Pub Date : 2022-02-15DOI: 10.7324/jabb.2022.100221
Aggarwal Sunita, Gupta Siddharth, Sehgal Shalini, S. Praneeta, Sen Aparajita, Gulyani Garishma, Jain Anmol
Sunita Aggarwal1*, Siddharth Gupta2, Shalini Sehgal3, Praneeta Srivastava1, Aparajita Sen4, Garishma Gulyani5, Anmol Jain2 1Department of Microbiology, Institute of Home Economics, University of Delhi, New Delhi, India. 2Department of Business Management, Ram Lal Anand College, University of Delhi, New Delhi, India. 3Department of Food Technology, Bhaskaracharya College of Applied Sciences, University of Delhi, New Delhi, India. 4Department of Genetics, University of Delhi, South Campus, New Delhi, India. 5Department of Commerce, Vivekananda Institute of Professional Studies, IP University, New Delhi, India.
{"title":"Vitamin K2: An emerging essential nutraceutical and its market potential","authors":"Aggarwal Sunita, Gupta Siddharth, Sehgal Shalini, S. Praneeta, Sen Aparajita, Gulyani Garishma, Jain Anmol","doi":"10.7324/jabb.2022.100221","DOIUrl":"https://doi.org/10.7324/jabb.2022.100221","url":null,"abstract":"Sunita Aggarwal1*, Siddharth Gupta2, Shalini Sehgal3, Praneeta Srivastava1, Aparajita Sen4, Garishma Gulyani5, Anmol Jain2 1Department of Microbiology, Institute of Home Economics, University of Delhi, New Delhi, India. 2Department of Business Management, Ram Lal Anand College, University of Delhi, New Delhi, India. 3Department of Food Technology, Bhaskaracharya College of Applied Sciences, University of Delhi, New Delhi, India. 4Department of Genetics, University of Delhi, South Campus, New Delhi, India. 5Department of Commerce, Vivekananda Institute of Professional Studies, IP University, New Delhi, India.","PeriodicalId":15032,"journal":{"name":"Journal of Applied Biology and Biotechnology","volume":"14 1","pages":""},"PeriodicalIF":0.0,"publicationDate":"2022-02-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"74009614","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}
Pub Date : 2022-02-15DOI: 10.7324/jabb.2022.100204
H. Hasnain, Edward-Atit Anastasia Shera, Julaihi Norzainizul, Tommy Rina, Nisar Mehvish, Hamdan Nurhazlina, Ehara Hiroshi
Hasnain Hussain1* , Anastasia Shera Edward-Atit1, Norzainizul Julaihi2, Rina Tommy2, Mehvish Nisar1, Nurhazlina Hamdan1, Hiroshi Ehara3 1Centre for Sago Research, Faculty of Resource Science and Technology, Universiti Malaysia Sarawak, Sarawak, Malaysia. 2PELITA Mukah Sebakong Sago Plantation Sdn Bhd, Mukah, Sarawak. 3International Center for Research and Education in Agriculture, Nagoya University, Nagoya, Japan.
{"title":"Identification of differentially expressed transcripts for trunk formation in sago palm using annealing control primer GeneFishing technique","authors":"H. Hasnain, Edward-Atit Anastasia Shera, Julaihi Norzainizul, Tommy Rina, Nisar Mehvish, Hamdan Nurhazlina, Ehara Hiroshi","doi":"10.7324/jabb.2022.100204","DOIUrl":"https://doi.org/10.7324/jabb.2022.100204","url":null,"abstract":"Hasnain Hussain1* , Anastasia Shera Edward-Atit1, Norzainizul Julaihi2, Rina Tommy2, Mehvish Nisar1, Nurhazlina Hamdan1, Hiroshi Ehara3 1Centre for Sago Research, Faculty of Resource Science and Technology, Universiti Malaysia Sarawak, Sarawak, Malaysia. 2PELITA Mukah Sebakong Sago Plantation Sdn Bhd, Mukah, Sarawak. 3International Center for Research and Education in Agriculture, Nagoya University, Nagoya, Japan.","PeriodicalId":15032,"journal":{"name":"Journal of Applied Biology and Biotechnology","volume":"1 1","pages":""},"PeriodicalIF":0.0,"publicationDate":"2022-02-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"78353724","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}
Pub Date : 2022-01-01DOI: 10.7324/jabb.2021.100104
Wongsnansilp Tassnapa, Phinrub Wikit, J. Niran
Marigold (Tagetes erecta L.) is a perennial edible medicinal plant. In order to test the allelopathic effect of marigold leaf extract on Chlorella vulgaris, the microalgae growth conditions under different concentrations of marigold leaf extract (0 to 50 g/l) were studied. The results showed that microalgal growth was inhibited by marigold leaf extract, and inhibition commonly increased with increasing concentration of the extract and culture time. The maximum inhibition rate (90.1%) appeared in leaf extract of 30 g/l after 14 days of incubation; marigold leaf extract induced chlorophyll degradation in algae cells, increased the permeability of cell membrane, and caused exudation of soluble protein and nucleic acid, leading to the damage of algae cell structure and metabolic dysfunction. The present results confirmed that marigold leaf extract has an allelopathic inhibition effect on C. vulgaris, and the results could be further applied to develop safe and efficient algaecides.
