{"title":"Immobilization of fungal α-galactosidase on magnetic nanoparticles and hydrolysis of raffinose family oligosaccharides (RFO) in soymilk","authors":"Purvi Bangoria, S. Chaki, A. Shah","doi":"10.1080/10242422.2023.2247516","DOIUrl":"https://doi.org/10.1080/10242422.2023.2247516","url":null,"abstract":"","PeriodicalId":8824,"journal":{"name":"Biocatalysis and Biotransformation","volume":" ","pages":""},"PeriodicalIF":1.8,"publicationDate":"2023-08-24","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"47094572","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}
D. Maany, M. Wahba, Mohamed I. Abo-Alkasem, M. El-Abd, A. Ibrahim
{"title":"Hexavalent chromium detoxification by haloalkaliphilic Nesterenkonia sp strain NRC-Y immobilized in different matrices","authors":"D. Maany, M. Wahba, Mohamed I. Abo-Alkasem, M. El-Abd, A. Ibrahim","doi":"10.1080/10242422.2023.2248336","DOIUrl":"https://doi.org/10.1080/10242422.2023.2248336","url":null,"abstract":"","PeriodicalId":8824,"journal":{"name":"Biocatalysis and Biotransformation","volume":" ","pages":""},"PeriodicalIF":1.8,"publicationDate":"2023-08-23","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"47940561","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}
Latafat, Mohammed Haris Siddiqui, Ashish, Archana Vimal, Prachi Bhargava
{"title":"Isolation and screening of keratinolytic bacteria from feather dumping soil near in Lucknow and Kanpur city, North region of Indian","authors":"Latafat, Mohammed Haris Siddiqui, Ashish, Archana Vimal, Prachi Bhargava","doi":"10.1080/10242422.2023.2235053","DOIUrl":"https://doi.org/10.1080/10242422.2023.2235053","url":null,"abstract":"<p><b>Abstract</b></p><h3>Background </h3><p>Keratinases are proteolytic enzymes that have the capability of degrading insoluble keratin substrates. LS4, LS5, and KS3 were newly isolated strains showing ability to hydrolyze keratins and keratin based products.</p><h3>Objective </h3><p>In this study, different bacterial strains were isolated from soil, screened for protease and keratinase production, and the best isolates were identified.</p><h3>Methods </h3><p>Serial dilution and plating method were used for isolation of pure bacterial culture. Isolated, 48 strains were screened, and their feather degrading ability on feather meal agar plates and keratin azure-based agar. The proteolytic activity of the isolates was also screened on casein agar.</p><h3>Results </h3><p>Three strains; LS4, LS5, and KS3 shows keratinolytic activity that reveal the keratinase enzyme on medium; feather meal agar, keratin azure agar, and casein agar. Among all the three strains (LS4, LS5, and KS3), KS3 show largest inhibition zone that show maximum enzymatic activity. For its characterization 16S RNA was performed, sequence KS3 was submitted to GenBank and was identified as <i>Bacillus tropicus</i> KS3. Newly isolated strain <i>B. tropicus</i> KS3 showed the keratinase production and highest keratinase activity (35.06 ± 2.5 U/ml). <i>B. tropicus</i> KS3 also show the highest degradation of feather efficiently showed 84% of whole chicken feather biodegradation at 37 °C within 15 days among all the isolated strains.</p><h3>Conclusion </h3><p>Keratinase enzyme possesses a wide range of potential applications in the bioremediation of feather waste and bio-fertilizer in agricultural land. The industry demands a better source of this enzyme due to its multivariate application and huge market demand. In the present study, a novel keratinase-producing bacteria was isolated and characterized as <i>Bacillus tropicus</i> KS3 from poultry waste contamination soil.</p>","PeriodicalId":8824,"journal":{"name":"Biocatalysis and Biotransformation","volume":"2015 8","pages":""},"PeriodicalIF":1.8,"publicationDate":"2023-08-02","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"138518487","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}
Y. Yuzugullu Karakus, Gulen Sinem Inci, Elif Kale Bakir, Bektore Mansurov
