Pub Date : 2024-01-29DOI: 10.1080/10242422.2024.2305969
Hsueh-Ling Cheng, Wei-Ting Hsu, Yu-Han Su, Yuan-Jia Lee, Huynh Nhu Tangthi, Chien-Ting Wu, Lin-Lee Lee
Enzymatic degradation of biomass is preferred over chemical methods for environmental protection. However, in most cases, a chemical pretreatment is still required to help improve enzyme accessibil...
{"title":"Cross-linked enzyme aggregates of xylanase, XynR8(N58D), for effective degradation of untreated lignocellulosic biomass","authors":"Hsueh-Ling Cheng, Wei-Ting Hsu, Yu-Han Su, Yuan-Jia Lee, Huynh Nhu Tangthi, Chien-Ting Wu, Lin-Lee Lee","doi":"10.1080/10242422.2024.2305969","DOIUrl":"https://doi.org/10.1080/10242422.2024.2305969","url":null,"abstract":"Enzymatic degradation of biomass is preferred over chemical methods for environmental protection. However, in most cases, a chemical pretreatment is still required to help improve enzyme accessibil...","PeriodicalId":8824,"journal":{"name":"Biocatalysis and Biotransformation","volume":"35 1","pages":""},"PeriodicalIF":1.8,"publicationDate":"2024-01-29","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"139577931","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}
6-Hydroxynicotinic acid emerged as a pivotal intermediate for fine chemicals. The current study aims to screen novel nicotinate dehydrogenase-producing strains. Based on the high-throughput UV colo...
{"title":"Screening of a novel and thermostable nicotinate dehydrogenase-producing strain Bacillus paramycoides for efficient synthesis of 6-hydroxynicotinic acid","authors":"Zhi Chen, Zhaohe Dong, Xin Ju, Lishi Yan, Liangzhi Li, Donzhi Wei","doi":"10.1080/10242422.2023.2289338","DOIUrl":"https://doi.org/10.1080/10242422.2023.2289338","url":null,"abstract":"6-Hydroxynicotinic acid emerged as a pivotal intermediate for fine chemicals. The current study aims to screen novel nicotinate dehydrogenase-producing strains. Based on the high-throughput UV colo...","PeriodicalId":8824,"journal":{"name":"Biocatalysis and Biotransformation","volume":"2014 18","pages":""},"PeriodicalIF":1.8,"publicationDate":"2023-12-03","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"138518472","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 : 2023-12-03DOI: 10.1080/10242422.2023.2289337
R. Shalini, K. Ravichandran, P. Kavitha, P. K. Praseetha, R. Mohan, P. Ravikumar
Specifically, biocatalyst coupled semiconductor photocatalysts have great potential towards the eco-friendly decomposition of toxic organic dyes that contaminate water bodies. This study reports th...
{"title":"Biocatalyst coupling with Mo-doped SnO2 nanoparticles for efficient photocatalytic dye degradation: An eco-friendly approach for environmental remediation","authors":"R. Shalini, K. Ravichandran, P. Kavitha, P. K. Praseetha, R. Mohan, P. Ravikumar","doi":"10.1080/10242422.2023.2289337","DOIUrl":"https://doi.org/10.1080/10242422.2023.2289337","url":null,"abstract":"Specifically, biocatalyst coupled semiconductor photocatalysts have great potential towards the eco-friendly decomposition of toxic organic dyes that contaminate water bodies. This study reports th...","PeriodicalId":8824,"journal":{"name":"Biocatalysis and Biotransformation","volume":"95 6","pages":""},"PeriodicalIF":1.8,"publicationDate":"2023-12-03","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"138518482","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 : 2023-11-24DOI: 10.1080/10242422.2023.2284116
Nicoly Subtil de Oliveira, Gabriel Pereira Lopes da Silva, Orozimbo Furlan, Lorena Carolina Peña, Luiz Fernando Bianchini, Nipuna Parahitiyawa, Edvaldo Antonio Ribeiro Rosa
Microbial biotransformation is valuable for obtaining pharmaceutical, nutritional, and cosmetical potential molecules. Basically, for its realization, only a parental molecule, a microorganism, and...
