Biocatalysis and Biotransformation最新文献_第10页

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

Practical access to (S)-heterocyclic aromatic acetates via CAL-B/Na2CO3-deacylation and Mitsunobu reaction protocol 通过CAL-B/Na2CO3脱酰和Mitsunobu反应方案实际获得（S）-杂环芳族乙酸酯

IF 1.8 4区生物学

Biocatalysis and Biotransformation Pub Date : 2022-01-31 DOI: 10.1080/10242422.2022.2030726

Louisa Aribi‐Zouioueche, Mounia Merabet-Khelassi, Nabila Braïa, M. Toffano

引用次数: 1

Production, partial purification and efficacy of keratinase from Bacillus halotolerans L2EN1 isolated from the poultry farm of Himachal Pradesh as a potential laundry additive 喜马偕尔邦家禽养殖场分离的耐盐芽孢杆菌L2EN1角化酶的生产、部分纯化及功效研究

IF 1.8 4区生物学

Biocatalysis and Biotransformation Pub Date : 2022-01-22 DOI: 10.1080/10242422.2022.2029851

S. Devi, A. Chauhan, R. Bishist, N. Sankhyan, Kavita Rana, N. Sharma

{"title":"Production, partial purification and efficacy of keratinase from Bacillus halotolerans L2EN1 isolated from the poultry farm of Himachal Pradesh as a potential laundry additive","authors":"S. Devi, A. Chauhan, R. Bishist, N. Sankhyan, Kavita Rana, N. Sharma","doi":"10.1080/10242422.2022.2029851","DOIUrl":"https://doi.org/10.1080/10242422.2022.2029851","url":null,"abstract":"Abstract To augment the keratinolytic ability of Bacillus halotolerans L2EN1 isolated from the poultry farm (Nahan, District Sirmour) of Himachal Pradesh, different cultural conditions were optimised using One Variable at a Time (OVAT) approach accompanied by Response Surface Methodology (RSM). Optimisation (OVAT) results revealed that after 3rd day of incubation, maximum enzyme activity was attained at 45 °C, pH 11.0 with 12.5% of inoculum size in the presence of Mn2 + and EDTA in the production medium. Sucrose (1.5%) and yeast extract (2.0%) were observed to be best carbon and nitrogen sources, respectively. A significant increase of 73.19 per cent in the keratinase activity was observed using Central Composite Design (CCD) of RSM. The SDS-PAGE results revealed that crude keratinase is a heterotetramer made up of four polypeptide chains with molecular weights of 17, 37, 40 and 60 kDa. Partial purification by 90 − 100 percent ammonium sulphate gave maximum keratinase production of 22.66 U/mL with purification of 1.68 and yield of 11.47 per cent. The enzyme showed compatibility with different commercial detergents and retained its activity in the order: Reshma (97.77%) > Speed (93.44%) > Tide (79.93%) >Ariel (70.18%) > Surf excel (67.98%) at 50 °C after 1 h of incubation. Wash performance analysis demonstrated that washing with tap water at 18, 28, 35 and 45 °C for 30, 45 and 60 min removed some amount of blood stains from the cotton cloth pieces. However, replacement of detergent’s enzyme (Reshma) with crude keratinase achieved complete blood stain removal under same conditions, suggesting its suitability as a potential cleaning additive in detergents for the removal of blood (proteinaceous) stains for long washing cycles (1 h).","PeriodicalId":8824,"journal":{"name":"Biocatalysis and Biotransformation","volume":"41 1","pages":"222 - 242"},"PeriodicalIF":1.8,"publicationDate":"2022-01-22","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"48111245","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: 4

Production of propionic acid through biotransformation of glucose and d-lactic acid by construction of synthetic acrylate pathway in metabolically engineered E. coli 在代谢工程大肠杆菌中构建合成丙烯酸酯途径生物转化葡萄糖和d-乳酸生产丙酸

IF 1.8 4区生物学

Biocatalysis and Biotransformation Pub Date : 2021-12-28 DOI: 10.1080/10242422.2021.2020760

Anitha Janet Roshni Yesudhas, Padmapriya Ganapathy Raman, Akila Thirumalai, Shuchi Saxena, R. Subramanian

{"title":"Production of propionic acid through biotransformation of glucose and d-lactic acid by construction of synthetic acrylate pathway in metabolically engineered E. coli","authors":"Anitha Janet Roshni Yesudhas, Padmapriya Ganapathy Raman, Akila Thirumalai, Shuchi Saxena, R. Subramanian","doi":"10.1080/10242422.2021.2020760","DOIUrl":"https://doi.org/10.1080/10242422.2021.2020760","url":null,"abstract":"Abstract Construction of an efficient synthetic acrylate pathway in recombinant hosts such as E. coli and lactic acid bacteria should lead to synthesis of an array of products such as propionic acid, β-alanine, α-amino butyric acid and other products. The major bottlenecks impeding the titre of propionic acid, from d-lactate via the acrylate pathway in Escherichia coli and Lactococcus lactis, mainly include regulatory hurdles, inefficiency of enzymes involved in production and inability to overexpress multiple enzymes in soluble functional form along with other factors. In this work, the three enzymes, propionyl-CoA transferase (Pct) and acryloyl-CoA reductase (Acr) from E. coli, and lactoyl-CoA dehydratase (Lcd) from Megasphaera elsdenii, that possess better kinetic parameters and reduced size, have been recruited based on the insights gained from kinetic modelling of the acrylate pathway. Secondly, a common strategy for functional expression of these pathway enzymes has been demonstrated to improve their specific activities. The expression levels of Pct, Acr and Lcd were enhanced by sorbitol-induced native folding, with exposure to heat and low expression temperature, resulting in 11-, 4- and 4-fold higher yield of soluble protein than in the control. The specific activities of Pct and Acr were 39- and 34-fold higher than Clostridium propionicum counterparts. Also, the enzyme activity of Lcd was equivalent to that in the native producer, C. propionicum. The recombinant strains exhibited 11% and 20% lesser growth rates than in the control with propionate titre of 240 mg/L and 320 mg/L when grown in glucose and d-lactate, respectively. The yields of propionic acid from glucose and lactic acid were 5% and 32%, respectively. Further improvement in yields should be achieved by expressing all the enzymes in sufficient amount and appropriate ratios, overcoming all the regulatory hurdles.","PeriodicalId":8824,"journal":{"name":"Biocatalysis and Biotransformation","volume":"41 1","pages":"26 - 37"},"PeriodicalIF":1.8,"publicationDate":"2021-12-28","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"44782484","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

