Biotransformation of Cinnamic Acid, Cinnamaldehyde, Furfural and Epoxidation of Cyclohexene by Plant Catalase

IF 0.9 Q4 CHEMISTRY, PHYSICAL
Takio Nene, Anindita Hazarika, Meera Yadav
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This study focuses on catalases as a biocatalyst for potential epoxidation reactions of olefins.Objective: To determine the possibility of using biocatalyst catalase from a novel source Sechium edule (squash) for epoxidation of olefins in the presence of H2O2. UV-Vis spectrophotometer was used to monitor the formation of epoxide from substrates- cyclohexene, cinnamic acid, cinnamaldehyde, furfural in acetonitrile solvent and a suitable aliquot of the enzyme solution in the presence of H2O2. The products formed were analyzed using FTIR and GC-MS. For the immobilized enzyme, chitosan beads activated with TPP were used in place of the enzyme and a similar procedure was followed for the analysis. Four different olefin substrates (cyclohexene, cinnamic acid, cinnamaldehyde, and furfural) were selected to study the catalysis reaction of epoxidation by the catalase enzyme. The course of the epoxidation was monitored by UV-Vis, FTIR, and GC-MS methods. However, under optimized reaction conditions and spectral analysis, further confirmed by GC-MS, data showed only epoxide formation from cyclohexene. CAT completely catalyzed other olefins like furfural, cinnamic acid, and cinnamaldehyde into its degraded products biochemically. Therefore, cyclohexene was selected for further immobilization studies and the identified metabolites of olefins and their degradation mechanism. Major biodegradation products of cinnamic acid were found to be styrene( m/z 104.0) and benzaldehyde(m/z 105.0). GC-MS data of biotransformation of cinnamaldehyde, identified 2,4 dimethyl benzaldehyde(m/z 133) as the main product. The catalytic biotransformation of furfural investigated by GC-MS data identified 2,5 dimethyl benzaldehyde (m/z 133), dodecanol (m/z 181) and Pentanoic acid, 5 hydroxy, 2,4 dibutyl phenyl ester(m/z 306) as the major product. Three major oxidized products were detected in GC-MS data from the epoxidation of cyclohexene viz., cyclohexane diol(m/z 116), cyclohexene epoxide-1-ol(m/z 110), cyclohexene epoxide-1-one(m/z 110). In this investigation, catalase purified from Sechium edule(squash) was developed as an efficient catalytic tool for the biotransformation of olefins and selective epoxidation of cyclohexene. Under optimized conditions, the experimental results revealed the main products found in cinnamaldehyde as benzaldehyde (m/z 133.0) and cinnamic acid as benzaldehyde (m/z 133), styrene (m/z 104.0) and benzoic acid (m/z 122.0), while the data from furfural oxidation could not be justified from previous studies. The optimal concentration of CH3CN solvent for cyclohexene epoxidation was found to be 4 mM. Enzymatic characterization of free and immobilized catalase on chitosan was investigated using cyclohexene as a variable substrate and found to be 0.017 mM, 83.33 μmol/min for Km and Vmax values, pH 6.8 and 30˚C for free CAT and 0.03 mM, 200 μmol/min, pH 7.6 and 35˚C for immobilized one. Immobilization increases the thermal stability of the CAT and changes the pH to alkalinity. The possible oxidation of cyclohexene was deduced as the radical chain mechanism for the generation of epoxide with the key products obtained as cyclohexane diol(m/z 116), cyclohexene epoxide-1-ol(m/z 110) and cyclohexene epoxide-1-one(m/z 110). The reusability of the biocatalytic tool opens up the opportunity to reduce the cost of various catalytic reactions. Further studies can focus on the separation and advancement of epoxide yields, improved immobilization strategy for maximum repetitive cycles, and chemo-enzymatic epoxidation on biological olefins.","PeriodicalId":10945,"journal":{"name":"Current Organocatalysis","volume":null,"pages":null},"PeriodicalIF":0.9000,"publicationDate":"2023-11-24","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Current Organocatalysis","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.2174/0122133372268423231101072640","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q4","JCRName":"CHEMISTRY, PHYSICAL","Score":null,"Total":0}