{"title":"Allelopathic effect of marigold (Tagetes erecta L.) leaf extract on growth of Chlorella vulgaris","authors":"Wongsnansilp Tassnapa, Phinrub Wikit, J. Niran","doi":"10.7324/jabb.2021.100104","DOIUrl":"https://doi.org/10.7324/jabb.2021.100104","url":null,"abstract":"Marigold (Tagetes erecta L.) is a perennial edible medicinal plant. In order to test the allelopathic effect of marigold leaf extract on Chlorella vulgaris, the microalgae growth conditions under different concentrations of marigold leaf extract (0 to 50 g/l) were studied. The results showed that microalgal growth was inhibited by marigold leaf extract, and inhibition commonly increased with increasing concentration of the extract and culture time. The maximum inhibition rate (90.1%) appeared in leaf extract of 30 g/l after 14 days of incubation; marigold leaf extract induced chlorophyll degradation in algae cells, increased the permeability of cell membrane, and caused exudation of soluble protein and nucleic acid, leading to the damage of algae cell structure and metabolic dysfunction. The present results confirmed that marigold leaf extract has an allelopathic inhibition effect on C. vulgaris, and the results could be further applied to develop safe and efficient algaecides.","PeriodicalId":15032,"journal":{"name":"Journal of Applied Biology and Biotechnology","volume":"1 1","pages":""},"PeriodicalIF":0.0,"publicationDate":"2022-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"71217022","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}
Pub Date : 2022-01-01DOI: 10.7324/jabb.2021.100110
Bhowmik Ratul, R. Shubham, Sengupta Sounok, R. Lokesh
Vibriosis, a bacterial infection, is very much responsible for causing significant losses in the aquaculture industry. Chloramphenicol acetyltransferase is an antibiotic resistant enzyme present in the vibrio class of bacteria. Florfenicol, a benzene sulphonyl antibiotic is the lead molecule in this study. OSIRIS property explorer, Chemsketch, Molinspiration, pre ADMET tools were used for ligand modification, while AutoDock Vina, PyMOL, and LigPlot+ were used for protein–ligand docking analysis. Florfenicol demonstrated a free binding energy of −6.0 kcal/mol and poor ADMET properties. Ligand structures were optimized using “uff” forcefield and conjugate gradients algorithm. Primary drug designing was done with emphasis on ADMET properties that yielded a total of 15 modified ligands. Among these 15 ligands, F006 exhibited the highest dock score of −7.3 kcal/mol along with significant ADME properties and was hence chosen for further secondary modifications. Ligand F006 was further modified on the basis of ADMET properties to obtain 17 modified ligands. Among the 17 secondary ligands, F016 demonstrated strong binding affinity of −8.6 kcal/mol and also demonstrated significant ADME properties. Based on the results of this studies, the structure based computational drug design of florfenicol concluded that the modified ligand F016 designed in this study has good ADMET properties along with strong binding affinity towards the drug target chloramphenicol acetyltransferase protein and could be a potential solution in treating vibriosis.
