Gabrielle P. de Assis, Vinícius S. Silva, Mateus V. C. da Silva, Amanda B. S. Rangel, Leandro G. Aguiar, Larissa de Freitas
{"title":"利用磁性聚（苯乙烯-三乙烯基羟基二甲基丙烯酸酯）作为脂肪酶 G 的固定化基质：油酸己酯的合成应用和动力学研究","authors":"Gabrielle P. de Assis, Vinícius S. Silva, Mateus V. C. da Silva, Amanda B. S. Rangel, Leandro G. Aguiar, Larissa de Freitas","doi":"10.1007/s10562-024-04819-3","DOIUrl":null,"url":null,"abstract":"<div><p>This study aimed to synthesize the emollient ester hexyl oleate by enzymatic catalysis using lipase G from <i>Penicillium camemberti</i> immobilized on the magnetic copolymer poly(styrene-<i>co</i>-triethylene glycol dimethacrylate) (STY-TEGDMA-M). For this, an experimental study was carried out on esterification reactions conducted in solvent-free medium, and the collected data were used to construct a mathematical model. The physical properties of the immobilized derivative were evaluated by scanning electron microscopy and Fourier-transform infrared spectroscopy. The results confirmed that lipase G was successfully immobilized onto the support, with a catalytic activity of 564.63 U g<sup>−1</sup>. The biocatalyst showed optimum performance at 45 °C, reaching 82% conversion after 48 h of reaction. A chromatographic method was used to confirm the formation of hexyl oleate. A thermal stability assay was conducted, showing that the biocatalyst retained 87% of its initial activity after 4 h of incubation at 60 °C. Mathematical modeling was based on the ping-pong bi-bi kinetic mechanism. The best model was selected according to the lowest value of the corrected Akaike information criterion (AIC<sub>C</sub> = 124.776). The model revealed equilibrium constant values (<i>K</i><sub>eq</sub>) ranging from 0.87 to 14.57, maximum rates of the forward reaction ranging from 0.088 to 0.090 mol L<sup>−1</sup> min<sup>−1</sup>, and a maximum rate of the reverse reaction of 0.021 mol L<sup>−1</sup> min<sup>−1</sup>.</p><h3>Graphical Abstract</h3>\n<div><figure><div><div><picture><source><img></source></picture></div></div></figure></div></div>","PeriodicalId":508,"journal":{"name":"Catalysis Letters","volume":null,"pages":null},"PeriodicalIF":2.3000,"publicationDate":"2024-10-07","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"Employment of Magnetic Poly(Styrene-co-Triethylene Gycol Dimethacrylate) as an Immobilization Matrix for Lipase G: Application of Hexyl Oleate Synthesis and Kinetic Study\",\"authors\":\"Gabrielle P. de Assis, Vinícius S. Silva, Mateus V. C. da Silva, Amanda B. S. Rangel, Leandro G. Aguiar, Larissa de Freitas\",\"doi\":\"10.1007/s10562-024-04819-3\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<div><p>This study aimed to synthesize the emollient ester hexyl oleate by enzymatic catalysis using lipase G from <i>Penicillium camemberti</i> immobilized on the magnetic copolymer poly(styrene-<i>co</i>-triethylene glycol dimethacrylate) (STY-TEGDMA-M). For this, an experimental study was carried out on esterification reactions conducted in solvent-free medium, and the collected data were used to construct a mathematical model. The physical properties of the immobilized derivative were evaluated by scanning electron microscopy and Fourier-transform infrared spectroscopy. The results confirmed that lipase G was successfully immobilized onto the support, with a catalytic activity of 564.63 U g<sup>−1</sup>. The biocatalyst showed optimum performance at 45 °C, reaching 82% conversion after 48 h of reaction. A chromatographic method was used to confirm the formation of hexyl oleate. A thermal stability assay was conducted, showing that the biocatalyst retained 87% of its initial activity after 4 h of incubation at 60 °C. Mathematical modeling was based on the ping-pong bi-bi kinetic mechanism. The best model was selected according to the lowest value of the corrected Akaike information criterion (AIC<sub>C</sub> = 124.776). The model revealed equilibrium constant values (<i>K</i><sub>eq</sub>) ranging from 0.87 to 14.57, maximum rates of the forward reaction ranging from 0.088 to 0.090 mol L<sup>−1</sup> min<sup>−1</sup>, and a maximum rate of the reverse reaction of 0.021 mol L<sup>−1</sup> min<sup>−1</sup>.</p><h3>Graphical Abstract</h3>\\n<div><figure><div><div><picture><source><img></source></picture></div></div></figure></div></div>\",\"PeriodicalId\":508,\"journal\":{\"name\":\"Catalysis Letters\",\"volume\":null,\"pages\":null},\"PeriodicalIF\":2.3000,\"publicationDate\":\"2024-10-07\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Catalysis Letters\",\"FirstCategoryId\":\"92\",\"ListUrlMain\":\"https://link.springer.com/article/10.1007/s10562-024-04819-3\",\"RegionNum\":4,\"RegionCategory\":\"化学\",\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"Q3\",\"JCRName\":\"CHEMISTRY, PHYSICAL\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Catalysis Letters","FirstCategoryId":"92","ListUrlMain":"https://link.springer.com/article/10.1007/s10562-024-04819-3","RegionNum":4,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q3","JCRName":"CHEMISTRY, PHYSICAL","Score":null,"Total":0}
Employment of Magnetic Poly(Styrene-co-Triethylene Gycol Dimethacrylate) as an Immobilization Matrix for Lipase G: Application of Hexyl Oleate Synthesis and Kinetic Study
This study aimed to synthesize the emollient ester hexyl oleate by enzymatic catalysis using lipase G from Penicillium camemberti immobilized on the magnetic copolymer poly(styrene-co-triethylene glycol dimethacrylate) (STY-TEGDMA-M). For this, an experimental study was carried out on esterification reactions conducted in solvent-free medium, and the collected data were used to construct a mathematical model. The physical properties of the immobilized derivative were evaluated by scanning electron microscopy and Fourier-transform infrared spectroscopy. The results confirmed that lipase G was successfully immobilized onto the support, with a catalytic activity of 564.63 U g−1. The biocatalyst showed optimum performance at 45 °C, reaching 82% conversion after 48 h of reaction. A chromatographic method was used to confirm the formation of hexyl oleate. A thermal stability assay was conducted, showing that the biocatalyst retained 87% of its initial activity after 4 h of incubation at 60 °C. Mathematical modeling was based on the ping-pong bi-bi kinetic mechanism. The best model was selected according to the lowest value of the corrected Akaike information criterion (AICC = 124.776). The model revealed equilibrium constant values (Keq) ranging from 0.87 to 14.57, maximum rates of the forward reaction ranging from 0.088 to 0.090 mol L−1 min−1, and a maximum rate of the reverse reaction of 0.021 mol L−1 min−1.
期刊介绍：
Catalysis Letters aim is the rapid publication of outstanding and high-impact original research articles in catalysis. The scope of the journal covers a broad range of topics in all fields of both applied and theoretical catalysis, including heterogeneous, homogeneous and biocatalysis.
The high-quality original research articles published in Catalysis Letters are subject to rigorous peer review. Accepted papers are published online first and subsequently in print issues. All contributions must include a graphical abstract. Manuscripts should be written in English and the responsibility lies with the authors to ensure that they are grammatically and linguistically correct. Authors for whom English is not the working language are encouraged to consider using a professional language-editing service before submitting their manuscripts.
求助内容：
应助结果提醒方式：
京公网安备 11010802042870号