Sequential optimization of bioprocess nutritional parameters for maximum l-asparaginase production from Pseudomonas aeruginosa BGR1I1 铜绿假单胞菌BGR1I1产l-天冬酰胺酶生物工艺营养参数的顺序优化

IF 1.8 4区生物学

Biocatalysis and Biotransformation Pub Date : 2021-12-22 DOI: 10.1080/10242422.2021.2018420

R. Dhingani, G. S. Shah, B. Joshi

{"title":"Sequential optimization of bioprocess nutritional parameters for maximum l-asparaginase production from Pseudomonas aeruginosa BGR1I1","authors":"R. Dhingani, G. S. Shah, B. Joshi","doi":"10.1080/10242422.2021.2018420","DOIUrl":"https://doi.org/10.1080/10242422.2021.2018420","url":null,"abstract":"Abstract l-Asparaginase enzyme belongs to the amidase group which carries out the deamination of asparagine to ammonia and aspartic acid. It has important applications in the pharmaceutical and food processing industries. Extensive screening of l-asparaginase producing bacteria from the rhizospheric soil was carried out. An efficient l-asparaginase producer was selected and identified by morphological, cultural, biochemical methods together with 16S rRNA sequencing as a Pseudomonas aeruginosa BGR1I1. A sequential optimization of bioprocess nutritional parameters was carried out using Plackett-Burman design (PBD) and response surface methodology (RSM) for maximum production of l-asparaginase from Pseudomonas aeruginosa BGR1I1. Fourteen processing variables were screened out using PBD. Four variables (glucose, asparagine, pH and time) found to be significantly affecting l-asparaginase production were further optimized by the central composite design of RSM. Maximum l-asparaginase enzyme activity (307 IU/mL) was obtained under the optimum concentration of glucose, 0.22% asparagine, 0.71% pH, 7.45 of modified M9 medium and incubation time 63 h which is 2.22-fold higher than in the basal medium.","PeriodicalId":8824,"journal":{"name":"Biocatalysis and Biotransformation","volume":"41 1","pages":"198 - 207"},"PeriodicalIF":1.8,"publicationDate":"2021-12-22","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"42017397","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

Immobilization and applications of esterases 酯酶的固定化及其应用

IF 1.8 4区生物学

Biocatalysis and Biotransformation Pub Date : 2021-12-21 DOI: 10.1080/10242422.2021.2013825

D. Sharma, K. Bhardwaj, Reena Gupta

引用次数: 4

Kinetic and docking study of synthesis of glyceryl monostearate by immobilized lipase in non-aqueous media 非水介质中固定化脂肪酶合成单硬脂酸甘油酯的动力学及对接研究

IF 1.8 4区生物学

Biocatalysis and Biotransformation Pub Date : 2021-12-07 DOI: 10.1080/10242422.2021.2003343

P. Jawale, B. Bhanage

{"title":"Kinetic and docking study of synthesis of glyceryl monostearate by immobilized lipase in non-aqueous media","authors":"P. Jawale, B. Bhanage","doi":"10.1080/10242422.2021.2003343","DOIUrl":"https://doi.org/10.1080/10242422.2021.2003343","url":null,"abstract":"Abstract Glyceryl monostearate is extensively used as an emulsifier in many industries. Mono acylation of glycerol was carried out by utilizing immobilized Candida antarctica lipase B (Cal B) as a biocatalyst and vinyl stearate as an acyl donor. Different reaction parameters, such as selection of lipases from various sources (like Candida antarctica, Candida rugosa, and Mucor meihei) and their quantity, shaking speed, temperature, substrate concentration, and reusability were studied in detail to achieve excellent conversion. Overall, 98% conversion of glycerol was obtained at a mole ratio of 1:1 of glycerol to vinyl stearate, using 12 mg of immobilized Cal B at 45 °C for 3 h. The mechanism of the given reaction was anticipated based on the results of the Lineweaver-Burk plots. It was found that the reaction followed the Ping-Pong Bi Bi mechanism with inhibition of glycerol. As it was a kinetically controlled synthesis, different kinetic constants were estimated by non-linear regression analysis. The activation energy for Cal B was found to be 10.3 kcal/mol. Further, biocatalyst can be reused up to four catalytic cycles with an average four percent loss of activity. A molecular docking study was done to find out the confirmation of substrates and their binding positions in an enzyme. It was noticed that the reaction proceeds through acyl-enzyme complex formation followed by the transfer of that acyl group to another substrate.","PeriodicalId":8824,"journal":{"name":"Biocatalysis and Biotransformation","volume":"41 1","pages":"123 - 132"},"PeriodicalIF":1.8,"publicationDate":"2021-12-07","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"47949610","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