S. Ramesh, B. S. Chouhan, G. Gupta, R. Ramteke, S. Chand, S. M. Husain
Aim: Coat protein (CP) genes encoded by Legume yellow mosaic viruses (LYMVs) were analysed to study molecular diversity and to devise effective PCR based assay to distinguish major Begomovirus species ( Mungbean yellow mosaic India virus and Mungbean yellow mosaic virus ) infecting soybean Design of the Study: All the known coat protein gene sequences encoded by begomoviruses causing yellow mosaic disease (YMD) in legumes were obtained from GenBank. YMD infected soybean leaf samples were collected from different parts of India during Kharif 2012 and species of virus infections identified using CP gene based primers in a PCR assay.
{"title":"Molecular Diversity Analysis of Coat Protein Gene Encoded by Legume Begomoviruses and PCR Assay to Detect Yellow Mosaic Viruses Infecting Soybean in India","authors":"S. Ramesh, B. S. Chouhan, G. Gupta, R. Ramteke, S. Chand, S. M. Husain","doi":"10.9734/BBJ/2016/24362","DOIUrl":"https://doi.org/10.9734/BBJ/2016/24362","url":null,"abstract":"Aim: Coat protein (CP) genes encoded by Legume yellow mosaic viruses (LYMVs) were analysed to study molecular diversity and to devise effective PCR based assay to distinguish major Begomovirus species ( Mungbean yellow mosaic India virus and Mungbean yellow mosaic virus ) infecting soybean Design of the Study: All the known coat protein gene sequences encoded by begomoviruses causing yellow mosaic disease (YMD) in legumes were obtained from GenBank. YMD infected soybean leaf samples were collected from different parts of India during Kharif 2012 and species of virus infections identified using CP gene based primers in a PCR assay.","PeriodicalId":90120,"journal":{"name":"British biotechnology journal","volume":"12 1","pages":"1-10"},"PeriodicalIF":0.0,"publicationDate":"2016-01-10","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"71164809","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Aim: The present study was conducted to evaluate the antifungal activity of camel faeces on some pathogenic fungi. Study Design: This is a descriptive evaluation study. Methodology: Camel faeces was extracted following Harborne method using organic solvents. Organic extracts besides, aqueous extract and ash were screened against clinical isolates using agar-well diffusion and incorporated methods. Parallel experiments were conducted with ketoconazole and nystatin, as positive control whereas; the vehicle solvents were used as negative control. Phytochemical analysis of Camel feaces was carried out following Harborne method. Short Research Article Suleiman et al.; BBJ, 13(2): 1-5, 2016; Article no.BBJ.24744 2 Results: Water and ethanol extracts exerted significant effect on dermatophytes followed by chloroform and hexane extracts compared to the ash which revealed no activity. Aspergillus and Pencillium species were found insensitive to all test extracts where as Candida albicans was found sensitive only to the hexane extract. Sterols and triterpenes were revealed on phytochemical analysis. Discussion: The antifungal activity of camel faeces might be due to the sterols and triterpenes. Conclusion: The study confirms efficacy of camel faeces as natural antifungal agent, and suggests the possibility of employing it for treatment of skin infections, caused by the test pathogens. The present study reveals first report on the use of camel faeces against some pathogenic fungi. Recommendation: Identification and characterization of novel molecules are highly recommended.
