Biocatalysis and Biotransformation最新文献

{"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}

{"title":"Bioprospecting fruit waste to purify invertase for low calorie food products","authors":"Kavita Rana, Neerja Rana, Sunita Devi, Nilakshi Chauhan","doi":"10.1080/10242422.2023.2296347","DOIUrl":"https://doi.org/10.1080/10242422.2023.2296347","url":null,"abstract":"","PeriodicalId":8824,"journal":{"name":"Biocatalysis and Biotransformation","volume":" 28","pages":""},"PeriodicalIF":1.8,"publicationDate":"2024-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"139393168","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}

{"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}

{"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}

{"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}

{"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}

{"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}

{"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}

{"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}

{"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}