引用次数: 0

Abstract

Epoxides are widely useful in various fields such as pharmaceuticals, pesticides, cosmetics, polymer synthesis, fragrance compounds, and food additives. However, the synthesis of epoxides involves heavy metal catalysts and toxic, unstable organic catalysts which causes serious environmental and safety concerns. In recent years, biocatalysts have received a great deal of interest in the synthesis of olefin-derived epoxides due to their mild reaction conditions, environmental friendliness, good selectivity, and sustainability. This study focuses on catalases as a biocatalyst for potential epoxidation reactions of olefins.Objective: To determine the possibility of using biocatalyst catalase from a novel source Sechium edule (squash) for epoxidation of olefins in the presence of H2O2. UV-Vis spectrophotometer was used to monitor the formation of epoxide from substrates- cyclohexene, cinnamic acid, cinnamaldehyde, furfural in acetonitrile solvent and a suitable aliquot of the enzyme solution in the presence of H2O2. The products formed were analyzed using FTIR and GC-MS. For the immobilized enzyme, chitosan beads activated with TPP were used in place of the enzyme and a similar procedure was followed for the analysis. Four different olefin substrates (cyclohexene, cinnamic acid, cinnamaldehyde, and furfural) were selected to study the catalysis reaction of epoxidation by the catalase enzyme. The course of the epoxidation was monitored by UV-Vis, FTIR, and GC-MS methods. However, under optimized reaction conditions and spectral analysis, further confirmed by GC-MS, data showed only epoxide formation from cyclohexene. CAT completely catalyzed other olefins like furfural, cinnamic acid, and cinnamaldehyde into its degraded products biochemically. Therefore, cyclohexene was selected for further immobilization studies and the identified metabolites of olefins and their degradation mechanism. Major biodegradation products of cinnamic acid were found to be styrene( m/z 104.0) and benzaldehyde(m/z 105.0). GC-MS data of biotransformation of cinnamaldehyde, identified 2,4 dimethyl benzaldehyde(m/z 133) as the main product. The catalytic biotransformation of furfural investigated by GC-MS data identified 2,5 dimethyl benzaldehyde (m/z 133), dodecanol (m/z 181) and Pentanoic acid, 5 hydroxy, 2,4 dibutyl phenyl ester(m/z 306) as the major product. Three major oxidized products were detected in GC-MS data from the epoxidation of cyclohexene viz., cyclohexane diol(m/z 116), cyclohexene epoxide-1-ol(m/z 110), cyclohexene epoxide-1-one(m/z 110). In this investigation, catalase purified from Sechium edule(squash) was developed as an efficient catalytic tool for the biotransformation of olefins and selective epoxidation of cyclohexene. Under optimized conditions, the experimental results revealed the main products found in cinnamaldehyde as benzaldehyde (m/z 133.0) and cinnamic acid as benzaldehyde (m/z 133), styrene (m/z 104.0) and benzoic acid (m/z 122.0), while the data from furfural oxidation could not be justified from previous studies. The optimal concentration of CH3CN solvent for cyclohexene epoxidation was found to be 4 mM. Enzymatic characterization of free and immobilized catalase on chitosan was investigated using cyclohexene as a variable substrate and found to be 0.017 mM, 83.33 μmol/min for Km and Vmax values, pH 6.8 and 30˚C for free CAT and 0.03 mM, 200 μmol/min, pH 7.6 and 35˚C for immobilized one. Immobilization increases the thermal stability of the CAT and changes the pH to alkalinity. The possible oxidation of cyclohexene was deduced as the radical chain mechanism for the generation of epoxide with the key products obtained as cyclohexane diol(m/z 116), cyclohexene epoxide-1-ol(m/z 110) and cyclohexene epoxide-1-one(m/z 110). The reusability of the biocatalytic tool opens up the opportunity to reduce the cost of various catalytic reactions. Further studies can focus on the separation and advancement of epoxide yields, improved immobilization strategy for maximum repetitive cycles, and chemo-enzymatic epoxidation on biological olefins.