{"title":"Computer aided drug design of florfenicol to target chloramphenicol acetyltransferase of vibriosis causing pathogens","authors":"Bhowmik Ratul, R. Shubham, Sengupta Sounok, R. Lokesh","doi":"10.7324/jabb.2021.100110","DOIUrl":"https://doi.org/10.7324/jabb.2021.100110","url":null,"abstract":"Vibriosis, a bacterial infection, is very much responsible for causing significant losses in the aquaculture industry. Chloramphenicol acetyltransferase is an antibiotic resistant enzyme present in the vibrio class of bacteria. Florfenicol, a benzene sulphonyl antibiotic is the lead molecule in this study. OSIRIS property explorer, Chemsketch, Molinspiration, pre ADMET tools were used for ligand modification, while AutoDock Vina, PyMOL, and LigPlot+ were used for protein–ligand docking analysis. Florfenicol demonstrated a free binding energy of −6.0 kcal/mol and poor ADMET properties. Ligand structures were optimized using “uff” forcefield and conjugate gradients algorithm. Primary drug designing was done with emphasis on ADMET properties that yielded a total of 15 modified ligands. Among these 15 ligands, F006 exhibited the highest dock score of −7.3 kcal/mol along with significant ADME properties and was hence chosen for further secondary modifications. Ligand F006 was further modified on the basis of ADMET properties to obtain 17 modified ligands. Among the 17 secondary ligands, F016 demonstrated strong binding affinity of −8.6 kcal/mol and also demonstrated significant ADME properties. Based on the results of this studies, the structure based computational drug design of florfenicol concluded that the modified ligand F016 designed in this study has good ADMET properties along with strong binding affinity towards the drug target chloramphenicol acetyltransferase protein and could be a potential solution in treating vibriosis.","PeriodicalId":15032,"journal":{"name":"Journal of Applied Biology and Biotechnology","volume":"1 1","pages":""},"PeriodicalIF":0.0,"publicationDate":"2022-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"71217574","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}
Pub Date : 2022-01-01DOI: 10.7324/jabb.2021.100114
S. Suganthi, Kumar Kavitha Saravana
The application of agro-waste in the form of compost is an ecofriendly approach to minimize the use of chemicals for crop improvement. Hence, compost was prepared by the Indore method from banana spathe obtained from five popular varieties of banana cultivated in Tamil Nadu, India, and its growth promoting ability was tested on the rice cultivar CO-51. The banana spathe was applied as both an aqueous extract and compost to evaluate the growth parameters in bioassays and pot culture experiments. The compost improved the growth in terms of root length, shoot length, biomass, tillers, length, and width of flag leaf and yield in CO-51 rice cultivar significantly (p < 0.001%) when compared to the untreated control and fertilizer-treated plants. The maximum yield was observed in the treatment with Rasthali spathe. Biochemical analysis of the compost-treated rice plants showed an increase in chlorophyll, carotenoid, carbohydrate, protein, and amino acid content when compared to the untreated control plants. The results from the study suggest that the banana spathe compost could be used as an effective organic fertilizer for the growth of rice plants thus providing a strategy to reduce landfills, as well as the use of fertilizers, thereby further helping to protect the agroecosystem.
