Biocatalysis and Biotransformation最新文献

{"title":"Characterization and biodegradation of paracetamol by <i>Bacillus pumilus</i> strain PYP2","authors":"Sunil Chopra, Dharmender Kumar","doi":"10.1080/10242422.2023.2261592","DOIUrl":"https://doi.org/10.1080/10242422.2023.2261592","url":null,"abstract":"AbstractAs we know the recent pandemic, coronavirus disease (COVID-19) due to SARS CoV-2 virus has led to an increase in the consumption of various drugs as medicines by the patients. Paracetamol (acetaminophen, APAP) act as an emerging contaminant classified among the class pharmaceutical and personal care pollutant (PPCP) and is detected in wastewater and sewage systems. The enrichment culture approach was used for the isolation APAP-degrading bacterium wastewater sample. Microscopic examination, biochemical and 16S rRNA sequence analysis showed that the isolate PYP-2 belongs to the Bacillus pumilus strain. Shake flask and batch culture degradation studies have shown that the strain can degrade APAP. Further, the response surface methodology (RSM) plot was used to know the best physical condition for biodegradation by optimization study. The optimum pH of 5.0, temperature of 30 °C, agitation speed of 146 rpm, and APAP 267 mg/L concentration were reported for PYP-2-based degradation. Bacterial biomass kinetic analysis was performed at the best physical condition, and the results showed that the specific growth rate (µ) was 713 mg/L. Oxalic acid, 2-isopropyl-5-methyl cyclohexanone, and phenothiazine were the intermediates of the APAP degradation pathway detected by the GC-MS chromatogram peaks. Therefore, this research has shown that Bacillus pumilus strain PYP-2 has the metabolic capacity to biodegrade APAP, providing new tools for bioremediation.Keywords: ParacetamolBacillus pumilus strain PYP-2biodegradation16S rRNA sequence analysisshake flask studywastewater AcknowledgmentsThe authors are thankful to Department of Biotechnology, Deenbandhu Chhotu Ram University of Science and Technology Murthal Sonipat Haryana India, for providing necessary facilities to conduct this study. The authors also acknowledge the sample analysis for FTIR at Central Instrumentation Laboratory (CIL), DCRUST Murthal Sonipat India, DNA sequencing at Eurofins Genomics India Pvt Ltd, Advanced Instrumentation Research Facility (AIRF), JNU New Delhi, India for GC-MS analysis. S. Chopra, also wishes to thank UGC, New Delhi India, for providing a research assistantship in the form RGNF fellowship. Authors are thankful to Editor/Reviewers for suggestions that has improved the the manuscript.Disclosure statementNo potential conflict of interest was reported by the authors.Author contributionsAll authors contributed to the study conception and design. The material preparation, data collection and analysis were performed by SC and DK. The first draft of the manuscript was written by SC and all authors commented on previous versions of the manuscript. All authors read and approved the final manuscript. DK supervised this research.Ethics approvalNot applicable.Data availability statementThe 16S rRNA gene sequence data of the paracetamol degrading Bacillus pumilus strain PYP-2 was deposited to National Centre of Biotechnology Information (NCBI) GenBank with accession number MN74432","PeriodicalId":8824,"journal":{"name":"Biocatalysis and Biotransformation","volume":"115 1","pages":"0"},"PeriodicalIF":0.0,"publicationDate":"2023-10-02","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"135830904","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":"Recovery of antioxidative phenolic compounds by the valorization of rice biomass under the influence of lignocellulolytic enzymes","authors":"Kumar Shankar, R. V. Beladhadi, S. K. Jayalakshmi, Kuruba Sreeramulu","doi":"10.1080/10242422.2023.2257835","DOIUrl":"https://doi.org/10.1080/10242422.2023.2257835","url":null,"abstract":"AbstractThe present work aimed to optimize the recovery of antioxidative phenolic compounds from steam treated and untreated rice biomass (rice bran and rice straw) by the influence of lignocellulolytic enzymes of Burkholderia sp SMB1. The optimization of extraction was carried out by response surface methodology targeting to maximize phenolic release. These compounds were separated from the extracts using charcoal and un-utilized hydrolysed rice bran wastes and analysed for antioxidant properties. 10% (w/v) rice biomass with 60 mg of enzyme loadings (mg of protein in crude enzyme extract) at 40 °C, pH 7 for 30 min. Ferulic acid, gallic acid, coumaric acid, syringic acid, caffeic acid, epicatechin and kaemferol were identified by HPLC in both rice biomass extracts. Maximum total phenolics (83.35 mg GAE/100 g), total flavonoid content (16.89 mg/100 g QE), total tannin content (78.69 mg/100 g TAE) and antioxidant properties viz., 87.68% for ABTS, 77.11% for DPPH and 0.82 absorbance for FRAP was obtained for steam treated rice bran followed by rice straw. This work signifies the biomass transformation into phenolics possessing antioxidant nature under simple extraction process. It not only favours waste management process but also increases the income to agriculture sector.Keywords: Rice biomassBurkholderia sp SMB1lignocellulolytic enzymesphenolics extractionnatural antioxidants Disclosure statementNo