{"title":"Antifungal Activity of Camel Faeces with Special Reference to Dermatophytes","authors":"E. Suleiman, M. Kabashi, S. Elbashir, A. Elhassan","doi":"10.9734/BBJ/2016/24744","DOIUrl":"https://doi.org/10.9734/BBJ/2016/24744","url":null,"abstract":"Aim: The present study was conducted to evaluate the antifungal activity of camel faeces on some pathogenic fungi. Study Design: This is a descriptive evaluation study. Methodology: Camel faeces was extracted following Harborne method using organic solvents. Organic extracts besides, aqueous extract and ash were screened against clinical isolates using agar-well diffusion and incorporated methods. Parallel experiments were conducted with ketoconazole and nystatin, as positive control whereas; the vehicle solvents were used as negative control. Phytochemical analysis of Camel feaces was carried out following Harborne method. Short Research Article Suleiman et al.; BBJ, 13(2): 1-5, 2016; Article no.BBJ.24744 2 Results: Water and ethanol extracts exerted significant effect on dermatophytes followed by chloroform and hexane extracts compared to the ash which revealed no activity. Aspergillus and Pencillium species were found insensitive to all test extracts where as Candida albicans was found sensitive only to the hexane extract. Sterols and triterpenes were revealed on phytochemical analysis. Discussion: The antifungal activity of camel faeces might be due to the sterols and triterpenes. Conclusion: The study confirms efficacy of camel faeces as natural antifungal agent, and suggests the possibility of employing it for treatment of skin infections, caused by the test pathogens. The present study reveals first report on the use of camel faeces against some pathogenic fungi. Recommendation: Identification and characterization of novel molecules are highly recommended.","PeriodicalId":90120,"journal":{"name":"British biotechnology journal","volume":"251 1","pages":"1-5"},"PeriodicalIF":0.0,"publicationDate":"2016-01-10","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"71164896","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
H. Hamoud, Y. Soliman, Samah M. M. Eldemery, K. Abdellatif
{"title":"Field Performance and Gene Expression of Drought Stress Tolerance in Cotton (Gossypium barbadense L.)","authors":"H. Hamoud, Y. Soliman, Samah M. M. Eldemery, K. Abdellatif","doi":"10.9734/BBJ/2016/26643","DOIUrl":"https://doi.org/10.9734/BBJ/2016/26643","url":null,"abstract":"","PeriodicalId":90120,"journal":{"name":"British biotechnology journal","volume":"14 1","pages":"1-9"},"PeriodicalIF":0.0,"publicationDate":"2016-01-10","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"71165215","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Studies on the Proximate, Functional and Antioxidant Properties of Fermented and Unfermented Kariya (Hildergardia barterii) Seed Protein Hydrolysates Obtained by Enzymatic Hydrolysis","authors":"O. Gbadamosi, A. Famuwagun","doi":"10.9734/BBJ/2016/26685","DOIUrl":"https://doi.org/10.9734/BBJ/2016/26685","url":null,"abstract":"","PeriodicalId":90120,"journal":{"name":"British biotechnology journal","volume":"14 1","pages":"1-14"},"PeriodicalIF":0.0,"publicationDate":"2016-01-10","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"71165279","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
K. Dhanalakshmi, P. Bhavan, G. Rajkumar, V. Nathiya, V. Srinivasan, T. Satgurunathan
{"title":"Phytochemical Characterization of Couch Grass (Cynodon dactylon) and Its Growth Promoting Potential on the Freshwater Prawn Macrobrachium rosenbergii Post-Larvae","authors":"K. Dhanalakshmi, P. Bhavan, G. Rajkumar, V. Nathiya, V. Srinivasan, T. Satgurunathan","doi":"10.9734/BBJ/2016/26863","DOIUrl":"https://doi.org/10.9734/BBJ/2016/26863","url":null,"abstract":"","PeriodicalId":90120,"journal":{"name":"British biotechnology journal","volume":"14 1","pages":"1-24"},"PeriodicalIF":0.0,"publicationDate":"2016-01-10","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"71165296","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Influence of Various Nitrogen Sources on Biomass and Lipid Production by Chlorella vulgaris","authors":"O. Agwa, G. Abu","doi":"10.9734/BBJ/2016/21727","DOIUrl":"https://doi.org/10.9734/BBJ/2016/21727","url":null,"abstract":"","PeriodicalId":90120,"journal":{"name":"British biotechnology journal","volume":"15 1","pages":"1-13"},"PeriodicalIF":0.0,"publicationDate":"2016-01-10","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"71163883","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Significant of the Study: Biomass is renewable, organic, plant and animal derived source of biomaterial that can be converted into different forms of biofuel, bioplastic, bio-solvent, and bioenergy using different biotechnological procedures. Biomass derived bio-fuel is biodegradable, nontoxic, sustainable and substitute for fossil fuel as well as capable to reduce greenhouse gas emission. It is renewable and outstanding energy resource for the creation of steam and electricity, transportation fuel, manufacturing industries. Biomass derived from animal and plants like, fruits, vegetable, crops, fish, chicken and other animal byproducts or waste biomass which can be used for bioenergy production like biofuel and nano-catalyst for biofuel. Original Research Article Hossain and AlEissa; BBJ, 10(4): 1-9, 2016; Article no.BBJ.22338 2 Aim: The purpose of this study was to compare and investigate the suitable biodiesel properties produced from waste fish byproducts, palm and sunflower oil which were more economically viable. Results: There was a total of 7, 5 and 4 types of fatty acid methyl esters presence in the fish, palm and sunflower biodiesel, respectively. The quality of biodiesel such as viscosity, total acid number, fuel consumption and emission rate was evaluated. The kinematic viscosity was maintained ASTM standard in case of all produced biodiesel. However, sunflower biodiesel was slightly viscous compared to palm and fish biodiesel. Metal elements such as phosphorus, magnesium, and calcium were present moderately in all biodiesel but it was limited range in fish oil. In the engine tests, the emissions of unburned hydrocarbons, oxides of nitrogen and carbon monoxide were lower in palm biodiesel than in sunflower and fish biodiesel. Fuel consumption was higher in palm biodiesel. Fish biodiesel had the lowest fuel consumption than that of palm and sunflower biodiesel. Conclusion: It can be concluded that waste palm oil and fish oil can be considered as a great potential source for commercial biodiesel.