{"title":"The song remains the same. The lab bench dilemma of using shaken flasks in microbial biotransformation experiments","authors":"Nicoly Subtil de Oliveira, Gabriel Pereira Lopes da Silva, Orozimbo Furlan, Lorena Carolina Peña, Luiz Fernando Bianchini, Nipuna Parahitiyawa, Edvaldo Antonio Ribeiro Rosa","doi":"10.1080/10242422.2023.2284116","DOIUrl":"https://doi.org/10.1080/10242422.2023.2284116","url":null,"abstract":"Microbial biotransformation is valuable for obtaining pharmaceutical, nutritional, and cosmetical potential molecules. Basically, for its realization, only a parental molecule, a microorganism, and...","PeriodicalId":8824,"journal":{"name":"Biocatalysis and Biotransformation","volume":"2014 20","pages":""},"PeriodicalIF":1.8,"publicationDate":"2023-11-24","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"138518467","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}
Ketoreductases are widely explored for the reduction of prochiral ketones for the preparation of chiral alcohols. Though, the chiral Ir(III) catalyst has been used for the asymmetric reduction of k...
酮还原酶被广泛用于还原前手性酮以制备手性醇。然而，手性Ir(III)催化剂已被用于k的不对称还原。
{"title":"Enzymatic approach to the synthesis of chiral intermediate of Rodatristat ethyl","authors":"Deepthi Pulivarthi, Rakesh Goparaju, Ravinder Reddy Patlolla, Vinaykumar Allam, Anjali Priya Naik Kethavath, Linga Banoth, Subba Reddy BV","doi":"10.1080/10242422.2023.2281874","DOIUrl":"https://doi.org/10.1080/10242422.2023.2281874","url":null,"abstract":"Ketoreductases are widely explored for the reduction of prochiral ketones for the preparation of chiral alcohols. Though, the chiral Ir(III) catalyst has been used for the asymmetric reduction of k...","PeriodicalId":8824,"journal":{"name":"Biocatalysis and Biotransformation","volume":"2014 22","pages":""},"PeriodicalIF":1.8,"publicationDate":"2023-11-16","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"138518466","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 : 2023-11-10DOI: 10.1080/10242422.2023.2279009
Larissa Emanuelle da Silva Almeida, Sandra Aparecida de Assis
AbstractThe utilization of lignocellulosic materials for second-generation ethanol production via enzymatic catalysts is primarily hindered by enzyme cost. Enzymatic immobilization emerges as a viable solution, enabling enzyme reuse. This study investigated the immobilization of an enzymatic extract obtained from Moniliophthora perniciosa fermentation in calcium alginate spheres using the direct trapping method. Initial tests assessed β-glucosidase activity, showing that a higher concentration of calcium chloride (1 M) alongside larger diameter spheres yielded improved results. The immobilized enzyme was reused for up to 17 cycles without significant loss of activity. The percentage of reducing sugars after 48-h hydrolysis with the supplemented enzymatic extract was 226%, doubling the value achieved with only the free enzymatic extract. The immobilized enzyme retained 50% of its initial activity after 1 h at 80 °C, demonstrating higher activity at pH 6 and 60 °C. These findings suggest that this immobilization technique is simple, economically viable, and effective for the hydrolysis of pretreated sugarcane bagasse.HIGHLIGHTSSuccessful immobilization of M. perniciosa enzymatic extract achieved through direct entrapment in calcium alginate.Immobilized β-glucosidase demonstrates sustained activity over 16 reuse cycles, showcasing the potential for cost-effective bioconversion processes.Enhanced hydrolysis of sugarcane bagasse observed with immobilized enzymatic extract, indicating a promising approach for improved biomass utilization.Keywords: β-Glucosidase immobilizationmoniliophthora perniciosacalcium alginate spheressugarcane bagasse hydrolysisenzymatic bioconversionlignocellulosic ethanolreducing sugars AcknowledgmentsWe thank the Biotechnology Graduate Program of State University of Feira de Santana (UEFS/FIOCRUZ), the Coordenação de Aperfeiçoamento Pessoal de Nível Superior (CAPES) for a doctoral scholarship (88882.447813/2019-01), the Bahia State Research Support Foundation (FAPESB), and the National Council for Scientific and Technological Development (CNPq).Authors’ contributionsAll authors contributed to the study conception and design. Material preparation, data collection, and analysis were performed by Larissa E. S. Almeida and Sandra A. Assis. The first draft of the manuscript was written by Larissa E. S. Almeida, and all authors commented on previous versions of the manuscript. All authors read and approved the final manuscript.Disclosure statementNo potential conflict of interest was reported by the author(s).Additional informationFundingWe thank the Biotechnology Graduate Program of State University of Feira de Santana (UEFS/FIOCRUZ), the Coordenação de Aperfeiçoamento Pessoal de Nível Superior (CAPES) for a doctoral scholarship (88882.447813/2019-01), the Bahia State Research Support Foundation (FAPESB), and the National Council for Scientific and Technological Development (CNPq).
