Biocatalysis and Biotransformation最新文献_第10页

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":null,"pages":null},"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":null,"pages":null},"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":null,"pages":null},"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":null,"pages":null},"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":null,"pages":null},"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":null,"pages":null},"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