Pub Date : 2022-11-11DOI: 10.1080/10242422.2022.2144263
Isamayra Germano de Sousa, Anderson Valério Chaves, A. L. B. de Oliveira, Katerine da Silva Moreira, Paulo Gonçalves De Sousa Junior, Francisco Simão Neto, Simone Cristina Freitas de Carvalho, Roberta Bussons Rodrigues Valério, Gledson Vieira Lima, Ada Amélia Sanders Lopes, Maria Cristiane Martins de Souza, Aluísio Marques da Fonseca, P. Fechine, M. D. de Mattos, J. C. D. dos Santos
{"title":"A novel hybrid biocatalyst from immobilized Eversa® Transform 2.0 lipase and its application in biolubricant synthesis","authors":"Isamayra Germano de Sousa, Anderson Valério Chaves, A. L. B. de Oliveira, Katerine da Silva Moreira, Paulo Gonçalves De Sousa Junior, Francisco Simão Neto, Simone Cristina Freitas de Carvalho, Roberta Bussons Rodrigues Valério, Gledson Vieira Lima, Ada Amélia Sanders Lopes, Maria Cristiane Martins de Souza, Aluísio Marques da Fonseca, P. Fechine, M. D. de Mattos, J. C. D. dos Santos","doi":"10.1080/10242422.2022.2144263","DOIUrl":"https://doi.org/10.1080/10242422.2022.2144263","url":null,"abstract":"","PeriodicalId":8824,"journal":{"name":"Biocatalysis and Biotransformation","volume":" ","pages":""},"PeriodicalIF":1.8,"publicationDate":"2022-11-11","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"48745848","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 : 2022-11-08DOI: 10.1080/10242422.2022.2140588
Mudzuli Maphupha, Adela Vidov, C. D. de Koning, D. Brady
{"title":"Laccase-catalysed azide-alkyne cycloadditions: Synthesis of benzothiazole and benzimidazole fused 1,2,3-triazole derivatives by copper containing oxidoreductase enzymes","authors":"Mudzuli Maphupha, Adela Vidov, C. D. de Koning, D. Brady","doi":"10.1080/10242422.2022.2140588","DOIUrl":"https://doi.org/10.1080/10242422.2022.2140588","url":null,"abstract":"","PeriodicalId":8824,"journal":{"name":"Biocatalysis and Biotransformation","volume":" ","pages":""},"PeriodicalIF":1.8,"publicationDate":"2022-11-08","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"43709884","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 : 2022-11-02DOI: 10.1080/10242422.2022.2138360
D. Yanto, S. Anita, N. N. Solihat
{"title":"Enzymatic degradation and metabolic pathway of acid blue 129 dye by crude laccase from newly isolated Trametes hirsuta EDN 082","authors":"D. Yanto, S. Anita, N. N. Solihat","doi":"10.1080/10242422.2022.2138360","DOIUrl":"https://doi.org/10.1080/10242422.2022.2138360","url":null,"abstract":"","PeriodicalId":8824,"journal":{"name":"Biocatalysis and Biotransformation","volume":" ","pages":""},"PeriodicalIF":1.8,"publicationDate":"2022-11-02","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"44737193","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 : 2022-10-31DOI: 10.1080/10242422.2022.2138359
R. S. Manhas, Diksha Koul, Parveen Kumar, Ajay Kumar, Asha Bhagat, Sreedhar Madishetti, P. Sangwan, Zabeer Ahmed, A. Chaubey
{"title":"Talaromyces purpurogenus MRS-F13 catalyzed biotransformation of (-)-verbenone to (-)-10-hydroxyverbenone and their anti-inflammatory activity profile","authors":"R. S. Manhas, Diksha Koul, Parveen Kumar, Ajay Kumar, Asha Bhagat, Sreedhar Madishetti, P. Sangwan, Zabeer Ahmed, A. Chaubey","doi":"10.1080/10242422.2022.2138359","DOIUrl":"https://doi.org/10.1080/10242422.2022.2138359","url":null,"abstract":"","PeriodicalId":8824,"journal":{"name":"Biocatalysis and Biotransformation","volume":" ","pages":""},"PeriodicalIF":1.8,"publicationDate":"2022-10-31","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"44170899","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 : 2022-10-21DOI: 10.1080/10242422.2022.2124111
Ahmet Melih Öten, Evren Atak, Banu Taktak Karaca, S. Fırtına, Aslı Kutlu
