Biocatalysis and Biotransformation最新文献_第9页

Continuous-flow biocatalysed kinetic resolution of 4-fluorophenyl-furan-2-yl methanol 连续流动生物催化动力学拆分4-氟苯-呋喃-2-基甲醇

IF 1.8 4区生物学

Biocatalysis and Biotransformation Pub Date : 2022-07-01 DOI: 10.1080/10242422.2022.2094258

R. D. de Souza, Raquel A. C. Leão, Barbara Maia, M. Gomez

{"title":"Continuous-flow biocatalysed kinetic resolution of 4-fluorophenyl-furan-2-yl methanol","authors":"R. D. de Souza, Raquel A. C. Leão, Barbara Maia, M. Gomez","doi":"10.1080/10242422.2022.2094258","DOIUrl":"https://doi.org/10.1080/10242422.2022.2094258","url":null,"abstract":"Abstract Enantiomerically pure secondary alcohols are useful in the synthesis of several natural products and as active pharmaceutical intermediates (API). Due to the high demand for these chiral compounds, much progress has been made in the areas of asymmetric synthesis and catalysis. In this context, biocatalysis together with continuous flow technology can be a valuable tool for more versatile and sustainable methods, with lower cost, greater stereoselectivity and less environmental impact. This work aims to obtain an enantiomerically pure alcohol of industrial interest, (4 Fluorophenyl) (furan-2-yl) methanol (3), by performing a kinetic resolution using immobilized Candida antarctica lipase B (Novozyme 435, N435) under continuous-flow conditions. Initial study was carried out to optimize batch reaction conditions. The best results were obtained using isooctane as solvent, 37.7 mg of N435 and three equivalents of isopropenyl acetate as acyl donor at 60 °C for 24 h. Under these conditions, a conversion of 49% and 91 of enantiomeric ratio was obtained. Optimized batch conditions were translated to the continuous flow reactor leading to the desired product in 30 min of residence time, 47% conversion and an enantiomeric ratio of 61.","PeriodicalId":8824,"journal":{"name":"Biocatalysis and Biotransformation","volume":"41 1","pages":"367 - 373"},"PeriodicalIF":1.8,"publicationDate":"2022-07-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"49092455","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Cyanide bioremediation potential of Klebsiella oxytoca JCM 1665 rhodanese immobilized on alginate-glutaraldehyde beads 藻酸盐-戊二醛珠固定化羟基克雷伯菌JCM 1665硫丹酸盐的氰化物生物修复潜力

IF 1.8 4区生物学

Biocatalysis and Biotransformation Pub Date : 2022-06-17 DOI: 10.1080/10242422.2022.2087510

B. Itakorode, R. E. Okonji, N. Torimiro

{"title":"Cyanide bioremediation potential of Klebsiella oxytoca JCM 1665 rhodanese immobilized on alginate-glutaraldehyde beads","authors":"B. Itakorode, R. E. Okonji, N. Torimiro","doi":"10.1080/10242422.2022.2087510","DOIUrl":"https://doi.org/10.1080/10242422.2022.2087510","url":null,"abstract":"Abstract Rhodanese, a cyanide detoxifying enzyme synthesized by Klebsiella oxytoca was immobilized on alginate-glutaraldehyde beads. K. oxytoca was isolated from industrial wastewater and identified using 16S rRNA gene sequencing with gene bank accession number MN590525. Rhodanese was produced from the bacterium through submerged fermentation. The rhodanese produced was immobilized on alginate-glutaraldehyde beads; its physicochemical properties and cyanide bioremediation potential were compared with the free enzyme. In this study, the optimum concentrations of glutaraldehyde and sodium alginate that resulted in the highest enzyme immobilization yield (89.71%) and lower leakage (1.45 ± 0.2%) were 4.5% (v/v) and 2.5 (%) respectively. The optimum temperature for free and immobilized rhodanese was observed at 50 °C and 60 °C respectively while the optimum pH for both preparations was 6.0. The free rhodanese retained 31% and 23% of relative activity at 60 °C and 70 °C respectively after 30 minutes of incubation while immobilized rhodanese retained about 95% and 70% at the same condition. The entrapped rhodanese showed activity until the 10th cycle and maintained about 70% of its activity after the fifth cycle. After 180 minutes of incubation, the free and immobilized rhodanese was able to biodegrade 115 mg/L cyanide to 77 mg/L and 45 mg/L respectively with degradation efficiency of 33 and 64.34%. These results suggest that immobilized K. oxytoca rhodanese may be profitably exploited in bioremediation of cyanide polluted environment due to its thermal stability and its reusability.","PeriodicalId":8824,"journal":{"name":"Biocatalysis and Biotransformation","volume":"41 1","pages":"299 - 308"},"PeriodicalIF":1.8,"publicationDate":"2022-06-17","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"49300559","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 3