摘要利用木质纤维素材料通过酶催化生产第二代乙醇主要受到酶成本的阻碍。酶固定化作为一种可行的解决方案出现，使酶能够重复使用。本研究采用直接捕集法，研究了在海藻酸钙球中固定化黑霉菌发酵酶提取物的方法。最初的测试评估了β-葡萄糖苷酶的活性，表明更高浓度的氯化钙(1 M)和更大直径的球产生了更好的结果。固定化酶可重复使用17个循环而没有明显的活性损失。添加酶提取物48小时后，还原糖的百分比为226%，是仅添加游离酶提取物时的两倍。固定酶在80°C条件下1 h后仍保持50%的初始活性，在pH 6和60°C条件下表现出更高的活性。这些结果表明，这种固定化技术简单，经济可行，对预处理甘蔗渣的水解是有效的。通过直接包埋在海藻酸钙中，成功地固定化了perniciosa酶提取物。固定化β-葡萄糖苷酶在16次重复使用循环中表现出持续的活性，显示了具有成本效益的生物转化过程的潜力。固定化酶提取物对蔗渣的水解作用增强，为提高生物质利用率提供了一条有前途的途径。关键词:我们感谢费拉·德·桑塔纳州立大学生物技术研究生项目(UEFS/FIOCRUZ)、协调委员会(CAPES)为我们提供的博士奖学金(88882.447813/2019-01)、巴伊亚州立研究支持基金会(FAPESB)、巴伊亚州立研究支持基金会(FAPESB)、巴伊亚州立研究支持基金会(FAPESB)。国家科学技术发展委员会。作者的贡献所有作者都对研究的构思和设计做出了贡献。材料准备、数据收集和分析由Larissa E. S. Almeida和Sandra A. Assis完成。手稿的初稿是由Larissa E. S. Almeida撰写的，所有作者都对以前的手稿版本进行了评论。所有作者都阅读并批准了最终的手稿。披露声明作者未报告潜在的利益冲突。我们感谢费拉·德·桑塔纳州立大学生物技术研究生项目(UEFS/FIOCRUZ)、技术合作与发展协调委员会(CAPES)提供的博士奖学金(88882.447813/2019-01)、巴伊亚州研究支持基金会(FAPESB)和国家科学技术发展委员会(CNPq)。
{"title":"Calcium alginate-immobilized β-glucosidase from <i>Moniliophthora perniciosa</i> : characterization and sugarcane bagasse hydrolysis","authors":"Larissa Emanuelle da Silva Almeida, Sandra Aparecida de Assis","doi":"10.1080/10242422.2023.2279009","DOIUrl":"https://doi.org/10.1080/10242422.2023.2279009","url":null,"abstract":"AbstractThe utilization of lignocellulosic materials for second-generation ethanol production via enzymatic catalysts is primarily hindered by enzyme cost. Enzymatic immobilization emerges as a viable solution, enabling enzyme reuse. This study investigated the immobilization of an enzymatic extract obtained from Moniliophthora perniciosa fermentation in calcium alginate spheres using the direct trapping method. Initial tests assessed β-glucosidase activity, showing that a higher concentration of calcium chloride (1 M) alongside larger diameter spheres yielded improved results. The immobilized enzyme was reused for up to 17 cycles without significant loss of activity. The percentage of reducing sugars after 48-h hydrolysis with the supplemented enzymatic extract was 226%, doubling the value achieved with only the free enzymatic extract. The immobilized enzyme retained 50% of its initial activity after 1 h at 80 °C, demonstrating higher activity at pH 6 and 60 °C. These findings suggest that this immobilization technique is simple, economically viable, and effective for the hydrolysis of pretreated sugarcane bagasse.HIGHLIGHTSSuccessful immobilization of M. perniciosa enzymatic extract achieved through direct entrapment in calcium alginate.Immobilized β-glucosidase demonstrates sustained activity over 16 reuse cycles, showcasing the potential for cost-effective bioconversion processes.Enhanced hydrolysis of sugarcane bagasse observed with immobilized enzymatic extract, indicating a promising approach for improved biomass utilization.Keywords: β-Glucosidase immobilizationmoniliophthora perniciosacalcium alginate spheressugarcane bagasse hydrolysisenzymatic bioconversionlignocellulosic ethanolreducing sugars AcknowledgmentsWe thank the Biotechnology Graduate Program of State University of Feira de Santana (UEFS/FIOCRUZ), the Coordenação de Aperfeiçoamento Pessoal de Nível Superior (CAPES) for a doctoral scholarship (88882.447813/2019-01), the Bahia State Research Support Foundation (FAPESB), and the National Council for Scientific and Technological Development (CNPq).Authors’ contributionsAll authors contributed to the study conception and design. Material preparation, data collection, and analysis were performed by Larissa E. S. Almeida and Sandra A. Assis. The first draft of the manuscript was written by Larissa E. S. Almeida, and all authors commented on previous versions of the manuscript. All authors read and approved the