Abstract Lipases and cellulases have been extensively used in the field of biotechnology for varied purposes. Mainly, the ongoing researches focus on the improvements of kinetic and enzymatic characteristics of enzymes to meet industrial needs. With the discovery of psychrophilic cellulase and lipase sources, a new era has opened for protein research by allowing the discovery of novel functions together with the description of unique cold adaptation mechanisms to harsh environments. The ability of cold-adapted lipase and cellulases to enable chemical reactions at lower temperatures provides a great opportunity to cut the cost of the finished product by lowering energy and purifying expanses. The advances in the cold-adapted lipase and cellulase enzymes are the cumulative efforts of organic chemists, biophysicists, biotechnologists, and process engineers who greatly contribute to a better understanding of cold-adaptation phenomena from different points of view. In this review, we cover the cold-adaptation aspects of cellulase and lipase enzymes from structural points of view by referring to the roles of Gly and Pro residues. Gly and Pro residues accelerate the cold-adaptation of enzymes by altering the conformational changes in the 3 D structure of proteins The list of microorganisms as a source of cold-adapted cellulases and lipases is given by referring to biotechnological applications. After introducing the thermodynamic background of Gly and Pro residues in the phenomena of cold-adaptation, specific examples are given to emphasise how introducing Gly and Pro into 3 D structure of protein molecules adds value in terms of biotechnological application by contributing to cold-adaptation.
{"title":"Discussing the roles of proline and glycine from the perspective of cold adaptation in lipases and cellulases","authors":"Ahmet Melih Öten, Evren Atak, Banu Taktak Karaca, S. Fırtına, Aslı Kutlu","doi":"10.1080/10242422.2022.2124111","DOIUrl":"https://doi.org/10.1080/10242422.2022.2124111","url":null,"abstract":"Abstract Lipases and cellulases have been extensively used in the field of biotechnology for varied purposes. Mainly, the ongoing researches focus on the improvements of kinetic and enzymatic characteristics of enzymes to meet industrial needs. With the discovery of psychrophilic cellulase and lipase sources, a new era has opened for protein research by allowing the discovery of novel functions together with the description of unique cold adaptation mechanisms to harsh environments. The ability of cold-adapted lipase and cellulases to enable chemical reactions at lower temperatures provides a great opportunity to cut the cost of the finished product by lowering energy and purifying expanses. The advances in the cold-adapted lipase and cellulase enzymes are the cumulative efforts of organic chemists, biophysicists, biotechnologists, and process engineers who greatly contribute to a better understanding of cold-adaptation phenomena from different points of view. In this review, we cover the cold-adaptation aspects of cellulase and lipase enzymes from structural points of view by referring to the roles of Gly and Pro residues. Gly and Pro residues accelerate the cold-adaptation of enzymes by altering the conformational changes in the 3 D structure of proteins The list of microorganisms as a source of cold-adapted cellulases and lipases is given by referring to biotechnological applications. After introducing the thermodynamic background of Gly and Pro residues in the phenomena of cold-adaptation, specific examples are given to emphasise how introducing Gly and Pro into 3 D structure of protein molecules adds value in terms of biotechnological application by contributing to cold-adaptation.","PeriodicalId":8824,"journal":{"name":"Biocatalysis and Biotransformation","volume":"41 1","pages":"243 - 260"},"PeriodicalIF":1.8,"publicationDate":"2022-10-21","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"49133235","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 : 2022-10-19DOI: 10.1080/10242422.2022.2136523
C. Ong, D. Ibrahim, Mohd Jain Noordin Mohd Kassim
{"title":"The Tannase from red yeast Rhodotorula glutinis: purification and characterization","authors":"C. Ong, D. Ibrahim, Mohd Jain Noordin Mohd Kassim","doi":"10.1080/10242422.2022.2136523","DOIUrl":"https://doi.org/10.1080/10242422.2022.2136523","url":null,"abstract":"","PeriodicalId":8824,"journal":{"name":"Biocatalysis and Biotransformation","volume":" ","pages":""},"PeriodicalIF":1.8,"publicationDate":"2022-10-19","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"42227402","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 : 2022-09-12DOI: 10.1080/10242422.2022.2116277
