Biocatalysis and Biotransformation最新文献_第10页

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

Trametes versicolour laccase immobilization by covalent binding and its application in Kraft E1 effluent pre-treated with ozone 共价结合固定彩板菌漆酶及其在臭氧预处理卡夫E1废水中的应用

IF 1.8 4区生物学

Biocatalysis and Biotransformation Pub Date : 2022-03-15 DOI: 10.1080/10242422.2022.2051495

M. Assalin, M. A. Rosa, N. Durán

{"title":"Trametes versicolour laccase immobilization by covalent binding and its application in Kraft E1 effluent pre-treated with ozone","authors":"M. Assalin, M. A. Rosa, N. Durán","doi":"10.1080/10242422.2022.2051495","DOIUrl":"https://doi.org/10.1080/10242422.2022.2051495","url":null,"abstract":"Abstract Wastewater deriving from cellulose and paper manufacturing is one of the most important industrial effluents due to its large-volume production and high pollution load. Effluent deriving from the pulp bleaching stage (Kraft E1 effluent) remains one of the major issues faced by paper mills among all wastewaters generated in each stage of paper-making processes. Kraft E1 effluent was submitted to a sequential chemical (ozonization) – biological (immobilized laccase) treatment. Laccase was obtained from Trametes versicolour in liquid medium of culture using 2,5 -xylidine as inducer. Crude laccase extract was immobilized through covalent binding in Montmorillonite KSF and Eupergit®C supports based on different protocols. Eupergit®C has shown the best protein immobilization (51%), retention activity (100%), and operational stability (ten oxidative cycles) results. Enzymatic treatments using free and immobilized laccase onto Eupergit®C were applied to Kraft E1 effluent. After 18-h treatment, total phenol removal reached 20% and 40% in free and immobilized laccase, respectively. Ozone combined to enzymatic processes using reactor assembled with immobilized laccase (31 U g−1, total mass = 10.0 g) had effect on decolonization efficiency and on total phenols’ removal from Kraft effluent. Ozone treatment was capable of removing 52% of total phenols and 76% of colour from the investigated effluent. Sequential enzymatic treatment has increased total phenols’ removal to 64% within 30-minute treatment and reached 70% removal within 60 minutes. The herein observed additional phenol removal based on enzymatic treatment is an important outcome if one takes into consideration the fraction of total phenols that could not be removed by the ozone process.","PeriodicalId":8824,"journal":{"name":"Biocatalysis and Biotransformation","volume":"41 1","pages":"270 - 278"},"PeriodicalIF":1.8,"publicationDate":"2022-03-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"48798662","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

Enhancement of cellulase production by co-culture of Streptomyces ambofaciens OZ2 and Cytobacillus oceanisediminis OZ5 isolated from rumen samples 双歧杆菌OZ2和海洋细胞芽孢杆菌OZ5共同培养瘤胃纤维素酶产量的研究

IF 1.8 4区生物学

Biocatalysis and Biotransformation Pub Date : 2022-02-11 DOI: 10.1080/10242422.2022.2038581

