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51.
Luciana F. Fleuri Paula K. Novelli Clarissa H. O. Delgado Mayara R. Pivetta Milene S. Pereira Mariana de L. C. Arcuri Bruna L. Capoville 《International Journal of Food Science & Technology》2014,49(12):2585-2591
Lipase from Aspergillus sp. obtained by solid‐state fermentation (SSF) on wheat bran (LWB), soybean bran (LSB) and soybean bran combined with sugarcane bagasse (LSBBC) were 67.5, 58 and 57.3 U of crude lipase per gram substrate, respectively. The optimum pH of activity and stability of the LWB was between 8 and 9, and the optimum temperature of activity and stability was 50 °C and up to 60 °C, respectively. The LSB and LSBBC showed two peaks of optimum pH (4 and 6) and optimal values of temperature and stability at 50 °C. The LSB was stable in the pH range of 6–7, while LSBBC in the range of pH 4–7. All the enzymes show activities on p‐nitrophenyl esters (butyrate, laurate and palmitate). LWB stood out either on the hydrolysis of sunflower oil, presenting 66.1% of the activity over commercial lipase and on the esterification of oleic acid and ethanol, surpassing the activities of the commercial lipases studied. The thin layer chromatography showed that LWB and LSB have produced ethyl esters from corn oil, while LWB produced it from sunflower oil. 相似文献
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One‐Pot Lipase Entrapment Within Silica Particles to Prepare a Stable and Reusable Biocatalyst for Transesterification 下载免费PDF全文
In order to enhance the reusability, Rhizomucor miehei lipase was entrapped in a single step within silica particles having an oleic acid core (RML@SiO2). Characterization of RML@SiO2 by scanning and transmission electron microscopy and Fourier transform infrared studies supported the lipase immobilization within silica particles. The immobilized enzyme was employed for transesterification of cottonseed oil with methanol and ethanol. Under the optimum reaction conditions of a methanol‐to‐oil molar ratio of 12:1 or ethanol‐to‐oil molar ratio of 15:1, stirring speed of 250 revolutions/min (flask radius = 3 cm), reaction temperature of 40 °C, and biocatalyst concentration of 5 wt% (with respect to oil), more than 98 % alkyl ester yield was achieved in 16 and 24 h of reaction duration in case of methanolysis and ethanolysis, respectively. The immobilized enzyme did not require any buffer solution or organic solvent for optimum activity; hence, the produced biodiesel and glycerol were free from metal ion or organic molecule contamination. The activation energies for the immobilized enzyme‐catalyzed ethanolysis and methanolysis were found to be 34.9 ± 1.6 and 19.7 ± 1.8 kJ mol?1, respectively. The immobilized enzyme was recovered from the reaction mixture and reused in 12 successive runs without significant loss of activity. Additionally, RML@SiO2 demonstrated better reusability as well as stability in comparison to the native enzyme as the former did not lose the activity even upon storage at room temperature (25–30 °C) over an 8‐month period. 相似文献
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Calix[4]arene amide derivatives were employed as new additives within the sol-gel encapsulation of lipase from Candida rugosa (CRL) to improve its catalytic properties. Evaluation of catalytic activity of the encapsulated lipases was acheived by enantioselective hydrolysis of both racemates, Naproxen methyl ester and 2-phenoxypropionic acid methyl ester, in aqueous buffer solution/isooctane reaction system. Results show that enantioselectivity was improved by using calix[4]arene amide derivatives-based encapsulated lipases. The reaction of naproxen methyl ester resulted in 47.6% conversion (x) in 24 h with 88.9% enantiomeric excess of substrate (ees), analogous to an enantioselectivity (E) value of 297 (E = 137 for the encapsulated free enzyme). The conversion of 2-phenoxypropionic acid methyl ester, obtained was 48.4% with E value of 327, enantiomeric excess of substrate (ees) of 92% for the reaction time of 1 h (E = 211 for the encapsulated free enzyme). 相似文献
