Biocatalysis and Biotransformation最新文献

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Immobilization of fungal α-galactosidase on magnetic nanoparticles and hydrolysis of raffinose family oligosaccharides (RFO) in soymilk 磁性纳米颗粒固定化真菌α-半乳糖苷酶及豆浆中棉子糖家族寡糖(RFO)的水解研究
IF 1.8 4区 生物学
Biocatalysis and Biotransformation Pub Date : 2023-08-24 DOI: 10.1080/10242422.2023.2247516
Purvi Bangoria, S. Chaki, A. Shah
{"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}
引用次数: 0
Hexavalent chromium detoxification by haloalkaliphilic Nesterenkonia sp strain NRC-Y immobilized in different matrices 不同基质固定化嗜盐Nesterenkonia菌株NRC-Y对六价铬的解毒作用
IF 1.8 4区 生物学
Biocatalysis and Biotransformation Pub Date : 2023-08-23 DOI: 10.1080/10242422.2023.2248336
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}
引用次数: 0
Isolation and screening of keratinolytic bacteria from feather dumping soil near in Lucknow and Kanpur city, North region of Indian 印度北部勒克瑙和坎普尔市附近羽毛倾倒土壤中角化细菌的分离和筛选
IF 1.8 4区 生物学
Biocatalysis and Biotransformation Pub Date : 2023-08-02 DOI: 10.1080/10242422.2023.2235053
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}
引用次数: 0
Identification and characterization of a novel thermostable transaminase (TATP) from Thermorudis peleae peleae Thermorudis中一种新型热稳定转氨酶(TATP)的鉴定与表征
IF 1.8 4区 生物学
Biocatalysis and Biotransformation Pub Date : 2023-08-01 DOI: 10.1080/10242422.2023.2241601
Xiao Li, Ping Gui, Ruolin Yang, Zelin Lu, Xuefeng Wang, Chengkun Luo, Jingjie Jiang, Fuqiang Ma
{"title":"Identification and characterization of a novel thermostable transaminase (TATP) from Thermorudis peleae","authors":"Xiao Li, Ping Gui, Ruolin Yang, Zelin Lu, Xuefeng Wang, Chengkun Luo, Jingjie Jiang, Fuqiang Ma","doi":"10.1080/10242422.2023.2241601","DOIUrl":"https://doi.org/10.1080/10242422.2023.2241601","url":null,"abstract":"","PeriodicalId":8824,"journal":{"name":"Biocatalysis and Biotransformation","volume":" ","pages":""},"PeriodicalIF":1.8,"publicationDate":"2023-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"42750457","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}
引用次数: 0
Thermostable alkaline protease from Scytalidium thermophilum: production, purification, and biochemical characterization 嗜热镰刀菌耐热碱性蛋白酶:生产、纯化和生化表征
IF 1.8 4区 生物学
Biocatalysis and Biotransformation Pub Date : 2023-07-15 DOI: 10.1080/10242422.2023.2236760
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}
引用次数: 0
A review on preparation and applications of glycerol carbonate: Focus biocatalysis 碳酸甘油酯的制备及应用综述:聚焦生物催化
IF 1.8 4区 生物学
Biocatalysis and Biotransformation Pub Date : 2023-07-06 DOI: 10.1080/10242422.2023.2232914
S. Karmee
{"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}
引用次数: 0
Enhanced biodegradation of crude oil contamination by indigenous bacterial consortium under real conditions 真实条件下原生菌群对原油污染的强化生物降解
IF 1.8 4区 生物学
Biocatalysis and Biotransformation Pub Date : 2023-07-06 DOI: 10.1080/10242422.2023.2231592
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}
引用次数: 1
Improving hydrogen peroxide stability of a dye-decolorising peroxidase from Irpex lacteus F17 by site-directed mutagenesis 通过定点诱变提高Irpex lacteus F17染料脱色过氧化物酶的过氧化氢稳定性
IF 1.8 4区 生物学
Biocatalysis and Biotransformation Pub Date : 2023-07-04 DOI: 10.1080/10242422.2023.2231122
Wen-Yi Huang, Jingjing He, Liuqing Li, Rong Jia
{"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}
引用次数: 1
Tyrosinase from the peels of Musa cavendish: purification, characterization, immobilization and application in phenol biodegradation 麝香果皮酪氨酸酶的纯化、表征、固定化及其在苯酚生物降解中的应用
IF 1.8 4区 生物学
Biocatalysis and Biotransformation Pub Date : 2023-06-14 DOI: 10.1080/10242422.2023.2222206
M. Adeyanju, A. Ademakinwa
{"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}
引用次数: 0
Chitinase: a potent biocatalyst and its diverse applications 几丁质酶:一种有效的生物催化剂及其应用
IF 1.8 4区 生物学
Biocatalysis and Biotransformation Pub Date : 2023-06-02 DOI: 10.1080/10242422.2023.2218524
Gaytri Mahajan, Vibhuti Sharma, Reena Gupta
{"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}
引用次数: 1
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