{"title":"Thermostable alkaline protease from Scytalidium thermophilum: production, purification, and biochemical characterization","authors":"Y. Yuzugullu Karakus, Gulen Sinem Inci, Elif Kale Bakir, Bektore Mansurov","doi":"10.1080/10242422.2023.2236760","DOIUrl":"https://doi.org/10.1080/10242422.2023.2236760","url":null,"abstract":"Abstract An extracellular alkaline protease from Scytalidium thermophilum was produced in a glucose-containing medium supplemented with 5 mM NaCl for 3 days at pH 8.0 and 45 °C. The enzyme was 10-fold purified using ammonium sulfate precipitation followed by ion-exchange chromatography, and its molecular weight was calculated as 80 kDa from SDS-PAGE. The enzyme exhibited optimum activity at pH 8.0 and 60 °C. It was stable at pH and temperature range of 6.0–10.0 and 30–80 °C, respectively. Its half time was 30 h at pH 6.0, 7.0 and 8.0, while those were 22, 16, 8, and 3 h at 50 °C, 60 °C, 70 °C, and 80 °C, respectively. Kinetic parameters including Km (2 ± 0.02 mg/ml), Vmax (18.7 ± 1.5 µmole tyrosine ml−1 min−1), and kcat (2.5 x 103 min−1) were determined using casein. Ca2+ increased the enzyme activity, but it was slightly reduced by EDTA, Triton X-100, Tween 20, and Tween 80. It was active against reducing agents like β-mercaptoethanol but completely inhibited by phenyl methyl sulphonyl fluoride supporting the enzyme belonging to the serine protease family. Chloroform (143%), methanol (138%), and isopropanol (111%) increased the enzyme activity at 5% (v/v), while ethanol (71%) and acetone (81%) moderately reduced the proteolytic activity at the same concentration. Dimethyl sulfoxide (5%, v/v) did not significantly affect the enzyme. The enzyme was compatible with several detergents (1%, w/v), maintaining more than 90% of its original activity in almost all detergents tested. The stability of the enzyme presented against pH, temperature, organic solvents, and detergents indicates its potential use in various industrial applications, especially in peptide synthesis and the laundry industry.","PeriodicalId":8824,"journal":{"name":"Biocatalysis and Biotransformation","volume":"41 1","pages":"380 - 394"},"PeriodicalIF":1.8,"publicationDate":"2023-07-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"46661763","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 review on preparation and applications of glycerol carbonate: Focus biocatalysis","authors":"S. Karmee","doi":"10.1080/10242422.2023.2232914","DOIUrl":"https://doi.org/10.1080/10242422.2023.2232914","url":null,"abstract":"","PeriodicalId":8824,"journal":{"name":"Biocatalysis and Biotransformation","volume":" ","pages":""},"PeriodicalIF":1.8,"publicationDate":"2023-07-06","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"43245921","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}
M. Baltaci, M. A. Omeroglu, H. Ozkan, Mesut Taskin, A. Adiguzel
{"title":"Enhanced biodegradation of crude oil contamination by indigenous bacterial consortium under real conditions","authors":"M. Baltaci, M. A. Omeroglu, H. Ozkan, Mesut Taskin, A. Adiguzel","doi":"10.1080/10242422.2023.2231592","DOIUrl":"https://doi.org/10.1080/10242422.2023.2231592","url":null,"abstract":"","PeriodicalId":8824,"journal":{"name":"Biocatalysis and Biotransformation","volume":" ","pages":""},"PeriodicalIF":1.8,"publicationDate":"2023-07-06","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"47758433","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":"Improving hydrogen peroxide stability of a dye-decolorising peroxidase from Irpex lacteus F17 by site-directed mutagenesis","authors":"Wen-Yi Huang, Jingjing He, Liuqing Li, Rong Jia","doi":"10.1080/10242422.2023.2231122","DOIUrl":"https://doi.org/10.1080/10242422.2023.2231122","url":null,"abstract":"","PeriodicalId":8824,"journal":{"name":"Biocatalysis and Biotransformation","volume":" ","pages":""},"PeriodicalIF":1.8,"publicationDate":"2023-07-04","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"43187327","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":"Tyrosinase from the peels of Musa cavendish: purification, characterization, immobilization and application in phenol biodegradation","authors":"M. Adeyanju, A. Ademakinwa","doi":"10.1080/10242422.2023.2222206","DOIUrl":"https://doi.org/10.1080/10242422.2023.2222206","url":null,"abstract":"","PeriodicalId":8824,"journal":{"name":"Biocatalysis and Biotransformation","volume":" ","pages":""},"PeriodicalIF":1.8,"publicationDate":"2023-06-14","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"44654707","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":"Chitinase: a potent biocatalyst and its diverse applications","authors":"Gaytri Mahajan, Vibhuti Sharma, Reena Gupta","doi":"10.1080/10242422.2023.2218524","DOIUrl":"https://doi.org/10.1080/10242422.2023.2218524","url":null,"abstract":"","PeriodicalId":8824,"journal":{"name":"Biocatalysis and Biotransformation","volume":" ","pages":""},"PeriodicalIF":1.8,"publicationDate":"2023-06-02","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"48379316","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}