Saccharification of pre-treated wheat straw via optimized enzymatic production using Aspergillus niger: Chemical analysis of lignocellulosic matrix 利用黑曲霉优化酶法生产预处理小麦秸秆的糖化:木质纤维素基质的化学分析

IF 1.8 4区生物学

Biocatalysis and Biotransformation Pub Date : 2022-06-15 DOI: 10.1080/10242422.2022.2087511

M. El-sheekh, Mohammed Y. Bedaiwy, Aya A. El-Nagar, Eman Elgammal

{"title":"Saccharification of pre-treated wheat straw via optimized enzymatic production using Aspergillus niger: Chemical analysis of lignocellulosic matrix","authors":"M. El-sheekh, Mohammed Y. Bedaiwy, Aya A. El-Nagar, Eman Elgammal","doi":"10.1080/10242422.2022.2087511","DOIUrl":"https://doi.org/10.1080/10242422.2022.2087511","url":null,"abstract":"Abstract Bioconversion of lignocellulosic wastes to valuable end-products via multi-enzymatic hydrolysis is a potential low costing process for large-scale application in many industrial sectors. Thus, in this study, among thirty local fungal isolates, Aspergillus niger which gave the highest cellulase production, was identified under the accession number MZ062603 in GeneBank. Three types of pre-treatments (0.0–0.7%) acid, (0.0–2%) alkali, and (70–90 °C) hot water were applied to increase wheat straw (WS) digestibility by A. niger, and 1% NaOH treated WS was superior to the other pre-treatments (acid and hot water). During solid-state fermentation, the total cellulolytic activity of [filter-paper cellulase (FPase), carboxy-methyl cellulase (CMCase), and β- glucosidase (βGase)] increased about 2.8-fold. While reducing sugar was increased by 3.1 times. The optimum values of total cellulases activities and reducing sugar (8907.2 and 92.4 mg/gds) were obtained after 3 days of incubation at 30 °C and pH 5.2 at 75% v/w moisture using 3 days old inoculum (106 spores/mL/gds). The WS substrate which was subjected to alkali pre-treatment subsequent to fungal bioconversion was varied in its chemical composition and detailed structure compared to the raw and alkali pre-treatment ones as indicated by its chemical analysis, Scanning electron microscopy (SEM) observation, Fourier Transform Infra-red Spectroscopy (FTIR), and X-Ray Diffraction (XRD). All these analyses revealed that the lignocellulosic matrix was completely destroyed after the fungal treatment.","PeriodicalId":8824,"journal":{"name":"Biocatalysis and Biotransformation","volume":"41 1","pages":"309 - 321"},"PeriodicalIF":1.8,"publicationDate":"2022-06-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"43144120","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 3

Biocatalytic synthesis of dioctyl sebacate in toluene using an immobilised lipase 固定化脂肪酶在甲苯中的生物催化合成癸二酸二辛酯

IF 1.8 4区生物学

Biocatalysis and Biotransformation Pub Date : 2022-06-15 DOI: 10.1080/10242422.2022.2087512

Mingxin Zhu, Shuyi Guo, Rongchen Mang, Hua Zhou

{"title":"Biocatalytic synthesis of dioctyl sebacate in toluene using an immobilised lipase","authors":"Mingxin Zhu, Shuyi Guo, Rongchen Mang, Hua Zhou","doi":"10.1080/10242422.2022.2087512","DOIUrl":"https://doi.org/10.1080/10242422.2022.2087512","url":null,"abstract":"Abstract Sebacic esters have excellent lubricity, thermal stability, and biodegradability and therefore are widely used as aerospace lubricants, metal working oil, or engine oil. They are mainly produced by chemical synthesis which, however, may cause environmental pollution, its enzymatic synthesis represents a more environmentally friendly alternative. A few reports have described the synthesis of sebacic esters employing immobilised lipases, but these biocatalytic reactions were exclusively carried out in solvent-free systems and thus, could have been limited by slow reaction rates and high reaction temperatures due to poor enzyme dispersion, low substrate solubility, and high viscosity of the reaction mixture. The current study investigated the biosynthesis of dioctyl sebacate in toluene by Novozym 435, a commercial immobilised lipase. The reaction parameters were investigated using the single factor approach and an orthogonal array design. The optimal conditions obtained were as follows: 10 mL toluene, sebacic acid,1 mmol (202.25 mg); molar ratio of sebacic acid to 1-octanol, 1:3; Novozym 435, 0.03 g; 4 Å molecular sieves, 1.5 g; reaction temperature, 40 °C; reaction time, 30 h. A dioctyl sebacate conversion rate of 93% was achieved under these optimal conditions. In particular, the addition of molecular sieves to the reaction mixture markedly improved the product yield. The reaction temperature was low enough to make the operation easy and energy-efficient and therefore, well suited for large-scale production.","PeriodicalId":8824,"journal":{"name":"Biocatalysis and Biotransformation","volume":"41 1","pages":"395 - 402"},"PeriodicalIF":1.8,"publicationDate":"2022-06-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"44827323","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Comparative analysis of the white rot fungus Trametes hirsuta 072 laccases ability to modify 17β-oestradiol in the aqueous medium 白腐菌毛毡菌072漆酶在水溶液中修饰17β-雌二醇能力的比较分析