final manuscript.Disclosure statementNo potential conflict of interest was reported by the author(s).Additional informationFundingWe thank the Biotechnology Graduate Program of State University of Feira de Santana (UEFS/FIOCRUZ), the Coordenação de Aperfeiçoamento Pessoal de Nível Superior (CAPES) for a doctoral scholarship (88882.447813/2019-01), the Bahia State Research Support Foundation (FAPESB), and the National Council for Scientific and Technological Development (CNPq).","PeriodicalId":8824,"journal":{"name":"Biocatalysis and Biotransformation","volume":" 859","pages":"0"},"PeriodicalIF":0.0,"publicationDate":"2023-11-10","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"135186344","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 : 2023-11-01DOI: 10.1080/10242422.2023.2274815
Heidi Mohamed Abdel-Mageed, Shahinaze A. Fouad, Dina Nada, Rana R. Makar, Mahmoud H. Teaima, Nesrine Abdelrehim EL Gohary, Nermeen Z. AbuelEzz
AbstractEnzymes are challenging to formulate due to their inherent instability, particularly in solution. This study aims to use the design of experiment (DOE) approach to develop spray-dried encapsulated trypsin nano-powder (TrySP) with maximum activity and stability using a Büchi B-90 nano spray dryer. A 53 full factorial design with 26 randomly ordered experiments was created to study the impact of process variables on the quality attributes of TrySP. The additive concentration (%), mesh cap size (μm), inlet temperature (Tinlet) (°C), trypsin concentration (%), and additive type (Mannitol or trehalose) were selected as the independent variables. The dependent parameters were yield value, particle size, residual enzyme activity, and moisture content. Further, comparative physicochemical and kinetic characterization of TrySP was performed. TrySP had diverse qualities (yield value 60.2–96.8%, residual activity >90–50%, particle size 314–1030 nm, and moisture content 0.7–2.2%). Optimized TrySP exhibited 89% yield value and 95% residual activity in the presence of 8% (w/w) mannitol. Kcat of TypSP increased from 22.5/s to 25.6/s with improved operational and storage stabilities. The half-life (t1/2) of TrySP showed 6 folds increase. Furthermore, TrySP activation energy increased from 45,918 J/mol to 94,491 J/mol. The sustainable model presented in this study enables the development of a thermostable, encapsulated trypsin nano-powder with physical and chemical properties that are optimized for various biotechnological industrial applications.Keywords: Büchi B-90 spray dryingdesign of experimentsimmobilizationtrypsin enzyme formulationkinetic parametersnano powder Authors’ contributionsHM established, designed, and carried out some of the experiments, assisted with data analysis, and wrote the majority of the manuscript. SA and NZ co-developed the concept, designed some of the experiments, assisted with the analysis of data, and revised the written material. MT set up, carried out, and analyzed the factorial design, as well as writing the appropriate manuscript parts. DN, RM, and NA, carried out the experimental part and reviewed the written. The final manuscript was read and approved by all authors.Disclosure statementNo potential conflict of interest was reported by the author(s).Data availability statementThe datasets generated during and/or analyzed during the present study are provided by corresponding author upon request.Additional informationFundingOpen access funding is provided by Science, Technology and Innovation Funding Authority (STDF) in cooperation with The Egyptian Knowledge Bank (EKB). The authors did not receive any external funding from any organization for the submitted work.