{"title":"Biodiesel Fuel Production from Palm, Sunflower Waste Cooking Oil and Fish Byproduct Waste as Renewable Energy and Environmental Recycling Process","authors":"A. Hossain, Mohammed S. Aleissa","doi":"10.9734/bbj/2016/22338","DOIUrl":"https://doi.org/10.9734/bbj/2016/22338","url":null,"abstract":"Significant of the Study: Biomass is renewable, organic, plant and animal derived source of biomaterial that can be converted into different forms of biofuel, bioplastic, bio-solvent, and bioenergy using different biotechnological procedures. Biomass derived bio-fuel is biodegradable, nontoxic, sustainable and substitute for fossil fuel as well as capable to reduce greenhouse gas emission. It is renewable and outstanding energy resource for the creation of steam and electricity, transportation fuel, manufacturing industries. Biomass derived from animal and plants like, fruits, vegetable, crops, fish, chicken and other animal byproducts or waste biomass which can be used for bioenergy production like biofuel and nano-catalyst for biofuel. Original Research Article Hossain and AlEissa; BBJ, 10(4): 1-9, 2016; Article no.BBJ.22338 2 Aim: The purpose of this study was to compare and investigate the suitable biodiesel properties produced from waste fish byproducts, palm and sunflower oil which were more economically viable. Results: There was a total of 7, 5 and 4 types of fatty acid methyl esters presence in the fish, palm and sunflower biodiesel, respectively. The quality of biodiesel such as viscosity, total acid number, fuel consumption and emission rate was evaluated. The kinematic viscosity was maintained ASTM standard in case of all produced biodiesel. However, sunflower biodiesel was slightly viscous compared to palm and fish biodiesel. Metal elements such as phosphorus, magnesium, and calcium were present moderately in all biodiesel but it was limited range in fish oil. In the engine tests, the emissions of unburned hydrocarbons, oxides of nitrogen and carbon monoxide were lower in palm biodiesel than in sunflower and fish biodiesel. Fuel consumption was higher in palm biodiesel. Fish biodiesel had the lowest fuel consumption than that of palm and sunflower biodiesel. Conclusion: It can be concluded that waste palm oil and fish oil can be considered as a great potential source for commercial biodiesel.","PeriodicalId":90120,"journal":{"name":"British biotechnology journal","volume":"1 1","pages":"1-9"},"PeriodicalIF":0.0,"publicationDate":"2016-01-10","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"71164092","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
A. Priyadarshini, Sameer K. Singdevsachan, S. Tripathy, Y. K. Mohanta, J. Patra, B. Sethi
The mangrove ecosystem of India is an extensively unexplored source for actinomycetes with the potential to produce secondary metabolites of biological importance. In this study, twenty two actinomycetes were isolated from different soil samples collected from the Bhitarkanika mangrove forest along Odisha coast, India. These isolates were identified as Streptomyces sp. based on their morphological, physiological and biochemical characteristics as described in the International Streptomyces Project. Out of twenty two actinomycetes (designated as BSA-1 to BSA-22) isolates, only four isolates (BSA-5, BSA-10, BSA-11 and BSA-15) displayed significant antimicrobial Original Research Article Priyadarshini et al.; BBJ, 12(2): 1-13, 2016; Article no.BBJ.24102 2 properties in term of antagonistic activity against six human pathogenic bacterial strains (Staphylococcus aureus, Shigella flexneri, Bacillus licheniformis, Bacillus brevis, Pseudomonas aeruginosa and Escherichia coli). All these isolates exhibited excellent antimicrobial activity in a range of 14.0-22.0 mm as inhibition zone against the above studied human pathogens with highest activity displayed by the isolate BSA-11. The isolate, Streptomyces sp. BSA-11 was further identified up to the species level by 16S rRNA gene sequence analysis. The BLAST analysis confirmed that Streptomyces sp. BSA-11 was homologous to Streptomyces himastatinicus of order Actinomycetles and class Actinobacteria. The novel actinomycete, Streptomyces himastatinicus BSA-11 from Bhitarkanika has the ability to produce extracellular potent bioactive compounds which can be a potential source of many antimicrobials.