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George F. Finco Karina G. Fiametti Viviane da Silva Lobo Edson A. da Silva Fernando Palú João H. C. Wancura Maria L. F. Rodrigues Alexsandra Valério José Vladimir de Oliveira 《Journal of the American Oil Chemists' Society》2022,99(7):559-568
Monoacylglycerol (MAG) and diacylglycerol (DAG) are two natural components found in most edible oils and fats. Conventional synthesis of MAG and DAG is usually conducted by glycerolysis of triacylglycerol (TAG) at high temperatures (above 200°C) in the presence of an alkaline catalyst. In this work, the synthesis of MAG and DAG using enzymatic glycerolysis of olive oil was investigated using Tween 80 as surfactant, n-butanol as co-surfactant and the novel lipase in free/liquid formulation Lipozyme TL 100L as catalyst. Experimental design was used to evaluate the effect of enzyme load and reaction temperature on the feedstock conversion. Enzyme load and system temperature were significant variables in the statistical design and the best condition was found at 35°C, 7.5 vol% of Lipozyme TL 100L and glycerol to oil volumetric ratio of 2:1 with conversion of TAG at approximately 98% after 2 h of process. A mathematical model based on the Ping-Pong Bi-Bi mechanism was used to describe the reaction kinetics. The model adequately described the behavior of the system and can be a useful tool for the design of reactors in larger scales. 相似文献
57.
Typoselectivity of Crude Geobacillus sp. T1 Lipase Fused with a Cellulose-Binding Domain and Its Use in the Synthesis of Structured Lipids 总被引:1,自引:0,他引:1
Xiao-Li Qin Hui-Hua Huang Dong-Ming Lan Yong-Hua Wang Bo Yang 《Journal of the American Oil Chemists' Society》2014,91(1):55-62
Typoselectivity of crude CBD-T1 lipase (Geobacillus sp. T1 lipase fused with a cellulose binding domain) was investigated. Multi-competitive reaction mixtures including a set of n-chain fatty acids (C8:0, C10:0, C12:0, C14:0, C18:1 n-9, C18:2 n-6 and C18:3 n-3) and tripalmitin-enriched triacylglycerols were studied in hexane. The crude CBD-T1 lipase discriminated strongly against C18:1 n-9 [competitive factor (α) = 0.23] and showed the highest preference for C8:0 (α = 1). Utilizing the catalytic properties of crude CBD-T1 lipase, acidolysis of soybean oil with C8:0 was selected as a model reaction to investigate the ability of the lipase to produce MLM-type (medium-long-medium) structured lipids. Several reaction parameters (added water amount, reaction temperature, substrate molar ratio and reaction time) examined for incorporating C8:0 into soybean oil, the optimum conditions were: 1:3 (soybean oil/C8:0) of molar ratio, 3 mL of hexane, 50 °C of temperature, 48 h of reaction time, 20 % of crude CBD-T1 lipase (w/w total substrates), and 7.5 % of water (w/w enzyme). Under these conditions, the incorporation of C8:0 was 29.6 mol%. The results suggest that crude CBD-T1 lipase, which showed different fatty acid specificity profiles, is a potential biocatalyst for the modification of fats and oils. 相似文献
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固定化脂肪酶催化菜籽油合成蜡酯 总被引:2,自引:0,他引:2
以菜籽油、鲸蜡醇为原料,采用实验室自制的固定化Candidia sp.99-125脂肪酶分别在有机溶剂和无溶剂体系下合成了蜡酯,在两种体系下对影响蜡酯合成的各种因素进行了比较研究,研究表明:以正己烷为反应介质,在40℃条件下反应12h,油醇摩尔比1∶2,酶量15%(质量分数,上同),水含量7.5%,蜡酯产率可达85.87%;无溶剂体系中在50℃条件下反应20h,油醇摩尔比1∶1.5,蜡酯产率可达80.68%。通过流加鲸蜡醇可以提高酶的使用寿命。 相似文献
60.