酶由于其固有的不稳定性，特别是在溶液中，因此具有挑战性。本研究旨在采用实验设计(DOE)的方法，在b chi B-90纳米喷雾干燥机上开发具有最大活性和稳定性的胰蛋白酶包封纳米粉(TrySP)。采用53个全因子设计，26个随机排序试验，研究工艺变量对TrySP品质属性的影响。选取添加剂浓度(%)、网帽尺寸(μm)、进口温度(Tinlet)(°C)、胰蛋白酶浓度(%)和添加剂类型(甘露醇或海藻糖)作为自变量。相关参数为产率值、粒径、残留酶活性和水分含量。进一步进行了TrySP的比较理化和动力学表征。TrySP品质多样，产率60.2 ~ 96.8%，残留活性>90 ~ 50%，粒径314 ~ 1030 nm，含水率0.7 ~ 2.2%。优化后的TrySP在8% (w/w)甘露醇存在下的产率为89%，残留活性为95%。TypSP的Kcat从22.5/s提高到25.6/s，提高了操作和存储稳定性。TrySP的半衰期(t1/2)增加了6倍。TrySP的活化能由45,918 J/mol增加到94,491 J/mol。本研究中提出的可持续模型使开发具有物理和化学特性的热稳定、封装胰蛋白酶纳米粉末成为可能，该粉末可用于各种生物技术工业应用。关键词:b chi B-90喷雾干燥实验设计简化酶制剂动力学参数纳米粉体作者贡献shm建立、设计并进行了部分实验，协助数据分析，并撰写了大部分稿件。SA和NZ共同提出了概念，设计了一些实验，协助分析数据，并修改了书面材料。MT设置，进行，分析因子设计，并撰写相应的手稿部分。DN, RM, NA进行了实验部分，并复习了所写的内容。最后的手稿被所有作者阅读并批准。披露声明作者未报告潜在的利益冲突。数据可用性声明本研究过程中产生和/或分析的数据集由通讯作者应要求提供。资金开放获取资金由科学、技术和创新资助局(STDF)与埃及知识银行(EKB)合作提供。作者未因提交的工作从任何组织获得任何外部资助。
{"title":"A design of experiment approach for optimized production of encapsulated trypsin using nano spray drying: Comparative physicochemical and kinetic characterization","authors":"Heidi Mohamed Abdel-Mageed, Shahinaze A. Fouad, Dina Nada, Rana R. Makar, Mahmoud H. Teaima, Nesrine Abdelrehim EL Gohary, Nermeen Z. AbuelEzz","doi":"10.1080/10242422.2023.2274815","DOIUrl":"https://doi.org/10.1080/10242422.2023.2274815","url":null,"abstract":"AbstractEnzymes are challenging to formulate due to their inherent instability, particularly in solution. This study aims to use the design of experiment (DOE) approach to develop spray-dried encapsulated trypsin nano-powder (TrySP) with maximum activity and stability using a Büchi B-90 nano spray dryer. A 53 full factorial design with 26 randomly ordered experiments was created to study the impact of process variables on the quality attributes of TrySP. The additive concentration (%), mesh cap size (μm), inlet temperature (Tinlet) (°C), trypsin concentration (%), and additive type (Mannitol or trehalose) were selected as the independent variables. The dependent parameters were yield value, particle size, residual enzyme activity, and moisture content. Further, comparative physicochemical and kinetic characterization of TrySP was performed. TrySP had diverse qualities (yield value 60.2–96.8%, residual activity >90–50%, particle size 314–1030 nm, and moisture content 0.7–2.2%). Optimized TrySP exhibited 89% yield value and 95% residual activity in the presence of 8% (w/w) mannitol. Kcat of TypSP increased from 22.5/s to 25.6/s with improved operational and storage stabilities. The half-life (t1/2) of TrySP showed 6 folds increase. Furthermore, TrySP activation energy increased from 45,918 J/mol to 94,491 J/mol. The sustainable model presented in this study enables the development of a thermostable, encapsulated trypsin nano-powder with physical and chemical properties that are optimized for various biotechnological industrial applications.Keywords: Büchi B-90 spray dryingdesign of experimentsimmobilizationtrypsin enzyme formulationkinetic parametersnano powder Authors’ contributionsHM established, designed, and carried out some of the experiments, assisted with data analysis, and wrote the majority of the manuscript. SA and NZ co-developed the concept, designed some of the experiments, assisted with the analysis of data, and revised the written material. MT set up, carried out, and analyzed the factorial design, as well as writing the appropriate manuscript parts. DN, RM, and NA, carried out the experimental part and reviewed