植物过氧化氢酶对肉桂酸、肉桂醛、糠醛的生物转化和环己烯的环氧化作用
环氧化物在制药、杀虫剂、化妆品、聚合物合成、香料化合物和食品添加剂等多个领域具有广泛用途。然而,环氧化物的合成涉及重金属催化剂和有毒、不稳定的有机催化剂,这引起了严重的环境和安全问题。近年来,生物催化剂因其温和的反应条件、环境友好性、良好的选择性和可持续性,在烯烃衍生环氧化物的合成中受到了广泛关注。本研究的重点是将催化剂作为一种生物催化剂用于潜在的烯烃环氧化反应:目的:确定在 H2O2 存在的情况下,使用来自新型来源 Sechium edule(地瓜)的生物催化剂过氧化氢酶进行烯烃环氧化反应的可能性。 使用紫外可见分光光度计监测底物环己烯、肉桂酸、肉桂醛、糠醛在乙腈溶剂和适当等量的酶溶液中,在 H2O2 存在下形成环氧化物的情况。使用傅立叶变换红外光谱(FTIR)和气相色谱-质谱(GC-MS)分析生成的产物。对于固定化酶,则使用用 TPP 活化的壳聚糖珠代替酶,并按照类似的程序进行分析。 选择了四种不同的烯烃底物(环己烯、肉桂酸、肉桂醛和糠醛)来研究催化酶的环氧化催化反应。紫外可见光、傅立叶变换红外光谱和气相色谱-质谱法监测了环氧化反应的过程。然而,在优化的反应条件和光谱分析下,经 GC-MS 进一步确认,数据显示环己烯只生成环氧化物。CAT 可将糠醛、肉桂酸和肉桂醛等其他烯烃完全催化成其生化降解产物。因此,我们选择了环己烯作为进一步固定化研究的对象,并确定了烯烃的代谢产物及其降解机制。肉桂酸的主要生物降解产物是苯乙烯(m/z 104.0)和苯甲醛(m/z 105.0)。肉桂醛生物转化的气相色谱-质谱数据表明,2,4 二甲基苯甲醛(m/z 133)是主要产物。通过 GC-MS 数据研究糠醛的催化生物转化,发现 2,5 二甲基苯甲醛(m/z 133)、十二醇(m/z 181)和戊酸,5 羟基,2,4 二丁基苯基酯(m/z 306)是主要产物。环己烯环氧化反应的气相色谱-质谱数据中检测到三种主要氧化产物,即环己烷二醇(m/z 116)、环己烯环氧化物-1-醇(m/z 110)和环己烯环氧化物-1-酮(m/z 110)。 在这项研究中,从 Sechium edule(壁虱)中纯化的过氧化氢酶被开发为一种高效的催化工具,可用于烯烃的生物转化和环己烯的选择性环氧化。在优化条件下,实验结果表明肉桂醛的主要产物为苯甲醛(m/z 133.0),肉桂酸的主要产物为苯甲醛(m/z 133)、苯乙烯(m/z 104.0)和苯甲酸(m/z 122.0),而糠醛氧化的数据无法与之前的研究相吻合。环己烯环氧化的最佳 CH3CN 溶剂浓度为 4 mM。使用环己烯作为可变底物研究了壳聚糖上游离和固定过氧化氢酶的酶学特性,发现游离过氧化氢酶的 Km 和 Vmax 值分别为 0.017 mM、83.33 μmol/min,pH 值为 6.8,温度为 30˚C;固定过氧化氢酶的 Km 和 Vmax 值分别为 0.03 mM、200 μmol/min,pH 值为 7.6,温度为 35˚C。固定化增加了 CAT 的热稳定性,并使 pH 值变为碱性。推断环己烯的氧化可能是生成环氧化物的自由基链机制,主要产物为环己烷二醇(m/z 116)、环己烯环氧化物-1-醇(m/z 110)和环己烯环氧化物-1-酮(m/z 110)。生物催化工具的可重复使用性为降低各种催化反应的成本提供了机会。进一步的研究可以集中在环氧化物的分离和提高产量、改进固定化策略以实现最大限度的重复循环,以及生物烯烃的化学酶环氧化等方面。
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来源期刊
Current Organocatalysis
Current Organocatalysis CHEMISTRY, PHYSICAL-
CiteScore
2.00
自引率
0.00%
发文量
28
期刊介绍: Current Organocatalysis is an international peer-reviewed journal that publishes significant research in all areas of organocatalysis. The journal covers organo homogeneous/heterogeneous catalysis, innovative mechanistic studies and kinetics of organocatalytic processes focusing on practical, theoretical and computational aspects. It also includes potential applications of organocatalysts in the fields of drug discovery, synthesis of novel molecules, synthetic method development, green chemistry and chemoenzymatic reactions. This journal also accepts papers on methods, reagents, and mechanism of a synthetic process and technology pertaining to chemistry. Moreover, this journal features full-length/mini review articles within organocatalysis and synthetic chemistry. It is the premier source of organocatalysis and synthetic methods related information for chemists, biologists and engineers pursuing research in industry and academia.
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