{"title":"Isolation and Identification of Actinomycetes from Mangrove Soil and Extraction of Secondary Metabolites for Antibacterial Activity","authors":"A. Priyadarshini, Sameer K. Singdevsachan, S. Tripathy, Y. K. Mohanta, J. Patra, B. Sethi","doi":"10.9734/bbj/2016/24102","DOIUrl":"https://doi.org/10.9734/bbj/2016/24102","url":null,"abstract":"The mangrove ecosystem of India is an extensively unexplored source for actinomycetes with the potential to produce secondary metabolites of biological importance. In this study, twenty two actinomycetes were isolated from different soil samples collected from the Bhitarkanika mangrove forest along Odisha coast, India. These isolates were identified as Streptomyces sp. based on their morphological, physiological and biochemical characteristics as described in the International Streptomyces Project. Out of twenty two actinomycetes (designated as BSA-1 to BSA-22) isolates, only four isolates (BSA-5, BSA-10, BSA-11 and BSA-15) displayed significant antimicrobial Original Research Article Priyadarshini et al.; BBJ, 12(2): 1-13, 2016; Article no.BBJ.24102 2 properties in term of antagonistic activity against six human pathogenic bacterial strains (Staphylococcus aureus, Shigella flexneri, Bacillus licheniformis, Bacillus brevis, Pseudomonas aeruginosa and Escherichia coli). All these isolates exhibited excellent antimicrobial activity in a range of 14.0-22.0 mm as inhibition zone against the above studied human pathogens with highest activity displayed by the isolate BSA-11. The isolate, Streptomyces sp. BSA-11 was further identified up to the species level by 16S rRNA gene sequence analysis. The BLAST analysis confirmed that Streptomyces sp. BSA-11 was homologous to Streptomyces himastatinicus of order Actinomycetles and class Actinobacteria. The novel actinomycete, Streptomyces himastatinicus BSA-11 from Bhitarkanika has the ability to produce extracellular potent bioactive compounds which can be a potential source of many antimicrobials.","PeriodicalId":90120,"journal":{"name":"British biotechnology journal","volume":"12 1","pages":"1-13"},"PeriodicalIF":0.0,"publicationDate":"2016-01-10","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"71164158","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Aims: A total of five mutant strains of Bacillus subtilis subsp. spizizenii ATCC 6633 designated as the MXB 1, MXB 2, MXB 3, MXB 4 and MXB 5 were developed using random mutagenesis of ethyl methane sulfonate (EMS) and acridine orange (AO) in our previous study. Based on our present investigation, we identified, verified and sequenced xylanase gene of mutant strains of B. subtilis ATCC 6633 as the potent bacterial xylanase producers under submerged fermentation. Furthermore, amino acid analysis and comparison between the xylanases of the mutants and other xylanolytic bacteria were also elucidated. Overall, this study would provide gene and protein molecular information correlating nucleotide and amino acid structure related to the increased xylanase production by random mutagenesis. In respect to the objectives of this study, we compared the endoxylanase sequence of wild type B. subtilis ATCC 6633 with its mutants in order to determine their possible site(s) of mutagenesis and to analyse amino acid xylanase sequence of the mutants of B. subtilis ATCC 6633. Methodology: After the verification of xylanase production by all mutants of B. subtilis ATCC 6633 Original Research Article Ling Ho and Chinonso; BBJ, 12(1): 1-20, 2016; Article no.BBJ.23057 2 on the xylan agar using Congo-red staining in the previous study, xylanase gene of the mutants was amplified from the genomic DNA to detect the mutagenesis site(s) by synthesizing primers directed against the sequence of xylanase gene obtained from the wild type of Bacillus subtilis subsp. spizizenii ATCC 6633. Results: The comparison of xylanase genes from different mutants of B. subtilis and the wild type revealed the site(s) of mutagenesis. Interestingly, the mutations of the mutants of B. subtilis ATCC 6633 in this study were significantly reflected at the 5’ end of the mutants xylanase genes. The open reading frames (ORF) of the mutant xylanase genes ranged from 644 bp to 684 bp with translated encoding protein between 214 and 228 amino acid residues were obtained. On the other hand, predicted molecular mass from 23.94 kDa to 25.40 kDa and theoretical pI which ranged from 8.63 to 9.16 