Lipases obtained from healthy and pebrinised larvae were purified by 45-85% (NH4) 2SO 4 fractionation followed by Sephadex S-100 gel filtration and CM-Sepharose. In both the samples final enzyme purification reported was 19.02 and 17.7 folds(magnitude) and the recovery of final purified enzyme was 19.32% and 17.14% with a specific activity of 7.87 and 7.52 µmol/min/mg. Results also show that activity of purified lipase was highest at pH 8 in both the samples. Highest lipase activity was recorded between 37°C to 40°C tem perature and lipase activity was maximum at 37°C temperature in healthy sample and 38°C tempe rature in pebrinised sample. The enzyme activity reduced with addition of NaCl, Urea and MgCl 2 whereas EDTA and CaCl 2 increased the activity. The molecular weight of the purified enzyme was 30 kDa as determined by SDSpolyacrylamide gel electrophoresis. Aim: The present study was conducted to isolate, purify and characterize lipases from the midgut of both healthy and pebrinised fifth instar larvae of Antheraea mylitta drury . Study Design: Study involves dissection of midgut from the fifth instar larvae of fourth day of both healthy and pebrinised larvae, Lipases obtained from both the samples were purified by 45-85%
{"title":"Isolation and Purification of Lipase from the Midgut of Fifth Instar Larvae of Antheraea mylitta drury","authors":"Lakshmi Marepally, G. Benarjee","doi":"10.9734/BBJ/2016/24442","DOIUrl":"https://doi.org/10.9734/BBJ/2016/24442","url":null,"abstract":"Lipases obtained from healthy and pebrinised larvae were purified by 45-85% (NH4) 2SO 4 fractionation followed by Sephadex S-100 gel filtration and CM-Sepharose. In both the samples final enzyme purification reported was 19.02 and 17.7 folds(magnitude) and the recovery of final purified enzyme was 19.32% and 17.14% with a specific activity of 7.87 and 7.52 µmol/min/mg. Results also show that activity of purified lipase was highest at pH 8 in both the samples. Highest lipase activity was recorded between 37°C to 40°C tem perature and lipase activity was maximum at 37°C temperature in healthy sample and 38°C tempe rature in pebrinised sample. The enzyme activity reduced with addition of NaCl, Urea and MgCl 2 whereas EDTA and CaCl 2 increased the activity. The molecular weight of the purified enzyme was 30 kDa as determined by SDSpolyacrylamide gel electrophoresis. Aim: The present study was conducted to isolate, purify and characterize lipases from the midgut of both healthy and pebrinised fifth instar larvae of Antheraea mylitta drury . Study Design: Study involves dissection of midgut from the fifth instar larvae of fourth day of both healthy and pebrinised larvae, Lipases obtained from both the samples were purified by 45-85%","PeriodicalId":90120,"journal":{"name":"British biotechnology journal","volume":"12 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":"71164951","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":"Antioxidant Property and Phenolic Content of Anthocleista vogelii Root Ethanolic Extract and Fractions","authors":"R. Sunday, O. Ilesanmi, E. Obuotor","doi":"10.9734/BBJ/2016/27016","DOIUrl":"https://doi.org/10.9734/BBJ/2016/27016","url":null,"abstract":"","PeriodicalId":90120,"journal":{"name":"British biotechnology journal","volume":"14 1","pages":"1-8"},"PeriodicalIF":0.0,"publicationDate":"2016-01-10","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"71165359","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":"Evaluation of Virulence of Tanzanian Strains of Fowlpox and Pigeonpox Viruses in Chickens","authors":"S. Masola, A. Mzula, C. Kasanga, P. Wambura","doi":"10.9734/bbj/2016/20150","DOIUrl":"https://doi.org/10.9734/bbj/2016/20150","url":null,"abstract":"","PeriodicalId":90120,"journal":{"name":"British biotechnology journal","volume":"10 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":"71163614","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}
Kishor Kumar Sarker, F. Monshi, Sayeda Sultana, Delara Akhter, M. Bhuiyan