the written. The final manuscript was read and approved by all authors.Disclosure statementNo potential conflict of interest was reported by the author(s).Data availability statementThe datasets generated during and/or analyzed during the present study are provided by corresponding author upon request.Additional informationFundingOpen access funding is provided by Science, Technology and Innovation Funding Authority (STDF) in cooperation with The Egyptian Knowledge Bank (EKB). The authors did not receive any external funding from any organization for the submitted work.","PeriodicalId":8824,"journal":{"name":"Biocatalysis and Biotransformation","volume":"147 1","pages":"0"},"PeriodicalIF":0.0,"publicationDate":"2023-11-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"135371388","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 : 2023-10-12DOI: 10.1080/10242422.2023.2267156
Oluwayinka O. Oke, Yawen Chen, Chukwuemeka Isanbor, Olayinka T. Asekun, David O’Hagan
An efficient conversion of ortho, meta and para fluoro- and trifluoromethyl-substituted benzoic acids to the corresponding benzamides in fermentations of the soil bacterium Streptomyces sp. JCM9888 is described. We also report the efficient reduction of the same class of substrates to the corresponding benzyl alcohols with the fungi Cunninghamella elegans. These biotransformations were surprisingly efficient and may have value as disruptive technologies in process chemistry.
{"title":"Efficient biotransformations in <i>Cunninghamella elegans</i> and <i>Streptomyces sp.</i> JCM9888 of selectively fluorinated benzoic acids to the corresponding benzamides and benzyl alcohols","authors":"Oluwayinka O. Oke, Yawen Chen, Chukwuemeka Isanbor, Olayinka T. Asekun, David O’Hagan","doi":"10.1080/10242422.2023.2267156","DOIUrl":"https://doi.org/10.1080/10242422.2023.2267156","url":null,"abstract":"An efficient conversion of ortho, meta and para fluoro- and trifluoromethyl-substituted benzoic acids to the corresponding benzamides in fermentations of the soil bacterium Streptomyces sp. JCM9888 is described. We also report the efficient reduction of the same class of substrates to the corresponding benzyl alcohols with the fungi Cunninghamella elegans. These biotransformations were surprisingly efficient and may have value as disruptive technologies in process chemistry.","PeriodicalId":8824,"journal":{"name":"Biocatalysis and Biotransformation","volume":"19 1","pages":"0"},"PeriodicalIF":0.0,"publicationDate":"2023-10-12","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"135968999","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 : 2023-10-05DOI: 10.1080/10242422.2023.2265019
Glauco Silva Dias, David Alexander Mitchell, Fernando Wypych, Nadia Krieger
AbstractLayered double hydroxides (LDHs) are brucite-like nanomaterials that have been used to immobilize several enzymes. However, layered hydroxide salts (LHSs), another group of brucite-like nanomaterials, have not yet been used for enzyme immobilization. In this work, we prepared two types of layered hydroxide salts, zinc hydroxide nitrate (ZHN: Zn5(OH)8(NO3)2.2H2O) and zinc hydroxide chloride (ZHC: Zn5(OH)8Cl2.H2O) and used them to immobilize Pseudomonas cepacia lipase (LipPS). The best protein loading for both ZHN and ZHC was 162.5 mg g−1 of LHS, which gave high values of triolein-hydrolyzing activity in organic medium (103 U g−1 for LipPS-ZHN and 105 U