were attained from all of the mutant strains in this study. Based on the characteristics obtained, the mutant xylanases were suggested to belong to Glycosyl Hydrolase (GH) Family 11 with 98% homology to endo-1,4-beta-xylanase of B. subtilis subsp. spizizenii of W23. In fact, conserved regions, signal peptide, a cleavage site between the Ala28 and Ala29 residues and four Tyr residues specific to GH Family 11 xylanase were also observed and detected in all mutants. Indeed, two conserved glutamate residues of E94 and E183 that directly involved in the enzyme catalytic mechanism were also detected in the amino acid sequences of the mutants. The analysis of the deduced amino acid sequences revealed that the mutations in the signal peptide regions fostered increased hydrophobic core of xylanase residue. We suggested that thes
{"title":"Detection and Analysis of the Random Mutagenesis Site(s) of Xylanase Gene from Mutants of Bacillus subtilis subsp. spizizenii ATCC 6633","authors":"H. Ho, Ajounmah Maryann Chinonso","doi":"10.9734/bbj/2016/23057","DOIUrl":"https://doi.org/10.9734/bbj/2016/23057","url":null,"abstract":"Aims: A total of five mutant strains of Bacillus subtilis subsp. spizizenii ATCC 6633 designated as the MXB 1, MXB 2, MXB 3, MXB 4 and MXB 5 were developed using random mutagenesis of ethyl methane sulfonate (EMS) and acridine orange (AO) in our previous study. Based on our present investigation, we identified, verified and sequenced xylanase gene of mutant strains of B. subtilis ATCC 6633 as the potent bacterial xylanase producers under submerged fermentation. Furthermore, amino acid analysis and comparison between the xylanases of the mutants and other xylanolytic bacteria were also elucidated. Overall, this study would provide gene and protein molecular information correlating nucleotide and amino acid structure related to the increased xylanase production by random mutagenesis. In respect to the objectives of this study, we compared the endoxylanase sequence of wild type B. subtilis ATCC 6633 with its mutants in order to determine their possible site(s) of mutagenesis and to analyse amino acid xylanase sequence of the mutants of B. subtilis ATCC 6633. Methodology: After the verification of xylanase production by all mutants of B. subtilis ATCC 6633 Original Research Article Ling Ho and Chinonso; BBJ, 12(1): 1-20, 2016; Article no.BBJ.23057 2 on the xylan agar using Congo-red staining in the previous study, xylanase gene of the mutants was amplified from the genomic DNA to detect the mutagenesis site(s) by synthesizing primers directed against the sequence of xylanase gene obtained from the wild type of Bacillus subtilis subsp. spizizenii ATCC 6633. Results: The comparison of xylanase genes from different mutants of B. subtilis and the wild type revealed the site(s) of mutagenesis. Interestingly, the mutations of the mutants of B. subtilis ATCC 6633 in this study were significantly reflected at the 5’ end of the mutants xylanase genes. The open reading frames (ORF) of the mutant xylanase genes ranged from 644 bp to 684 bp with translated encoding protein between 214 and 228 amino acid residues were obtained. On the other hand, predicted molecular mass from 23.94 kDa to 25.40 kDa and theoretical pI which ranged from 8.63 to 9.16 were attained from all of the mutant strains in this study. Based on the characteristics obtained, the mutant xylanases were suggested to belong to Glycosyl Hydrolase (GH) Family 11 with 98% homology to endo-1,4-beta-xylanase of B. subtilis subsp. spizizenii of W23. In fact, conserved regions, signal peptide, a cleavage site between the Ala28 and Ala29 residues and four Tyr residues specific to GH Family 11 xylanase were also observed and detected in all mutants. Indeed, two conserved glutamate residues of E94 and E183 that directly involved in the enzyme catalytic mechanism were also detected in the amino acid sequences of the mutants. The analysis of the deduced amino acid sequences revealed that the mutations in the signal peptide regions fostered increased hydrophobic core of xylanase residue. We suggested that thes","PeriodicalId":90120,"journal":{"name":"British biotechnology journal","volume":"12 1","pages":"1-20"},"PeriodicalIF":0.0,"publicationDate":"2016-01-10","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"71164346","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
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