Biocatalysis and Biotransformation最新文献_第9页

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

IF 1.8 4区生物学

Biocatalysis and Biotransformation Pub Date : 2022-05-11 DOI: 10.1080/10242422.2022.2073227

N. Aminudin, Nurul Aqilah Amran, Zaima Azira Zainal Abidin, D. Susanti

引用次数: 2

Preparation of optically active cyanohydrins from 2-substituted benzaldehydes using a hydroxynitrile lyase from Pouteria sapota seeds immobilized on celite 用固定化紫菜种子的羟基腈裂解酶从2-取代苯甲醛制备旋光性氰醇

IF 1.8 4区生物学

Biocatalysis and Biotransformation Pub Date : 2022-05-11 DOI: 10.1080/10242422.2022.2070430

A. Solís, Abraham Cano, R. M. Martínez-Cásares, M. Solís-Oba, R. Castro-Rivera, Oscar Velázquez Flores

{"title":"Preparation of optically active cyanohydrins from 2-substituted benzaldehydes using a hydroxynitrile lyase from Pouteria sapota seeds immobilized on celite","authors":"A. Solís, Abraham Cano, R. M. Martínez-Cásares, M. Solís-Oba, R. Castro-Rivera, Oscar Velázquez Flores","doi":"10.1080/10242422.2022.2070430","DOIUrl":"https://doi.org/10.1080/10242422.2022.2070430","url":null,"abstract":"Abstract The HNL from the defatted meal of the seeds of Pouteria sapota (PsHNL) was extracted with water, and the aqueous extract was immobilized over celite or lyophilized and used as semi-purified PsHNL. The aqueous extract was mixed with celite, ratios 1:1, 1:2 and 1:4, and lyophilized. The immobilized PsHNLdir-celite catalysed the addition of HCN to 1b in buffer saturated-DIPE (microaqueous system) with high enantioselectivity in the first cycle but diminished in the next two cycles, best results were obtained with the ratio 1:4. The reaction with PsHNLdir-celite in biphasic medium (5% citrates buffer) improved the conversion compared with the microaqueous system, but it was still lower to that obtained with the PsHNL. Other way of immobilization studied was the precipitation of the enzyme with acetone and immobilization on celite, the PsHNLpp-celite catalysed the enantioselective addition of HCN to 2-fluoro (1a), 2-chloro (1b), 2-bromo (1c), 2-methyl (1d) and 2-nitro (1e) benzaldehydes, in the biphasic medium (1:4 ratio, 5% citrates buffer). The enantiomeric excess (ee) of (R)-2a, (R)-2b, (R)-2c and (R)-2d were >98% and remained during the three cycles. The ee of 2-nitromandelonitrile was 82% and was raised to 95% in the third cycle. Compared with the PsHNL, the conversion of 1a and 1b diminished 6% and 40%, respectively, after third cycle; for 2c, conversion was almost 10% higher in the first two cycles and diminished 19% in the third; for 2d and 2e the conversion was between 18–13% and 31–18% higher, respectively.","PeriodicalId":8824,"journal":{"name":"Biocatalysis and Biotransformation","volume":"41 1","pages":"344 - 352"},"PeriodicalIF":1.8,"publicationDate":"2022-05-11","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"48062976","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

Metal-organic framework based on iron and terephthalic acid as a multiporous support for lipase Burkholderia lata LBBIO-BL02 and its potential for biocatalysis 基于铁和对苯二甲酸的金属有机骨架作为脂肪酶LBBIO-BL02的多孔载体及其生物催化潜力

IF 1.8 4区生物学

Biocatalysis and Biotransformation Pub Date : 2022-05-02 DOI: 10.1080/10242422.2022.2068371

A. M. Baron, Ricardo de Sousa Rodrigues, Luis Guilherme Giannina Sante, Jocácia Muriele de Miranda Kister, Valéria Marta Gomes do Nascimento, Alesandro Bail

