipase (ET2) is a recent lipase formulation derived from the Thermomyces lanuginosus lipase cultivated on Aspergillus oryzae and specially designed for biodiesel production. Since it has not been available for a long time, research on the efficiency of this enzyme in other applications remains unexplored. Moreover, even though it has been launched as a free enzyme, its immobilization may extend the scope of ET2 applications. This work explored ET2 immobilization on octadecyl methacrylate beads (IB-ADS-3) and proved the efficiency of the derivatives for esterification of glycerophosphocholine (GPC) with oleic acid in anhydrous systems. ET2 immobilized via interfacial activation on commercial hydrophobic support Immobead IB-ADS-3 showed maximum enzyme loading of 160 mg/g (enzyme/support) and great stability for GPC esterification under 30% butanone and solvent-free systems. For reusability, yields above 63% were achieved after six reaction cycles for GPC esterification. Considering the very high enzyme loading and the number of reuses achieved, these results suggest a potential application of this immobilized biocatalyst for esterification reactions in anhydrous media. This study is expected to encourage the exploration of other approaches for this enzyme, thereby opening up several new possibilities.

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“…28 Pinto et al 40 found that when lipase is immobilized on hydrophobic support, the catalytic activity of lipase is greatly affected because of the interfacial activation mechanism. Moreover, Anand et al 41 investigated the effects of functional groups on the efficiency of lipase immobilization and suggested that lipase immobilized on octadecyl resin showed the highest hydrophobicity and was more effective in esterification. A study by Basso et al 42 indicated that, unlike the resin (Lewatit VP OC 1600) used for the production of Novozym®435 (a commercially immobilized enzyme widely used in industrial production), the ECR® resins possess high mechanical stability and are therefore more suitable for applications that expose the polymers to high mechanical stress, such as multiple reuses in stirred reactors.…”

Section: Introductionmentioning

confidence: 99%

Study on the synthesis of pine sterol esters in solvent‐free systems catalyzed by Candida rugosa lipase immobilized on hydrophobic macroporous resin

Zhang

Wang

et al. 2023

J Sci Food Agric

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BACKGROUNDPine sterol ester is a type of novel food source nutrient with great advantages in lowering blood cholesterol levels, inhibiting tumors, preventing prostate enlargement, and regulating immunity. Macroporous resins with large specific surface area, stable structures, and various functional groups (epoxy, amino, and octadecyl groups) have been selected for immobilization of Candida rugosa lipase (CRL) to improve its stability and efficiency in the synthesis of pine sterol esters. A solvent‐free strategy using oleic acid (substrate) as an esterification reaction medium is an important alternative for avoiding the use of organic solvents.RESULTSThe immobilization conditions of CRL immobilized on several types of commercial macroporous resins were optimized. Fortunately, by adsorption (hydrophobic interaction), a high immobilization efficiency of CRL was obtained using macroporous resins with hydrophobic octadecyl groups with an immobilization efficiency of 86.5%, enzyme loading of 138.5 mg g−1 and enzyme activity of 34.7 U g−1. The results showed that a 95.1% yield could be obtained with a molar ratio of oleic acid to pine sterol of 5:1, an enzyme amount of 6.0 U g−1 (relative to pine sterol mass) at 50 °C for 48 h.CONCLUSIONThe hydrophobic macroporous resin (ECR8806M) with a large specific surface area and abundant functional groups was used to achieve efficient immobilization of CRL. CRL@ECR8806M is an efficient catalyst for the synthesis of phytosterol esters and has the potential for further large‐scale applications. Therefore, this simple, green, and low‐cost strategy for lipase immobilization provides new possibilities for the high‐efficiency production of pine sterol esters and other food source nutrients. © 2023 Society of Chemical Industry.

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Study and deployment of methacrylate-based polymer resins for immobilized lipase catalyzed triglyceride hydrolysis

Cited by 13 publications

References 72 publications

Effects of Lipase Immobilization Conditions and Support Materials for the Production of Structured Triacylglycerols

Effects of Lipase Immobilization Conditions and Support Materials for the Production of Structured Triacylglycerols

Strategies for the Immobilization of Eversa® Transform 2.0 Lipase and Application for Phospholipid Synthesis

Study on the synthesis of pine sterol esters in solvent‐free systems catalyzed by Candida rugosa lipase immobilized on hydrophobic macroporous resin

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