Pub Date : 2022-08-25DOI: 10.1080/10242422.2022.2113517
Shilpa Saikia, M. Yadav, Rohida Amin Hoque, H. S. Yadav
Abstract Manganese peroxidase (MnP) plays an important role in the treatment of environmental pollutants existing around us. This review article covers all its recent potential applicability in a wide range of different areas, such as textile and food industry, in alcohol production, pulp and paper industry, in biofuel, in agriculture, in cosmetic wastes and in waste water treatment. MnP plays a potential role in biodegradation of phenolic compounds and non-phenolic substrates, dyes, and many xenobiotic compounds and in bioethanol production. This review article evaluates the important structural, catalytic cycle of MnP and its applications in the degradation of lignocellulosic waste, in industrial and biotechnological areas.
{"title":"Bioremediation mediated by manganese peroxidase – An overview","authors":"Shilpa Saikia, M. Yadav, Rohida Amin Hoque, H. S. Yadav","doi":"10.1080/10242422.2022.2113517","DOIUrl":"https://doi.org/10.1080/10242422.2022.2113517","url":null,"abstract":"Abstract Manganese peroxidase (MnP) plays an important role in the treatment of environmental pollutants existing around us. This review article covers all its recent potential applicability in a wide range of different areas, such as textile and food industry, in alcohol production, pulp and paper industry, in biofuel, in agriculture, in cosmetic wastes and in waste water treatment. MnP plays a potential role in biodegradation of phenolic compounds and non-phenolic substrates, dyes, and many xenobiotic compounds and in bioethanol production. This review article evaluates the important structural, catalytic cycle of MnP and its applications in the degradation of lignocellulosic waste, in industrial and biotechnological areas.","PeriodicalId":8824,"journal":{"name":"Biocatalysis and Biotransformation","volume":"41 1","pages":"161 - 173"},"PeriodicalIF":1.8,"publicationDate":"2022-08-25","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"46069710","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}
Pub Date : 2022-08-23DOI: 10.1080/10242422.2022.2113518
Anita Rani Santal, R. Rani, Anil Kumar, J. Sharma, N. Singh
{"title":"Biodegradation and detoxification of textile dyes using a novel bacterium Bacillus sp. AS2 for sustainable environmental cleanup","authors":"Anita Rani Santal, R. Rani, Anil Kumar, J. Sharma, N. Singh","doi":"10.1080/10242422.2022.2113518","DOIUrl":"https://doi.org/10.1080/10242422.2022.2113518","url":null,"abstract":"","PeriodicalId":8824,"journal":{"name":"Biocatalysis and Biotransformation","volume":" ","pages":""},"PeriodicalIF":1.8,"publicationDate":"2022-08-23","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"49369055","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}
Pub Date : 2022-08-09DOI: 10.1080/10242422.2022.2107919
Y. Bhandari, Hemlata Sajwan, Parul Pandita, V. Koteswara Rao
Abstract Biocatalysts can accelerate the catalysis of a chemical reaction that is difficult to synthesize with typical chemical methods. The global enzyme market size is predicted to expand at a CAGR of 6.5% from 2021 to 2028. Enzymatic reactions are highly chemo, regio, and stereoselective and produce various fine chemicals such as drugs, agrochemicals, and fragrance molecules. Peroxidases (PO) (EC 1.11.1.x) are a large class of enzymes that play an important role in various biological processes. Chloroperoxidase (CPO, EC 1.1.1.10) is a versatile fungal haem-thiolate protein that is useful in the asymmetric synthesis of chiral building blocks and has an important role in a number of biological processes. CPO’s main biological role is chlorination, although it also catalyses haem PO, catalase (CAT), and reactions similar to cytochrome P450. However, CPO performs both oxidation and stereo-specific halogenation of chemical molecules. The haem and vanadium POs are produced by Caldariomyces fumago, and Curvularia inaequalis, respectively, and are capable of halogenating the flavanones, naringenin, and hesperetin, at C-6 and C-8 in the presence of either Cl− or Br−. In this review, we discussed the various applications of CPO including synthesis of epoxides, drugs, halogenation of thymol, nitriles, the Aza-Achmatowicz reaction, and biomedical applications such as cancer and biosensors. In light of these novel features, we have provided a detailed review of CPOs and their applications in various stereoselective chemical transformations of industrial relevance.