{"title":"Metal-organic framework based on iron and terephthalic acid as a multiporous support for lipase Burkholderia lata LBBIO-BL02 and its potential for biocatalysis","authors":"A. M. Baron, Ricardo de Sousa Rodrigues, Luis Guilherme Giannina Sante, Jocácia Muriele de Miranda Kister, Valéria Marta Gomes do Nascimento, Alesandro Bail","doi":"10.1080/10242422.2022.2068371","DOIUrl":"https://doi.org/10.1080/10242422.2022.2068371","url":null,"abstract":"Abstract Metal-organic frameworks (MOFs) are versatile materials because they have a large internal surface area and tuneable pores, making them suitable for enzyme immobilization. In this study, we prepared a typical microporous Fe-BDC MOF through a thermal treatment to produce additional meso and macropores interconnected to each other, capable of immobilizing the Burkholderia lata LBBIO-BL02 (BLL) lipase by entrapment and physical adsorption. The immobilization efficiency (E) was 90%, and the activity retention (R) was 400% (pNPP hydrolysis). The immobilized lipase (BLL@BDC) also showed excellent activity in the hydrolysis of vegetable oils in aqueous medium, achieving up to 3,200 U g−1 for olive oil, as well as high stability in organic solvents, especially for polar ones, such as iso-propanol (101.5 ± 2.6%), ethanol (103.0 ± 6.0%) and acetone (107.7 ± 8.3%). The results indicate that the multiporous Fe-BDC MOF is a promising support for lipase immobilization and further application in biocatalysis performed in organic media. Graphical Abstract","PeriodicalId":8824,"journal":{"name":"Biocatalysis and Biotransformation","volume":"41 1","pages":"332 - 343"},"PeriodicalIF":1.8,"publicationDate":"2022-05-02","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"48516749","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: 1

Protease immobilization on activated chitosan/cellulose acetate electrospun nanofibrous polymers: Biochemical characterization and efficient protein waste digestion 活化壳聚糖/醋酸纤维素电纺丝纳米纤维聚合物的蛋白酶固定化:生化表征和高效蛋白质废物消化

IF 1.8 4区生物学

Biocatalysis and Biotransformation Pub Date : 2022-03-31 DOI: 10.1080/10242422.2022.2056450

Arastoo Badoei-dalfard, Mahla Saeed, Z. Karami

{"title":"Protease immobilization on activated chitosan/cellulose acetate electrospun nanofibrous polymers: Biochemical characterization and efficient protein waste digestion","authors":"Arastoo Badoei-dalfard, Mahla Saeed, Z. Karami","doi":"10.1080/10242422.2022.2056450","DOIUrl":"https://doi.org/10.1080/10242422.2022.2056450","url":null,"abstract":"Abstract In this paper, a Serratia marcescens fibrinolytic protease KD was covalently immobilized onto the electrospun prepared glutaraldehyde (GA)-functionalized chitosan/cellulose acetate membrane nanofibres. Enzyme immobilization has been optimized at some conditions such as different GA values, different crosslinking times, different enzyme and pH values, and different times of immobilization. Results exhibited that the optimized immobilization conditions were obtained in 5.0% GA, after 4 h of crosslinking time, after 8 h immobilization time, using 210 mg protein/g support at pH 9.0. Based on these optimal conditions, the best encapsulation yield (EY) and activity recovery (AR) were obtained about 85% and 121.3%, respectively. The immobilized protease showed a 52% enhancement in protease activity than the free protease in pH 10. Furthermore, results displayed that the V max values of free and immobilized enzymes towards casein were gained 0.491 and 0.79 µmol/min, respectively. Moreover, the activity of immobilized protease was retained about 75% after incubation at 60 °C for 180 min at pH 9.0, in which the free protease only preserved about 20% of its primary activity. Results exhibited that the protease-NFs kept nearly 73% of its initial activity after three weeks of storage, while the free protease retained about 20% of its initial activity at the same condition. Results showed that the free protease exhibited 31% clot lysis, whereas the immobilized enzyme exhibited 39% clot lysis. The highest hydrolysis value of both proteases was done 17 and 48% after 4 h at 40 °C, respectively. These results indicated that Chit/CA electrospun nanofibres are excellent membranes for protease immobilization with high application in the digestion of protein waste.","PeriodicalId":8824,"journal":{"name":"Biocatalysis and Biotransformation","volume":"41 1","pages":"279 - 298"},"PeriodicalIF":1.8,"publicationDate":"2022-03-31","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"49096601","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: 1