{"title":"Application of banana spathe extracts and compost for improving growth in rice plants","authors":"S. Suganthi, Kumar Kavitha Saravana","doi":"10.7324/jabb.2021.100114","DOIUrl":"https://doi.org/10.7324/jabb.2021.100114","url":null,"abstract":"The application of agro-waste in the form of compost is an ecofriendly approach to minimize the use of chemicals for crop improvement. Hence, compost was prepared by the Indore method from banana spathe obtained from five popular varieties of banana cultivated in Tamil Nadu, India, and its growth promoting ability was tested on the rice cultivar CO-51. The banana spathe was applied as both an aqueous extract and compost to evaluate the growth parameters in bioassays and pot culture experiments. The compost improved the growth in terms of root length, shoot length, biomass, tillers, length, and width of flag leaf and yield in CO-51 rice cultivar significantly (p < 0.001%) when compared to the untreated control and fertilizer-treated plants. The maximum yield was observed in the treatment with Rasthali spathe. Biochemical analysis of the compost-treated rice plants showed an increase in chlorophyll, carotenoid, carbohydrate, protein, and amino acid content when compared to the untreated control plants. The results from the study suggest that the banana spathe compost could be used as an effective organic fertilizer for the growth of rice plants thus providing a strategy to reduce landfills, as well as the use of fertilizers, thereby further helping to protect the agroecosystem.","PeriodicalId":15032,"journal":{"name":"Journal of Applied Biology and Biotechnology","volume":"1 1","pages":""},"PeriodicalIF":0.0,"publicationDate":"2022-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"71217984","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}
Pub Date : 2022-01-01DOI: 10.7324/jabb.2021.100121
R. Rajesh Kumar, P. Preeti, S. Sadhana, Hajela Krishnan
The present study was carried out to isolate, purify, and characterize protease from the seeds of Cyamopsis tetragonoloba. The protease was precipitated by a 60% ammonium sulfate cut and further purified by elution from ion-exchange chromatography at 0.3 M NaCl. The sodium dodecyl sulfate-polyacrylamide gel electrophoresis result showed that protease was monomeric having 69.9 kDa molecular weight. Gelatin zymography was carried out to confirm the proteolytic activity of the protease. The protease has a wide range of substrate specificity and could cleave natural substrates like casein, gelatin, bovine serum albumin (BSA), hemoglobin (Hb), and synthetic substrate like N-αBenzoyl-DL-arginine ϸ-nitroanilide (BAPNA). The Vmax value of the protease was 102.04 μM/minute with casein as the substrate and Km value was 56.56 μM/minute. The purified protease was completely inhibited by serine proteases inhibitors like Phenyl Methyl Sulfonyl Fluoride, soybean trypsin inhibitor, and aprotinin, and not inhibited by other protease inhibitors. This concluded that the purified protease was serine protease. The protease was highly stable at a wide range of temperatures from 20°C to 70°C. Gelatin showed the highest proteolytic activity when compared to the casein, Hb, and BSA. BAPNA showed 1.5101 U/mg specific activity. The sugar content of protease was estimated by the method of DuBois. The protease was highly glycosylated and contained 35 μg of sugar in 0.2 mg of protease.
{"title":"Purification and biochemical characterization of protease from the seeds of Cyamopsis tetragonoloba","authors":"R. Rajesh Kumar, P. Preeti, S. Sadhana, Hajela Krishnan","doi":"10.7324/jabb.2021.100121","DOIUrl":"https://doi.org/10.7324/jabb.2021.100121","url":null,"abstract":"The present study was carried out to isolate, purify, and characterize protease from the seeds of Cyamopsis tetragonoloba. The protease was precipitated by a 60% ammonium sulfate cut and further purified by elution from ion-exchange chromatography at 0.3 M NaCl. The sodium dodecyl sulfate-polyacrylamide gel electrophoresis result showed that protease was monomeric having 69.9 kDa molecular weight. Gelatin zymography was carried out to confirm the proteolytic activity of the protease. The protease has a wide range of substrate specificity and could cleave natural substrates like casein, gelatin, bovine serum albumin (BSA), hemoglobin (Hb), and synthetic substrate like N-αBenzoyl-DL-arginine ϸ-nitroanilide (BAPNA). The Vmax value of the protease was 102.04 μM/minute with casein as the substrate and Km value was 56.56 μM/minute. The purified protease was completely inhibited by serine proteases inhibitors like Phenyl Methyl Sulfonyl Fluoride, soybean trypsin inhibitor, and aprotinin, and not inhibited by other protease inhibitors. This concluded that the purified protease was serine protease. The protease was highly stable at a wide range of temperatures from 20°C to 70°C. Gelatin showed the highest proteolytic activity when compared to the casein, Hb, and BSA. BAPNA showed 1.5101 U/mg specific activity. The sugar content of protease was estimated by the method of DuBois. The protease was highly glycosylated and contained 35 μg of sugar in 0.2 mg of protease.","PeriodicalId":15032,"journal":{"name":"Journal of Applied Biology and Biotechnology","volume":"1 1","pages":""},"PeriodicalIF":0.0,"publicationDate":"2022-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"71217935","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}