{"title":"Chloroperoxidase applications in chemical synthesis of industrial relevance","authors":"Y. Bhandari, Hemlata Sajwan, Parul Pandita, V. Koteswara Rao","doi":"10.1080/10242422.2022.2107919","DOIUrl":"https://doi.org/10.1080/10242422.2022.2107919","url":null,"abstract":"Abstract Biocatalysts can accelerate the catalysis of a chemical reaction that is difficult to synthesize with typical chemical methods. The global enzyme market size is predicted to expand at a CAGR of 6.5% from 2021 to 2028. Enzymatic reactions are highly chemo, regio, and stereoselective and produce various fine chemicals such as drugs, agrochemicals, and fragrance molecules. Peroxidases (PO) (EC 1.11.1.x) are a large class of enzymes that play an important role in various biological processes. Chloroperoxidase (CPO, EC 1.1.1.10) is a versatile fungal haem-thiolate protein that is useful in the asymmetric synthesis of chiral building blocks and has an important role in a number of biological processes. CPO’s main biological role is chlorination, although it also catalyses haem PO, catalase (CAT), and reactions similar to cytochrome P450. However, CPO performs both oxidation and stereo-specific halogenation of chemical molecules. The haem and vanadium POs are produced by Caldariomyces fumago, and Curvularia inaequalis, respectively, and are capable of halogenating the flavanones, naringenin, and hesperetin, at C-6 and C-8 in the presence of either Cl− or Br−. In this review, we discussed the various applications of CPO including synthesis of epoxides, drugs, halogenation of thymol, nitriles, the Aza-Achmatowicz reaction, and biomedical applications such as cancer and biosensors. In light of these novel features, we have provided a detailed review of CPOs and their applications in various stereoselective chemical transformations of industrial relevance.","PeriodicalId":8824,"journal":{"name":"Biocatalysis and Biotransformation","volume":"41 1","pages":"403 - 420"},"PeriodicalIF":1.8,"publicationDate":"2022-08-09","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"47184745","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}
Pub Date : 2022-08-04DOI: 10.1080/10242422.2022.2107427
Anirudh Sharma, J. Melo, R. Prakash, N. Tejo Prakash
{"title":"Biomass suspension catalysed the generation of various alkyl esters from acid oil and virgin cottonseed oil","authors":"Anirudh Sharma, J. Melo, R. Prakash, N. Tejo Prakash","doi":"10.1080/10242422.2022.2107427","DOIUrl":"https://doi.org/10.1080/10242422.2022.2107427","url":null,"abstract":"","PeriodicalId":8824,"journal":{"name":"Biocatalysis and Biotransformation","volume":" ","pages":""},"PeriodicalIF":1.8,"publicationDate":"2022-08-04","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"41373618","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}
Pub Date : 2022-07-01DOI: 10.1080/10242422.2022.2094258
R. D. de Souza, Raquel A. C. Leão, Barbara Maia, M. Gomez
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.
摘要对映体纯仲醇可用于合成几种天然产物和作为活性药物中间体（API）。由于对这些手性化合物的高需求，在不对称合成和催化领域取得了很大进展。在这种情况下，生物催化与连续流技术一起可以成为一种有价值的工具，用于更通用和可持续的方法，具有更低的成本、更大的立体选择性和更少的环境影响。本工作旨在通过在连续流动条件下使用固定化南极假丝酵母脂肪酶B（Novozyme 435，N435）进行动力学拆分，获得具有工业意义的对映体纯醇（4-氟苯基）（呋喃-2-基）甲醇（3）。对间歇反应条件进行了初步优化研究。使用异辛烷作为溶剂获得最佳结果，37.7 mg的N435和三当量的乙酸异丙烯酯作为酰基供体，在60 °C 24 h.在这些条件下，获得49%的转化率和91的对映体比率。将优化的批处理条件转化为连续流反应器，在30 停留时间分钟、47%的转化率和61的对映体比率。
{"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}
Pub Date : 2022-06-17DOI: 10.1080/10242422.2022.2087510
B. Itakorode, R. E. Okonji, N. Torimiro
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.