M. Baltaci

{"title":"Enhancement of cellulase production by co-culture of Streptomyces ambofaciens OZ2 and Cytobacillus oceanisediminis OZ5 isolated from rumen samples","authors":"M. Baltaci","doi":"10.1080/10242422.2022.2038581","DOIUrl":"https://doi.org/10.1080/10242422.2022.2038581","url":null,"abstract":"Abstract Cellulose is considered to be an alternative form of energy, and has recently gained significance representing millions of dollars for countries that have the opportunity to obtain energy from it. At the same time, cellulosic biomaterials are attractive since they are both cheap and abundant. To use this important resource, its stubborn structure must be broken down. Rumen bacteria are regarded as unique for this job. In this study, 17 cellulolytic bacteria were isolated from rumen samples collected from Erzurum slaughterhouses. Three bacteria (OZ2, OZ5, OZ17) with maximum enzyme activity were identified by sequencing the 16S rRNA gene region. As a result of the sequence analysis, it was determined that isolates belong to Streptomyces ambofaciens OZ2, Cytobacillus oceanisediminis OZ5, and Streptomyces violaceochromogenes OZ17. Then, cellulase production potentials of these identified bacteria were investigated as single and co-cultures. The co-culture of OZ2 and OZ5 demonstrated the best cellulase activity (26 U/mL). As a result of the optimization studies for the co-culture of OZ2 and OZ5, the best culture conditions were 3 g/L yeast extract, 60 h incubation time, pH 6, and temperature 35 °C. Under optimized conditions, the cellulase enzyme activity increased approximately 3.5-fold to 56 U/mL.","PeriodicalId":8824,"journal":{"name":"Biocatalysis and Biotransformation","volume":"40 1","pages":"144 - 152"},"PeriodicalIF":1.8,"publicationDate":"2022-02-11","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"45526707","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: 5

Kinetic resolution of racemic benzofused alcohols catalysed by HMFO variants in presence of natural deep eutectic solvents 天然深共晶溶剂存在下HMFO变体催化外消旋苯并稠醇的动力学拆分

IF 1.8 4区生物学

Biocatalysis and Biotransformation Pub Date : 2022-02-11 DOI: 10.1080/10242422.2022.2038582

G. de Gonzalo, Nikola Lončar, M. Fraaije

引用次数: 1

Preparation of enantiopure pregabalin intermediate using cross linked enzyme aggregates (CLEAs) in basket reactor 在篮式反应器中用交联酶聚集体（CLEAs）制备对映体普瑞巴林中间体

IF 1.8 4区生物学

Biocatalysis and Biotransformation Pub Date : 2022-01-31 DOI: 10.1080/10242422.2021.2023507

Shalini Basetty, T. Kumaraguru

{"title":"Preparation of enantiopure pregabalin intermediate using cross linked enzyme aggregates (CLEAs) in basket reactor","authors":"Shalini Basetty, T. Kumaraguru","doi":"10.1080/10242422.2021.2023507","DOIUrl":"https://doi.org/10.1080/10242422.2021.2023507","url":null,"abstract":"Abstract Route to the synthesis of enantiomerically pure ethyl (S)-3-cyano-5-methylhexanoate, (S)-5, a key chiral intermediate for Pregabalin has been improved. The racemic β-cyano diester, 3 was prepared in 98% purity via gelatine catalysed Knoevenagel condensation of diethylmalonate with isovaleraldehyde followed by hydrocyantion of α,β-unsaturated diester 14 using acetone cyanohydrin and K2CO3. Racemic diethyl 2-(1-cyano-3-methylbutyl)malonate, rac-3, has been resolved using lipase from Thermomyces lanuginosus immobilised in form of crosslinked enzyme aggregates, CLEAs. The CLEAs were made by employing commercial soymilk as an additional protein source and a reaction was carried out in a moving basket reactor. The immobilised enzyme was found to be stable in many organic solvents and temperature up to 50 °C. The resolution reaction was studied in a basket reactor at 50% substrate loading in calcium acetate buffer, pH 7.5 at 30 °C by using 20% w/w enzyme loading. The apparent kinetic parameters were V max,app = (8.74 ± 0.43) mM/h/g and K m,app = (1.5 ± 0.07) M (correlation coeff. r = 0.98). The desired ethyl (S)-3-cyano-5-methylhexanoate, (S)-5 is obtained in 90-92% theoretical yield and e.e > 99%. The advantages of this improved process are mild reaction conditions; an alternate method for hydrocyanation step avoiding the use of highly toxic potassium cyanide at large scale operation and an immobilised enzyme that can be reused for at least 11 recycles.","PeriodicalId":8824,"journal":{"name":"Biocatalysis and Biotransformation","volume":"41 1","pages":"208 - 221"},"PeriodicalIF":1.8,"publicationDate":"2022-01-31","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"46898856","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