Ferulic acid (FA), 4-hydroxyl-3-methoxy-2-benzylacrylic acid, has antioxidant, anticancer and ultraviolet absorption activities. However, the low hydrophilicity of FA has limited its application. Glyceryl ferulate (FG), which is an all-natural hydrophilic derivative of FA, can be used as an antioxidant and UV filter in food and cosmetic formulations. However, the applications of FG in these fields are limited due to its low content in nature. In this work, free liquid lipase was firstly used as a catalyst for FG preparation. Several different free liquid lipases (Candida antartica lipase-B, Candida antartica lipase-A, Thermomyces lanuginosus (Lipozyme TL 100L)) were screened and compared. The effects of the transesterification parameters (time, temperature, enzyme load and substrate ratio) were optimized and evaluated by response surface methodology. A reaction thermodynamic investigation was also performed. The results showed that, among the tested free lipases, the maximum FG yield (84.8±1.5%) was achieved using free Candida antartica lipase-B. Under the optimized conditions (an atmospheric system, an enzyme load of 11.1% and a 20:1 molar ratio of glycerol to EF at 70°C for 39.5 h), the FG yield and EF conversion were 84.8±1.5% and 95.7±1.2%, respectively. The activation energies of FG formation and EF conversion were 56.4 and 58.0kJ/mol, respectively.
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http://dx.doi.org/10.5650/jos.ess19283 | DOI Listing |
Bioresour Technol
November 2024
JNU-UPM International Joint Laboratory on Plant Oil Processing and Safety, Department of Food Science and Engineering, Jinan University, Guangzhou, Guangdong 510632, China. Electronic address:
Partial acylglycerols are valued for their emulsifying and stabilizing properties, yet precise green synthesis remains challenging due to low yield and selectivity. This study aimed to elucidate the "lipase selectivity-substrate structure-product composition" relationship to enhance the yield of targeted partial acylglycerol. The results showed that lipase exhibited a greater selectivity towards fatty acids with shorter chain lengths and higher unsaturation.
View Article and Find Full Text PDF3 Biotech
March 2023
Department of Chemistry, Payame Noor University (PNU), PO Box 19395-4697, Tehran, Iran.
In this study, lipase A, which has a unique applicability for the conversion of highly branched and bulky substrates, was subjected to immobilization on the flexible nanoporous MIL-53(Fe) by two approaches: covalent coupling and in situ immobilization method. The pre-synthesized support under ultrasound irradiation was incubated with -dicyclohexylcarbodiimide to mediate the covalent attachment between the carboxylic groups on the support surface and amino groups of enzyme molecules. The in situ immobilization in which the enzyme molecules directly were embedded into the metal-organic framework was performed under mild operating conditions in a facile one-step manner.
View Article and Find Full Text PDFBioresour Technol
November 2022
Department of Chemical Engineering, SSN College of Engineering, Chennai 603110, India.
In this study, Caulerpa racemosa oil was used to produce biodiesel by recombinant Pichia pastoris displaying bound (rPp-BL) and secretory lipase (rPp-SL). Collected algae was pre-treated using ultrasonication, microwave and solvent extraction. Defatted C.
View Article and Find Full Text PDFJ Sci Food Agric
December 2022
Chemical Engineering Discipline, School of Engineering, Monash University Malaysia, Subang Jaya, Malaysia.
Background: Crude palm oil (CPO) is rich with phytonutrients such as carotenoids and tocols which possesses many health benefits. The aim of this research was to develop a methanol-free process to produce palm phytonutrients via enzymatic hydrolysis. In this work, triacylglycerol was hydrolyzed into free fatty acids (FFAs) using three different types of liquid lipases derived from Aspergillus oryzae (ET 2.
View Article and Find Full Text PDFJ Biotechnol
February 2022
Department of Chemistry, Martin Luther University Halle-Wittenberg, Von-Danckelmann-Platz 4, Halle/Saale D-06099, Germany. Electronic address:
Erythropoietin (EPO) is a glycoprotein hormone that has been used to treat anemia in patients with chronic kidney disease and in cancer patients who are receiving chemotherapy. Here, we investigated the accessibility of the glutamine (Gln, Q) residues of recombinant human erythropoietin (rHuEPO) towards a thermoresistant variant microbial transglutaminase (mTGase), TG with the aim of developing novel rHuEPO conjugates that may potentially enhance its biological efficacy. As a model bioconjugation, we studied the reactivity of rHuEPO towards TG with a low molar mass amine group containing substrate, monodansyl cadaverine (MDC).
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