g−1 for LipPS-ZHC), immobilization efficiencies above 90% and activity retentions above 170%. In the kinetic resolution of (R,S)-1-phenylethanol, LipPS-ZHN gave better results, with 50% conversion being obtained in 2 h and an ees of 99%. With LipPS-ZHC, the conversion at 2 h was 40% and the ees, was lower, only 73%. For both immobilized materials, the eep was higher than 99% and E was higher than 200. The immobilized materials were stable after 5 cycles of reuse in successive 2-h kinetic resolutions. These results demonstrate that the layered hydroxide salts ZHN and ZHC have good potential as supports for the immobilization of lipases.Keywords: Pseudomonas cepacia lipaseimmobilizationlayered hydroxide saltsenzymatic kinetic resolution Authors’ contributionsAll authors contributed to the conception and design of the study. Material preparation, data collection and analysis were performed by Glauco Silva Dias. Nadia Krieger and Fernando Wypych directly supervised the work. The first draft of the manuscript was written by Glauco Silva Dias and all authors commented on this first draft and subsequent versions of the manuscript. All authors read and approved the final manuscript.Disclosure statementThe authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper. Although funding was received from various research funding agencies (listed in the acknowledgements section), none of the funding agencies were involved in the design, execution or reporting of the work.Additional informationFundingThis study was financed (Finance Code 001) by CAPES (Coordenação de Aperfeiçoamento de Pessoal de Nível Superior), a Brazilian government agency for the development of personnel in higher education and by a project financed by the Brazilian-Argentine Biotechnology Center (CBAB/CABBIO) and administered by CNPq (Conselho Nacional de Desenvolvimento Científico e Tecnológico), a Brazilian government agency for the advancement of science and technology (Project 441015/2016-6). Research scholarships were granted to Glauco Silva Dias by CAPES and to David Alexander Mitchell, Fernando Wypych and Nadia Krieger by CNPq. These funding agencies were not involved in the design, execution or reporting of the work.
层状双氢氧化物(LDHs)是一种类似水镁石的纳米材料，已被用于固定化多种酶。然而，层状氢氧化物盐(lhs)，另一组类似水镁石的纳米材料，尚未用于酶固定化。本文制备了两种层状氢氧化锌盐:硝酸氢氧化锌(ZHN: Zn5(OH)8(NO3)2.2H2O)和氯化锌(ZHC: Zn5(OH)8Cl2.H2O)，并将其用于固定化洋葱假单胞菌脂肪酶(LipPS)。zn和ZHC的最佳蛋白负荷均为162.5 mg g−1，在有机培养基中具有较高的三聚烯烃水解活性(LipPS-ZHN为103 U g−1,LipPS-ZHC为105 U g−1)，固定化效率在90%以上，活性保留率在170%以上。在(R,S)-1-苯乙醇的动力学拆分方面，LipPS-ZHN具有较好的效果，2 h内转化率达到50%，转化率达到99%。LipPS-ZHC在2 h的转化率为40%，ees较低，仅为73%。两种固定化材料的eep均大于99%，E均大于200。在连续的2 h动力学分辨率下，固定材料在重复使用5次后是稳定的。这些结果表明，层状氢氧化盐ZHN和ZHC作为固定化脂肪酶的载体具有良好的潜力。关键词:洋葱假单胞菌脂酶固定化层状氢氧盐酶动力学分解作者对本研究的构思和设计均有贡献。材料准备、数据收集和分析由Glauco Silva Dias完成。Nadia Krieger和Fernando Wypych直接监督这项工作。手稿的初稿是由Glauco Silva Dias撰写的，所有作者都对手稿的初稿和后续版本进行了评论。所有作者都阅读并批准了最终的手稿。披露声明作者声明，他们没有已知的竞争经济利益或个人关系，可能会影响本文所报道的工作。虽然资金来自不同的研究资助机构(列在致谢部分)，但没有一个资助机构参与研究的设计、执行或报告。本研究由巴西政府高等教育人才发展机构CAPES (codena ode aperfeiamento de Pessoal de Nível Superior)和巴西-阿根廷生物技术中心(CBAB/CABBIO)资助、CNPq (Conselho Nacional de Desenvolvimento Científico e Tecnológico)管理的一个项目资助(财务代码001)。巴西政府科技促进机构(项目441015/2016-6)。研究奖学金由CAPES授予Glauco Silva Dias，由CNPq授予David Alexander Mitchell, Fernando Wypych和Nadia Krieger。这些资助机构没有参与工作的设计、执行或报告。
