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| Li,Ying Xia; Dong,Bing Xue. |
| The aim of this work was to study the biodiesel production from cotton seed oil by lipase produced by Pichia guilliermondii lipase, which was immobilized onto hydrophobic magnetic particles (HMPs). The optimum reaction conditions were determined for lipase dosage, methanol-to-oil molar ratio, temperature and water content. Using response surface methodology, a quadratic polynomial equation was obtained for fatty acid methyl esters (FAMEs) content by multiple regression analysis. Verification experiments confirmed the validity of the predicted model. The optimal conditions for the enzymatic transesterification were temperature of 38.76℃, 31.3% immobilized lipase, 10.4% water content, and a methanol-to-oil molar ratio of 4.715:1. The gas chromatography- mass... |
| Tipo: Info:eu-repo/semantics/article |
Palavras-chave: Biodiesel response surface methodology; Lipase cotton seed oil. |
| Ano: 2016 |
URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1516-89132016000100400 |
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| Dong,Bing Xue; Zhang,Yu Hong; Li,Gang; Fang,Jin Tao; Zheng,Ji Huan; Mao,Run Qian. |
| ABSTRACT To seek a simple, rapid and sensitive Coprinus cinereus Peroxidase (CIP) activity assay, a convenient one-factor-at-a-time (OFAT) method and a response surface methodology (RSM) were used. The recombinant CIP expressed in Pichia pastoris was purified with the Ni-NTA spin column. Based on the results of catalytic efficiency (kcat/Km) analysis, 2,2'-azinobis (ethylbenzthiazoline -6-sulfonate) (ABTS) was selected as the optimal enzyme substrate. Results of the OFAT method showed that enzymatic reaction performed in 0.1 mol/L sodium acetate (pH 5.0) buffer in a 200-µl reaction mixture containing 0.5 mmol/L ABTS, 10 mmol/L hydrogen peroxide (H2O2), 49.7 ng CIP at 25°C gave an average CIP activity of 88 U/mL. The ABTS and H2O2 concentrations were then... |
| Tipo: Info:eu-repo/semantics/article |
Palavras-chave: Enzymatic activity assay; One-factor-at-a-time (OFAT) method; Response surface methodology (RSM); Coprinus cinereus peroxidase (CIP). |
| Ano: 2018 |
URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1516-89132018000100421 |
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