{"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}
Pub Date : 2022-06-15DOI: 10.1080/10242422.2022.2087511
M. El-sheekh, Mohammed Y. Bedaiwy, Aya A. El-Nagar, Eman Elgammal
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.
{"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}
Pub Date : 2022-06-15DOI: 10.1080/10242422.2022.2087512
Mingxin Zhu, Shuyi Guo, Rongchen Mang, Hua Zhou
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.
{"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}
Pub Date : 2022-06-13DOI: 10.1080/10242422.2022.2085034
O. Savinova, P. N. Solyev, T. Fedorova, S. Kochetkov, T. Savinova
Abstract A comparative study of the ability of Trametes hirsuta laccase isoenzymes to biotransform 17β-oestradiol (3,17β-dihydroxyestra-1,3,5(10)-triene, E2) was carried out. Native major LacA and recombinant minor isoenzymes (rLacC, rLacD, and rLacF) obtained in Penicillium canescens were used. It was found that all the studied isozymes are capable of catalysing the oxidative coupling of E2 in an aqueous medium (22 ± 2 °C, pH 4.5) with the formation of predominantly dimers and trimers. Other concurrently formed products were detected by high-pressure liquid chromatography – high-resolution mass spectrometry (HPLC–HRMS) and characterized, summarizing the overall condensation pathway of E2 in laccases. The highest catalytic activity was observed for major LacA. For other laccases, the activity decreased in the following sequence rLacF > rLacD > rLacC. Utilization of T. hirsuta enzymatic variety of laccases can be of benefit for detoxification of phenol-like steroid compounds in the environment.
{"title":"Comparative analysis of the white rot fungus Trametes hirsuta 072 laccases ability to modify 17β-oestradiol in the aqueous medium","authors":"O. Savinova, P. N. Solyev, T. Fedorova, S. Kochetkov, T. Savinova","doi":"10.1080/10242422.2022.2085034","DOIUrl":"https://doi.org/10.1080/10242422.2022.2085034","url":null,"abstract":"Abstract A comparative study of the ability of Trametes hirsuta laccase isoenzymes to biotransform 17β-oestradiol (3,17β-dihydroxyestra-1,3,5(10)-triene, E2) was carried out. Native major LacA and recombinant minor isoenzymes (rLacC, rLacD, and rLacF) obtained in Penicillium canescens were used. It was found that all the studied isozymes are capable of catalysing the oxidative coupling of E2 in an aqueous medium (22 ± 2 °C, pH 4.5) with the formation of predominantly dimers and trimers. Other concurrently formed products were detected by high-pressure liquid chromatography – high-resolution mass spectrometry (HPLC–HRMS) and characterized, summarizing the overall condensation pathway of E2 in laccases. The highest catalytic activity was observed for major LacA. For other laccases, the activity decreased in the following sequence rLacF > rLacD > rLacC. Utilization of T. hirsuta enzymatic variety of laccases can be of benefit for detoxification of phenol-like steroid compounds in the environment.","PeriodicalId":8824,"journal":{"name":"Biocatalysis and Biotransformation","volume":"41 1","pages":"475 - 485"},"PeriodicalIF":1.8,"publicationDate":"2022-06-13","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"48801490","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}
Pub Date : 2022-06-09DOI: 10.1080/10242422.2022.2085033
Elizabeth Mary John, J. Sreekumar, M. S. Jisha
Pesticides released into the environment have become a danger to the mother earth arousing a worldwide alert to initiate remediation at the point sources of contamination in an ecofriendly way. The...
农药释放到环境中已经成为对地球母亲的威胁，引起了世界范围内对污染源进行生态修复的警惕。…
{"title":"Remediation of chlorpyrifos in soil using immobilized bacterial consortium biostimulated with organic amendment","authors":"Elizabeth Mary John, J. Sreekumar, M. S. Jisha","doi":"10.1080/10242422.2022.2085033","DOIUrl":"https://doi.org/10.1080/10242422.2022.2085033","url":null,"abstract":"Pesticides released into the environment have become a danger to the mother earth arousing a worldwide alert to initiate remediation at the point sources of contamination in an ecofriendly way. The...","PeriodicalId":8824,"journal":{"name":"Biocatalysis and Biotransformation","volume":"325 1","pages":""},"PeriodicalIF":1.8,"publicationDate":"2022-06-09","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"138515806","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}
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