Xuejun Liu, Yi Jiang, Hongling Liu, Haibo Yuan, Di Huang, Tengfei Wang
Abstract Plant biomass is a kind of renewable, abundant, eco-friendly, and clean natural resource. Recent increase in industrial demand, coupled with development and utilization of biocatalysts for utilization and production of high value-added products from plant biomass have attracted numerous research interest. The ester bond, between plant cell wall polysaccharides and ferulic acid (FA), can be hydrolysed by feruloyl esterases (FAE), thereby destroying compactness of lignocellulosic materials, which is beneficial during utilization of biomass resources. This is this research focus. In this article, we reviewed classification, characteristics, and application of FAE from different species, then highlighted the synergistic effect of FAE action with other enzymes. The findings are considered to provide insights into role of FAE in functional research, biochemical properties, and industrial application, especially with focus on processing of lignocellulosic biomass, harnessing hydroxycinnamate from agricultural by-products, and production of biofuels among other industrial uses.
{"title":"Research progress and biotechnological applications of feruloyl esterases","authors":"Xuejun Liu, Yi Jiang, Hongling Liu, Haibo Yuan, Di Huang, Tengfei Wang","doi":"10.1080/10242422.2022.2116277","DOIUrl":"https://doi.org/10.1080/10242422.2022.2116277","url":null,"abstract":"Abstract Plant biomass is a kind of renewable, abundant, eco-friendly, and clean natural resource. Recent increase in industrial demand, coupled with development and utilization of biocatalysts for utilization and production of high value-added products from plant biomass have attracted numerous research interest. The ester bond, between plant cell wall polysaccharides and ferulic acid (FA), can be hydrolysed by feruloyl esterases (FAE), thereby destroying compactness of lignocellulosic materials, which is beneficial during utilization of biomass resources. This is this research focus. In this article, we reviewed classification, characteristics, and application of FAE from different species, then highlighted the synergistic effect of FAE action with other enzymes. The findings are considered to provide insights into role of FAE in functional research, biochemical properties, and industrial application, especially with focus on processing of lignocellulosic biomass, harnessing hydroxycinnamate from agricultural by-products, and production of biofuels among other industrial uses.","PeriodicalId":8824,"journal":{"name":"Biocatalysis and Biotransformation","volume":"41 1","pages":"421 - 439"},"PeriodicalIF":1.8,"publicationDate":"2022-09-12","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"44031816","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 : 2022-09-08DOI: 10.1080/10242422.2022.2120391
A. Ünlü, B. Prasad, Kishan Anavekar, P. Bubenheim, A. Liese
Abstract Natural deep eutectic solvents (NADESs) were investigated for the activity and stability of the laccase enzyme. Laccase was found to be active only in a low amount of choline chloride containing NADESs while it maintained its activity both in high and low amounts of betaine containing NADESs. Rutin, as a flavonoid monomer shows high antioxidant, antibacterial, antiviral and anti-inflammatory properties and these properties are enhanced in the polymerised form. In this study, the organic co-solvent that is conventionally used in the oligomerization of rutin was replaced with two different green solvents, choline chloride-ethylene glycol (1:2 molar ratio) and betaine-mannose (5:2 molar ratio). LC-MS results revealed spontaneous derivatization of rutin as well as the oligomerization of the derivatives besides rutin. The final products were found to have enhanced superoxide radical activity. In this study, enzymatic oligomerization of rutin was investigated for the first time in the presence of eco-friendly green solvents presenting an alternative pathway without any toxic components.