{"title":"Zinc hydroxide salts as new supports for the immobilization of <i>Pseudomonas cepacia</i> lipase","authors":"Glauco Silva Dias, David Alexander Mitchell, Fernando Wypych, Nadia Krieger","doi":"10.1080/10242422.2023.2265019","DOIUrl":"https://doi.org/10.1080/10242422.2023.2265019","url":null,"abstract":"AbstractLayered double hydroxides (LDHs) are brucite-like nanomaterials that have been used to immobilize several enzymes. However, layered hydroxide salts (LHSs), another group of brucite-like nanomaterials, have not yet been used for enzyme immobilization. In this work, we prepared two types of layered hydroxide salts, zinc hydroxide nitrate (ZHN: Zn5(OH)8(NO3)2.2H2O) and zinc hydroxide chloride (ZHC: Zn5(OH)8Cl2.H2O) and used them to immobilize Pseudomonas cepacia lipase (LipPS). The best protein loading for both ZHN and ZHC was 162.5 mg g−1 of LHS, which gave high values of triolein-hydrolyzing activity in organic medium (103 U g−1 for LipPS-ZHN and 105 U g−1 for LipPS-ZHC), immobilization efficiencies above 90% and activity retentions above 170%. In the kinetic resolution of (R,S)-1-phenylethanol, LipPS-ZHN gave better results, with 50% conversion being obtained in 2 h and an ees of 99%. With LipPS-ZHC, the conversion at 2 h was 40% and the ees, was lower, only 73%. For both immobilized materials, the eep was higher than 99% and E was higher than 200. The immobilized materials were stable after 5 cycles of reuse in successive 2-h kinetic resolutions. These results demonstrate that the layered hydroxide salts ZHN and ZHC have good potential as supports for the immobilization of lipases.Keywords: Pseudomonas cepacia lipaseimmobilizationlayered hydroxide saltsenzymatic kinetic resolution Authors’ contributionsAll authors contributed to the conception and design of the study. Material preparation, data collection and analysis were performed by Glauco Silva Dias. Nadia Krieger and Fernando Wypych directly supervised the work. The first draft of the manuscript was written by Glauco Silva Dias and all authors commented on this first draft and subsequent versions of the manuscript. All authors read and approved the final manuscript.Disclosure statementThe authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper. Although funding was received from various research funding agencies (listed in the acknowledgements section), none of the funding agencies were involved in the design, execution or reporting of the work.Additional informationFundingThis study was financed (Finance Code 001) by CAPES (Coordenação de Aperfeiçoamento de Pessoal de Nível Superior), a Brazilian government agency for the development of personnel in higher education and by a project financed by the Brazilian-Argentine Biotechnology Center (CBAB/CABBIO) and administered by CNPq (Conselho Nacional de Desenvolvimento Científico e Tecnológico), a Brazilian government agency for the advancement of science and technology (Project 441015/2016-6). Research scholarships were granted to Glauco Silva Dias by CAPES and to David Alexander Mitchell, Fernando Wypych and Nadia Krieger by CNPq. These funding agencies were not involved in the design, execution or reporting of the work.","PeriodicalId":8824,"journal":{"name":"Biocatalysis and Biotransformation","volume":"11 1","pages":"0"},"PeriodicalIF":0.0,"publicationDate":"2023-10-05","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"135482056","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}
京公网安备 11010802042870号
京ICP备2023020795号-1
扫码关注我们
求助内容：
应助结果提醒方式：