Pub Date : 2022-01-01DOI: 10.7324/jabb.2021.100115
R. Pilli
Ground nut (Arachis hypogaea L.) is one of the most important crops universally cultivated in many countries and India is the second largest producer of groundnut. Fusarium oxysporum is a soil borne and devastating fungal plant pathogen that causes Fusarium wilt in A. hypogaea. In fungi, the genes involved in secondary metabolite (SM) biosynthesis are often localized in close proximity in the genome, usually adjacent to each other, and are regulated in a co-ordinated manner. The biosynthetic gene cluster of SM encodes transcription factors, protein for transport and enzymes. Fusaric acid (FA) is a highly toxic SM derived from polyketide and is produced by several species belonging to the genus Fusarium which plays a significant role in disease development. A comparative genomic and transcriptomic analysis of the FA biosynthetic gene (FUB) cluster in A. hypogaea L. indicates that the FUB cluster is comprising 12 genes (FUB-1 to FUB-12). Among them, FUB-1 and FUB-11 are expressed significantly, and quantification by real-time polymerase chain reaction shows a 1.1-fold and 1.3-fold increase, respectively. RNA Transcriptome sequencing analysis of leaf samples infected with F. oxysporum and leaf samples treated with combinations of biocontrol agents (Trichoderma viride + Pseudomonas fluorescens) depicted 111 infected specific genes, 1162 treated specific genes, 33 up and downregulatory genes, and also the toxic levels of FA were significantly reduced (0.1-fold increase in FUB-1 and 0.3-fold increase in FUB-11 expression). Gene ontology and pathway analysis results shed light onto the genetic and biochemical mechanism for the identification of FUB genes associated with FA production in F. oxysporum infecting A. hypogaea L. and potential benefits of using combination treatments to suppress Fusarium wilt disease.
{"title":"Expression of FUB-1 and FUB-11 as Toxic genes responsible for virulence during pathogenesis and combination of biocontrol agents in inhibition of Fusaric acid of Fusarium oxysporum causing Fusarium wilt of Arachis hypogaea L.","authors":"R. Pilli","doi":"10.7324/jabb.2021.100115","DOIUrl":"https://doi.org/10.7324/jabb.2021.100115","url":null,"abstract":"Ground nut (Arachis hypogaea L.) is one of the most important crops universally cultivated in many countries and India is the second largest producer of groundnut. Fusarium oxysporum is a soil borne and devastating fungal plant pathogen that causes Fusarium wilt in A. hypogaea. In fungi, the genes involved in secondary metabolite (SM) biosynthesis are often localized in close proximity in the genome, usually adjacent to each other, and are regulated in a co-ordinated manner. The biosynthetic gene cluster of SM encodes transcription factors, protein for transport and enzymes. Fusaric acid (FA) is a highly toxic SM derived from polyketide and is produced by several species belonging to the genus Fusarium which plays a significant role in disease development. A comparative genomic and transcriptomic analysis of the FA biosynthetic gene (FUB) cluster in A. hypogaea L. indicates that the FUB cluster is comprising 12 genes (FUB-1 to FUB-12). Among them, FUB-1 and FUB-11 are expressed significantly, and quantification by real-time polymerase chain reaction shows a 1.1-fold and 1.3-fold increase, respectively. RNA Transcriptome sequencing analysis of leaf samples infected with F. oxysporum and leaf samples treated with combinations of biocontrol agents (Trichoderma viride + Pseudomonas fluorescens) depicted 111 infected specific genes, 1162 treated specific genes, 33 up and downregulatory genes, and also the toxic levels of FA were significantly reduced (0.1-fold increase in FUB-1 and 0.3-fold increase in FUB-11 expression). Gene ontology and pathway analysis results shed light onto the genetic and biochemical mechanism for the identification of FUB genes associated with FA production in F. oxysporum infecting A. hypogaea L. and potential benefits of using combination treatments to suppress Fusarium wilt disease.","PeriodicalId":15032,"journal":{"name":"Journal of Applied Biology and Biotechnology","volume":"1 1","pages":""},"PeriodicalIF":0.0,"publicationDate":"2022-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"71218025","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}
Pub Date : 2022-01-01DOI: 10.7324/jabb.2021.100126
Krishnan V. Gokula, D. J, Rao Pinagadi Venkateswara, D. V., K. S.