{"title":"The effect of natural deep eutectic solvents on laccase activity and oligomerization of rutin","authors":"A. Ünlü, B. Prasad, Kishan Anavekar, P. Bubenheim, A. Liese","doi":"10.1080/10242422.2022.2120391","DOIUrl":"https://doi.org/10.1080/10242422.2022.2120391","url":null,"abstract":"Abstract Natural deep eutectic solvents (NADESs) were investigated for the activity and stability of the laccase enzyme. Laccase was found to be active only in a low amount of choline chloride containing NADESs while it maintained its activity both in high and low amounts of betaine containing NADESs. Rutin, as a flavonoid monomer shows high antioxidant, antibacterial, antiviral and anti-inflammatory properties and these properties are enhanced in the polymerised form. In this study, the organic co-solvent that is conventionally used in the oligomerization of rutin was replaced with two different green solvents, choline chloride-ethylene glycol (1:2 molar ratio) and betaine-mannose (5:2 molar ratio). LC-MS results revealed spontaneous derivatization of rutin as well as the oligomerization of the derivatives besides rutin. The final products were found to have enhanced superoxide radical activity. In this study, enzymatic oligomerization of rutin was investigated for the first time in the presence of eco-friendly green solvents presenting an alternative pathway without any toxic components.","PeriodicalId":8824,"journal":{"name":"Biocatalysis and Biotransformation","volume":"41 1","pages":"353 - 366"},"PeriodicalIF":1.8,"publicationDate":"2022-09-08","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"47322910","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 : 2022-08-29DOI: 10.1080/10242422.2022.2113519
G. de Gonzalo, Nikola Lončar, M. Fraaije
{"title":"Sulphoxidation reactions catalysed by the Baeyer-Villiger monooxygenase OTEMO from Pseudomonas putida ATCC 17453","authors":"G. de Gonzalo, Nikola Lončar, M. Fraaije","doi":"10.1080/10242422.2022.2113519","DOIUrl":"https://doi.org/10.1080/10242422.2022.2113519","url":null,"abstract":"","PeriodicalId":8824,"journal":{"name":"Biocatalysis and Biotransformation","volume":" ","pages":""},"PeriodicalIF":1.8,"publicationDate":"2022-08-29","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"43897373","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}
Abstract Rapamycin is a macrolide antibiotic with antifungal, immunosuppressive, antitumor, and lifespan-extension activities etc. In order to increase its structural diversity, microbial transformation of rapamycin was conducted. More than 3 converted compounds were shown in the microbial conversion culture of rapamycin by Bacillus subtilis CGMCC7764. By extensive NMR and MS spectroscopic analyses, the major compound was identified as 43-O-(β-D-glucoside)-rapamycin. This compound has an inhibitory effect on tumour growth, and its activity is similar to rapamycin.
{"title":"43-O-(β-D-glucoside)-rapamycin, a microbial conversion product by Bacillus subtilis CGMCC7764","authors":"Xiaoming Chen, Guohua Yang, Xiaqin Chen, Dong-Wei Jin, Hui Yu, Yuan-rong Cheng, Jie Huang","doi":"10.1080/10242422.2022.2108707","DOIUrl":"https://doi.org/10.1080/10242422.2022.2108707","url":null,"abstract":"Abstract Rapamycin is a macrolide antibiotic with antifungal, immunosuppressive, antitumor, and lifespan-extension activities etc. In order to increase its structural diversity, microbial transformation of rapamycin was conducted. More than 3 converted compounds were shown in the microbial conversion culture of rapamycin by Bacillus subtilis CGMCC7764. By extensive NMR and MS spectroscopic analyses, the major compound was identified as 43-O-(β-D-glucoside)-rapamycin. This compound has an inhibitory effect on tumour growth, and its activity is similar to rapamycin.","PeriodicalId":8824,"journal":{"name":"Biocatalysis and Biotransformation","volume":"41 1","pages":"374 - 379"},"PeriodicalIF":1.8,"publicationDate":"2022-08-25","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"41762236","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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