Microbial degradation of lignocellulosic biomass for bioenergy production: A metagenomic-based approach 微生物降解木质纤维素生物质用于生物能源生产:基于宏基因组的方法

IF 1.8 4区生物学

Biocatalysis and Biotransformation Pub Date : 2022-03-30 DOI: 10.1080/10242422.2022.2056451

Nidhi Singh, V. Singh, M. P. Singh

引用次数: 3

Melioration of enzymatic ethanol production from alkali pre-treated paddy straw promoted by addition of surfactant 表面活性剂对碱预处理稻草酶促乙醇生产的促进作用

IF 1.8 4区生物学

Biocatalysis and Biotransformation Pub Date : 2022-03-29 DOI: 10.1080/10242422.2022.2055469

Rimple Chaudhary, Jyoti Kaushal, Gursharan Singh, A. Kaur, S. Arya

引用次数: 5

LDAmy, an α-amylase from Colorado potato beetle (Leptinotarsa decemlineata) with transglycosylation activity LDAmy是一种从科罗拉多马铃薯甲虫(Leptinotarsa decemlineata)中提取的具有转糖基化活性的α-淀粉酶

IF 1.8 4区生物学

Biocatalysis and Biotransformation Pub Date : 2022-03-15 DOI: 10.1080/10242422.2022.2050707

C. Hámori, L. Kandra, G. Gyémánt

{"title":"LDAmy, an α-amylase from Colorado potato beetle (Leptinotarsa decemlineata) with transglycosylation activity","authors":"C. Hámori, L. Kandra, G. Gyémánt","doi":"10.1080/10242422.2022.2050707","DOIUrl":"https://doi.org/10.1080/10242422.2022.2050707","url":null,"abstract":"Abstract Potential of α-amylase from the gut of Leptinotarsa decemlineata (LDAmy) to catalyse transfer reactions was investigated. LDAmy as a component of insect gut extract showed significant transfer activity on reducing-end- and both-end-protected maltoheptamer substrates. Transfer reaction was examined using purified enzyme, 2-chloro-4-nitrophenyl β-d-glucopyranoside as acceptor and starch and maltooligosaccharides as donors. In addition to suitability of various donors, effect of pH and acetonitrile (MeCN) concentration were also studied. The reactions were followed using separation of reaction products by a reversed phase HPLC method. LDAmy catalysed the hydrolysis and transglycosylation of the both-end-protected substrate 4,6-O-benzylidene-4-nitrophenyl β-maltoheptaoside in parallel reactions. Shorter and longer both-end-protected products with degree of polymerization 4–10 were formed. Identification of products was carried out based on HPLC retention time, UV and mass spectra. Ratio of transglycosylation to hydrolysis reached 0.5 in presence of 20% MeCN as organic solvent. Aromatic protecting group at the non-reducing end was favourable for transfer reaction. Lack of the mobile loop and presence of more nonpolar aromatic moieties near to the active site may be the reason for the enhanced transfer activity of LDAmy based on the comparison of the sequence and structure of mammalian and insect-derived α-amylases. Highlights Transferase activity of Colorado potato beetle derived α-amylase LDAmy is presented. Effect of pH and organic co-solvent on transfer reaction of LDAmy were studied. Shorter and longer products were formed from a both-end protected maltoheptamer. The unusual transfer ability was explained by sequence differences of α-amylases.","PeriodicalId":8824,"journal":{"name":"Biocatalysis and Biotransformation","volume":"41 1","pages":"153 - 160"},"PeriodicalIF":1.8,"publicationDate":"2022-03-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"46055359","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: 2