V. Gokula Krishnan1*, J. Deepa2, Pinagadi Venkateswara Rao3, V. Divya4, S. Kaviarasan5 1Associate Professor, CSIT Department, CVR College of Engineering, Hyderabad, India. 2Assistant Professor, CSE Department, Easwari Engineering College, Chennai,India. 3Associate Professor, CSE Department, ACE Engineering College, Hyderabad, India. 4Assistant Professor, EEE Department, CVR College of Engineering, Hyderabad, India. 5Assistant Professor, CSE Department, Panimalar Institute of Technology, Chennai, India.
V. Gokula Krishnan1*， J. deep2, Pinagadi Venkateswara Rao3, V. Divya4, S. Kaviarasan5 1印度海得拉巴CVR工程学院CSIT系副教授。2印度金奈Easwari工程学院CSE系助理教授。3印度海得拉巴ACE工程学院CSE系副教授。4印度海得拉巴CVR工程学院EEE系助理教授。5印度金奈Panimalar理工学院CSE系助理教授。
{"title":"An automated segmentation and classification model for banana leaf disease detection","authors":"Krishnan V. Gokula, D. J, Rao Pinagadi Venkateswara, D. V., K. S.","doi":"10.7324/jabb.2021.100126","DOIUrl":"https://doi.org/10.7324/jabb.2021.100126","url":null,"abstract":"V. Gokula Krishnan1*, J. Deepa2, Pinagadi Venkateswara Rao3, V. Divya4, S. Kaviarasan5 1Associate Professor, CSIT Department, CVR College of Engineering, Hyderabad, India. 2Assistant Professor, CSE Department, Easwari Engineering College, Chennai,India. 3Associate Professor, CSE Department, ACE Engineering College, Hyderabad, India. 4Assistant Professor, EEE Department, CVR College of Engineering, Hyderabad, India. 5Assistant Professor, CSE Department, Panimalar Institute of Technology, Chennai, India.","PeriodicalId":15032,"journal":{"name":"Journal of Applied Biology and Biotechnology","volume":"1 1","pages":""},"PeriodicalIF":0.0,"publicationDate":"2022-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"71218345","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}
Although widely known for its antioxidant properties, piperine’s (a compound from the pepper plant) physiologic involvement in apoptosis (programmed cell death) is unclear. As a prerequisite to unravel its role in this process, computational approaches simulating ligand–receptor docking are sought. Herein, we report the simulated binding of piperine with major apoptotic proteins via combined deployment of AutoDock suite (AutoDock Vina), PyMOL, and LigPlot + software. Our results demonstrated varied binding affinity toward the different apoptosis-associated proteins with a higher to lower affinity pattern in the order of TNFR-1 > Caspase-3 > TNF-α > Caspase-8 > Bcl-2 > Caspase-9 > Bax. Docking scores for all receptor–ligand interactions indicate a strong likelihood of impromptu receptor–ligand binding. Molecularly, the simulated analysis revealed hydrophobic interactions in all receptor–ligand models studied. Receptor–piperine complexes involving TNFR-1 and Caspase-8 showed single hydrogen bonding whereas amino acid residues of TNF-α exhibited double hydrogen bonding to piperine. In the TNFR-1-piperine complex (receptor–ligand docked model with strongest binding affinity) the hydrophobic interaction involves amino acid residues of SER74, LYS75, ASN110 (2), THR94, CYS96, VAL95, and PHE112. Our findings provide novel in silico evidence of piperine’s binding affinity toward apoptosis-associated proteins and the high likelihood of its influence on apoptosis reaction via the extrinsic pathway.