IF 1.8 4区生物学

Biocatalysis and Biotransformation Pub Date : 2022-06-13 DOI: 10.1080/10242422.2022.2085034

O. Savinova, P. N. Solyev, T. Fedorova, S. Kochetkov, T. Savinova

引用次数: 0

Remediation of chlorpyrifos in soil using immobilized bacterial consortium biostimulated with organic amendment 固定化菌群对土壤毒死蜱的修复研究

IF 1.8 4区生物学

Biocatalysis and Biotransformation Pub Date : 2022-06-09 DOI: 10.1080/10242422.2022.2085033

Elizabeth Mary John, J. Sreekumar, M. S. Jisha

引用次数: 0

A biocatalytic system obtained via immobilization of urease onto magnetic metal/alginate nanocomposite: Improving reusability and enhancing stability 磁性金属/海藻酸盐纳米复合材料固定化脲酶获得的生物催化体系：提高可重复使用性和稳定性

IF 1.8 4区生物学

Biocatalysis and Biotransformation Pub Date : 2022-06-01 DOI: 10.1080/10242422.2022.2082871

O. Almaghrabi, Y. Almulaiky

{"title":"A biocatalytic system obtained via immobilization of urease onto magnetic metal/alginate nanocomposite: Improving reusability and enhancing stability","authors":"O. Almaghrabi, Y. Almulaiky","doi":"10.1080/10242422.2022.2082871","DOIUrl":"https://doi.org/10.1080/10242422.2022.2082871","url":null,"abstract":"Abstract Alginate is a biomaterial that is considered suitable for enzyme immobilization. The biocompatibility and characteristics of the immobilized system can be improved by combining alginate with magnetite Fe3O4 nanoparticles. Therefore, the current study investigated the effect of magnetite Fe3O4 NPs on urease immobilization using different concentrations of magnetite Fe3O4 NPs. The morphological features for alginate/magnetite Fe3O4 NPs before and after immobilization were studied using an SEM, TGA, and FTIR. The reusability, half-life, enzymatic kinetics, and storage stability of the enzyme were all enhanced. The immobilization efficiency was determined to be 91% at optimal conditions. The immobilized urease was reused 20 times and a recovery of 59% of the initial activity. The soluble and immobilized urease was stored at 4 °C for 12 weeks and preserved 13% and 49% of the initial activities, respectively. The optimum pH for soluble and immobilized urease activity was estimated to be 7. The optimum temperature for soluble and immobilized urease activity was found to be 35 °C and 40 °C, respectively. The kinetics parameters showed the Vmax of 4.4 and 3.1 μmol/ml·min and the Km of 49.5 and 54.6 mM for the soluble and immobilized urease, respectively. Immobilized urease had a half-life of 11–20 min. The activation energy (Ea) of immobilized urease was determined to be 32 kJ K−1 mol−1, indicating that a small quantity of energy is required to produce the activated complex of substrate hydrolysis.","PeriodicalId":8824,"journal":{"name":"Biocatalysis and Biotransformation","volume":"41 1","pages":"456 - 465"},"PeriodicalIF":1.8,"publicationDate":"2022-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"47825227","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 6

Thermo-active and alkaliphilic amalgamated laccase immobilized on sodium alginate for synthetic dye decolourization 海藻酸钠固定化热活性亲碱汞化漆酶用于合成染料脱色

IF 1.8 4区生物学

Biocatalysis and Biotransformation Pub Date : 2022-05-24 DOI: 10.1080/10242422.2022.2078661

Chiedu E. Edoamodu, Uchechukwu U. Nwodo

引用次数: 1

Biotransformation of chalcones and flavanones: An update on their bio-based derivatizations 查尔酮和黄酮的生物转化:其生物基衍生化的最新进展

IF 1.8 4区生物学

Biocatalysis and Biotransformation Pub Date : 2022-05-18 DOI: 10.1080/10242422.2022.2073226

L. Aguiar, E. Silva, J. David

引用次数: 0

Biotransformation of curcumin and structure–activity relationship (SAR) of its analogues: A systematic review 姜黄素的生物转化及其类似物的构效关系综述