potential conflict of interest was reported by the authors.Additional informationFundingThe authors are thankful to Department of Biotechnology (DBT), New Delhi and University Grants Commission (UGC SAP DRS-II), New Delhi, Government of India, for funding this work in the form of project. The author Kumar Shankar also acknowledge CSIR, New Delhi, India for funding in the form of CSIR-SRF direct (File No: 09/450(0046)/2020-EMR-I).","PeriodicalId":8824,"journal":{"name":"Biocatalysis and Biotransformation","volume":"26 1","pages":"0"},"PeriodicalIF":0.0,"publicationDate":"2023-09-25","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"135864039","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":"Covalent immobilization of recombinant L-asparaginase from <i>Geobacillus kaustophilus</i> on ReliZyme supports for mitigation of acrylamide","authors":"F. İnci Özdemir, Burcu Karaaslan, Ahmet Tülek, Deniz Yildirim","doi":"10.1080/10242422.2023.2257351","DOIUrl":"https://doi.org/10.1080/10242422.2023.2257351","url":null,"abstract":"AbstractIn this study, a new recombinant L-asparaginase from Geobacillus kaustophilus was covalently immobilized on ReliZyme EA403 (Relizyme/EA@GkASNase) and ReliZyme HA403 (Relizyme/HA@GkASNase) supports, and the free and immobilized L-asparaginases were used for their acrylamide mitigation performances in a food model system. The immobilization was confirmed by fourier-transform infrared spectroscopy, scanning electron microscopy, and transmission electron microscopy analysis. The optimum pH was determined as 8.5 for all the free and immobilized L-asparaginase samples. The optimum temperature was determined as 55 °C for the free enzyme and 60 °C for both the immobilized samples. The thermal stability of L-asparaginase was increased by 17.6 and 37.2 folds at 60 °C for Relizyme/EA@GkASNase and Relizyme/HA@GkASNase, respectively. Relizyme/EA@GkASNase and Relizyme/HA@GkASNase showed 16% and 43% of the catalytic efficiency of free GkASNase. The acrylamide mitigation performances of free and immobilized L-asparaginase samples were investigated using the L-asparagine–starch food model system and the formed acrylamide was completely mitigated in 1 h for all the L-asparaginase samples. Both the immobilized L-asparaginase samples retained at least 80% of their activities after five reuses. Hence, the immobilized GkASNase preparations can be potentially used in heat-treated food industries to remove acrylamide.Keywords: Geobacillus kaustophilusL-asparaginaseReliZymeacrylamide mitigation Disclosure statementAll authors declare that they have no conflict of interest.","PeriodicalId":8824,"journal":{"name":"Biocatalysis and Biotransformation","volume":"35 1","pages":"0"},"PeriodicalIF":0.0,"publicationDate":"2023-09-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"135396708","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":"Enhancing lipases reactivity in benzylic acetates hydrolysis: impact of kosmotropic salts under non-conventional conditions","authors":"Nabila Braia, Farida Larit, Mounia Merabet-Khelassi","doi":"10.1080/10242422.2023.2256931","DOIUrl":"https://doi.org/10.1080/10242422.2023.2256931","url":null,"abstract":"The effect of four kosmotropic salts additives, namely Na2CO3, Na2SO4, Na2HPO4, and NaCl, on the reactivity and selectivity of immobilized Candida antarctica lipase B (CAL-B) and a free lipase of Pseudomonas cepacia (PCL) during the hydrolysis of rac-4-(1-methoxyphenyl) ethyl and rac − 1-phenyl ethyl acetates (1a-2a) was investigated in this study. The study was carried out in two different mediums: non-aqueous conditions and in low water content media. The impact of the anionic counter-ions was examined in four solvents: nonpolar, semipolar, protic, and aprotic, with and without the aforementioned salts. In non-aqueous media, the addition of Na2CO3 significantly enhanced CAL-B hydrolysis rates, resulting in a conversion of 50% for 1a and 44% for 2a, with high enantioselectivities (E > 200). These effects were independent of the solvent hydrophobicity. In contrast, PCL required the presence of external water for effective hydrolysis of both acetates. The addition of salt additives had an adverse impact on PCL activity during the hydrolysis of 1a in hexane, toluene, and TBME solvents. However, when 2M2B was used, the inclusion of salt additives had a notable positive effect on the conversion rates, except for NaCl, which resulted in a lower conversion rate with a value of 15.5%. The presence of Na2CO3 improved the conversion rate during the hydrolysis of 2a in both hexane and TBME. Na2HPO4 further enhanced the conversion rate, reaching 44% in TBME. However, in 2M2B solvent, the addition of Na2HPO4 significantly reduced the enantioselectivity.","PeriodicalId":8824,"journal":{"name":"Biocatalysis and Biotransformation","volume":"35 1","pages":"0"},"PeriodicalIF":0.0,"publicationDate":"2023-09-13","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"135741344","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":"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}

{"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}

{"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}

{"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}

{"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}