{"title":"Development of an Efficient Plant Regeneration System of Field Mustard (Brassica campestris)","authors":"Kishor Kumar Sarker, F. Monshi, Sayeda Sultana, Delara Akhter, M. Bhuiyan","doi":"10.9734/bbj/2016/21529","DOIUrl":"https://doi.org/10.9734/bbj/2016/21529","url":null,"abstract":"","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":"71163823","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":"Biovalorization of Olive Mill Waste Water for the Production of Single Cell Protein from Saccharomyces cerevisiae, Candida utilis and Pleurotus ostreatus","authors":"I. Giavasis, K. Petrotos","doi":"10.9734/bbj/2016/22509","DOIUrl":"https://doi.org/10.9734/bbj/2016/22509","url":null,"abstract":"","PeriodicalId":90120,"journal":{"name":"British biotechnology journal","volume":"11 1","pages":"1-16"},"PeriodicalIF":0.0,"publicationDate":"2016-01-10","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"71164173","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}
F. Orji, E. N. Dike, A. Lawal, A. Sadiq, F. Fashola, Y. Suberu, A. Famotemi, B. Ita, A. Ugbana, A. Adefiranye, E. Itoandon, G. Elemo
{"title":"Properties of Aspergillus flavus Cellulase Produced from Solid State Fermentation of Brewers’ Spent Grain (BSG) as Substrate","authors":"F. Orji, E. N. Dike, A. Lawal, A. Sadiq, F. Fashola, Y. Suberu, A. Famotemi, B. Ita, A. Ugbana, A. Adefiranye, E. Itoandon, G. Elemo","doi":"10.9734/BBJ/2016/24882","DOIUrl":"https://doi.org/10.9734/BBJ/2016/24882","url":null,"abstract":"","PeriodicalId":90120,"journal":{"name":"British biotechnology journal","volume":"13 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":"71164542","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. Dubey, S. Yadav, Manish Kumar, Gautam Anand, Dinesh Yadav
Pectate lyase represents an important member of pectinase group of enzymes responsible for the pathogenesis and softening of plant tissues. It also has role in fruit juice clarification and in retting of natural fibers. The biochemical characterization of pectate lyases from diverse microbial sources and plants along with an insight to the protein structure has been dealt earlier but there is a lack of exclusive review on the molecular biology of pectate lyases. This review tries to fill the gap by highlighting the various aspects of molecular biology of microbial pectate lyases especially the cloning and expression of pectate lyase genes from diverse sources attempted so far. The topics covered in this review are a brief description about enzymes associated with degradation of pectin, its classification, applications, updated information about the biochemical characterization of microbial pectate lyases and cloning and expression of microbial pectate lyase genes.
{"title":"Molecular Biology of Microbial Pectate Lyase: A Review","authors":"A. Dubey, S. Yadav, Manish Kumar, Gautam Anand, Dinesh Yadav","doi":"10.9734/BBJ/2016/24893","DOIUrl":"https://doi.org/10.9734/BBJ/2016/24893","url":null,"abstract":"Pectate lyase represents an important member of pectinase group of enzymes responsible for the pathogenesis and softening of plant tissues. It also has role in fruit juice clarification and in retting of natural fibers. The biochemical characterization of pectate lyases from diverse microbial sources and plants along with an insight to the protein structure has been dealt earlier but there is a lack of exclusive review on the molecular biology of pectate lyases. This review tries to fill the gap by highlighting the various aspects of molecular biology of microbial pectate lyases especially the cloning and expression of pectate lyase genes from diverse sources attempted so far. The topics covered in this review are a brief description about enzymes associated with degradation of pectin, its classification, applications, updated information about the biochemical characterization of microbial pectate lyases and cloning and expression of microbial pectate lyase genes.","PeriodicalId":90120,"journal":{"name":"British biotechnology journal","volume":"13 1","pages":"1-26"},"PeriodicalIF":0.0,"publicationDate":"2016-01-10","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"71164575","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":"Isolation of a Major Antimicrobial Compound from Stem Bark of Glossonema boveanum (Decne)","authors":"M. Sallau, A. Uttu, H. Ibrahim, A. Idris, H. Dama","doi":"10.9734/bbj/2016/24436","DOIUrl":"https://doi.org/10.9734/bbj/2016/24436","url":null,"abstract":"","PeriodicalId":90120,"journal":{"name":"British biotechnology journal","volume":"16 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":"71164828","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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