{"title":"Computational ligand–receptor docking simulation of piperine with apoptosis-associated factors","authors":"Vong Adrianne Dien-Yu, Hwang Siaw-San, Chee Xavier Wezen, Sim Edmund Ui-Hang","doi":"10.7324/jabb.2021.100105","DOIUrl":"https://doi.org/10.7324/jabb.2021.100105","url":null,"abstract":"Although widely known for its antioxidant properties, piperine’s (a compound from the pepper plant) physiologic involvement in apoptosis (programmed cell death) is unclear. As a prerequisite to unravel its role in this process, computational approaches simulating ligand–receptor docking are sought. Herein, we report the simulated binding of piperine with major apoptotic proteins via combined deployment of AutoDock suite (AutoDock Vina), PyMOL, and LigPlot + software. Our results demonstrated varied binding affinity toward the different apoptosis-associated proteins with a higher to lower affinity pattern in the order of TNFR-1 > Caspase-3 > TNF-α > Caspase-8 > Bcl-2 > Caspase-9 > Bax. Docking scores for all receptor–ligand interactions indicate a strong likelihood of impromptu receptor–ligand binding. Molecularly, the simulated analysis revealed hydrophobic interactions in all receptor–ligand models studied. Receptor–piperine complexes involving TNFR-1 and Caspase-8 showed single hydrogen bonding whereas amino acid residues of TNF-α exhibited double hydrogen bonding to piperine. In the TNFR-1-piperine complex (receptor–ligand docked model with strongest binding affinity) the hydrophobic interaction involves amino acid residues of SER74, LYS75, ASN110 (2), THR94, CYS96, VAL95, and PHE112. Our findings provide novel in silico evidence of piperine’s binding affinity toward apoptosis-associated proteins and the high likelihood of its influence on apoptosis reaction via the extrinsic pathway.","PeriodicalId":15032,"journal":{"name":"Journal of Applied Biology and Biotechnology","volume":"1 1","pages":""},"PeriodicalIF":0.0,"publicationDate":"2022-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"71217090","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}
Pub Date : 2022-01-01DOI: 10.7324/jabb.2021.100107
Giang Nguyen Thi Ngoc, Khai Tran Van, Thuyet Nguyen Minh
Koji is a term that describes the process of molds growing and producing enzymes that hydrolyze complex components in cooked materials into simpler compounds. In this study, the optimal conditions for the production of enzymes (amylase and protease) of koji incubation were determined by using the response surface methodology with the central composite design 22 + star. The experiments were conducted with two factors, including molds addition (X1) (0.02 ÷ 0.04%) and koji-making time (X2) (24 ÷ 36 hours), as well as incubation temperature (X3) (27 ÷ 33°C) and pH of koji (X4) (5.5 ÷ 6.5). The study results showed that the mycelium of Aspergillus oryzae developed a fairly thick layer on the medium at 0.030 ÷ 0.044% of molds addition and 30 ÷ 36 hours with pH 5.89 ÷ 6.12 and temperature 29.76 ÷ 30.24°C. The optimal conditions (molds addition, time, pH, and temperature) were 0.03%, 30 hours, pH 6.0, and 30°C, respectively. In these optimal parameters, amylase and protease activities were 61.35 and 12.27 U/g dry matter, respectively.
{"title":"Optimization of amylase and protease production from oyster mushrooms koji (Pleurotus spp.) using response surface methodology","authors":"Giang Nguyen Thi Ngoc, Khai Tran Van, Thuyet Nguyen Minh","doi":"10.7324/jabb.2021.100107","DOIUrl":"https://doi.org/10.7324/jabb.2021.100107","url":null,"abstract":"Koji is a term that describes the process of molds growing and producing enzymes that hydrolyze complex components in cooked materials into simpler compounds. In this study, the optimal conditions for the production of enzymes (amylase and protease) of koji incubation were determined by using the response surface methodology with the central composite design 22 + star. The experiments were conducted with two factors, including molds addition (X1) (0.02 ÷ 0.04%) and koji-making time (X2) (24 ÷ 36 hours), as well as incubation temperature (X3) (27 ÷ 33°C) and pH of koji (X4) (5.5 ÷ 6.5). The study results showed that the mycelium of Aspergillus oryzae developed a fairly thick layer on the medium at 0.030 ÷ 0.044% of molds addition and 30 ÷ 36 hours with pH 5.89 ÷ 6.12 and temperature 29.76 ÷ 30.24°C. The optimal conditions (molds addition, time, pH, and temperature) were 0.03%, 30 hours, pH 6.0, and 30°C, respectively. In these optimal parameters, amylase and protease activities were 61.35 and 12.27 U/g dry matter, respectively.","PeriodicalId":15032,"journal":{"name":"Journal of Applied Biology and Biotechnology","volume":"1 1","pages":""},"PeriodicalIF":0.0,"publicationDate":"2022-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"71217365","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}
京公网安备 11010802042870号
京ICP备2023020795号-1
扫码关注我们
求助内容：
应助结果提醒方式：