Pub Date : 2016-04-15DOI: 10.4172/0974-276X.C1.083
N. VarunC, R. Ravikumar
P of bioethanol has received much attention in recent years and many countries have made large investments in infrastructure, process development and production facilities. Energy crisis are the leading economic constrains in developed as well as in developing countries. With the exhaustion of non-renewable resources at an exponential rate, the need to develop alternative renewable sources which can be both cost effective, environmental friendly and high in yield is the need of time. Recently, the increasing demand of energy has strongly stimulated the research on conversion of lignocellulosic plant biomass by the action of cellulases enzymes into reducing sugars for the subsequent production of bioethanol. Endoglucanases are mainly responsible for hydrolyzing the internal glycosidic bond to decrease the length of the cellulose chains. Obtaining efficient and Thermostable Endoglucanase has become the goal of much research worldwide. Therefore, our research work was focus to search for new resources of Endoglucanase which was thermostable and with high catalytic efficiency. The article focuses on the thermo-tolerant endo-1,4β-glucanasegene of Thermotoga petrophila RKU-1 was cloned and over-expressed in E. coli strain BL21 CodonPlus for its potential usage for the hydrolysis of lignocellulosic biomass and in different industrial applications. Thermostable endoglucanase can be used simultaneously and directly in the saccharification procedure without a pre-cooling process of biomass. Purified enzyme was optimally active with 530 Umg-1 of specific activity against CMC at pH 6.0 and 95 °C which has exhibited a halflife (t1/2) of 6.6 min even at temperature as high as 97 °C and stable up to 8 hours at 80 °C. The recombinant enzyme saccharified pre-treated wheat straw and baggase to 3.32% and 3.2%, respectively after 6 hours incubation at 85 °C. Its thermostability, resistance to heavy metal ions and high specific activity make endoglucanase a potential and promising candidate for various industrial applications such as in textile industry (Biostoning and Biofinishing) in animal feed production, in processing of beer and fruit juice, in biomass hydrolysis (bioethanol production) and in plant oil, detergent, pulp and paper industry.
{"title":"Proteomics analysis reveals that HSP70 interacts with estrogen receptor alpha in the nucleus of human breast cancer","authors":"N. VarunC, R. Ravikumar","doi":"10.4172/0974-276X.C1.083","DOIUrl":"https://doi.org/10.4172/0974-276X.C1.083","url":null,"abstract":"P of bioethanol has received much attention in recent years and many countries have made large investments in infrastructure, process development and production facilities. Energy crisis are the leading economic constrains in developed as well as in developing countries. With the exhaustion of non-renewable resources at an exponential rate, the need to develop alternative renewable sources which can be both cost effective, environmental friendly and high in yield is the need of time. Recently, the increasing demand of energy has strongly stimulated the research on conversion of lignocellulosic plant biomass by the action of cellulases enzymes into reducing sugars for the subsequent production of bioethanol. Endoglucanases are mainly responsible for hydrolyzing the internal glycosidic bond to decrease the length of the cellulose chains. Obtaining efficient and Thermostable Endoglucanase has become the goal of much research worldwide. Therefore, our research work was focus to search for new resources of Endoglucanase which was thermostable and with high catalytic efficiency. The article focuses on the thermo-tolerant endo-1,4β-glucanasegene of Thermotoga petrophila RKU-1 was cloned and over-expressed in E. coli strain BL21 CodonPlus for its potential usage for the hydrolysis of lignocellulosic biomass and in different industrial applications. Thermostable endoglucanase can be used simultaneously and directly in the saccharification procedure without a pre-cooling process of biomass. Purified enzyme was optimally active with 530 Umg-1 of specific activity against CMC at pH 6.0 and 95 °C which has exhibited a halflife (t1/2) of 6.6 min even at temperature as high as 97 °C and stable up to 8 hours at 80 °C. The recombinant enzyme saccharified pre-treated wheat straw and baggase to 3.32% and 3.2%, respectively after 6 hours incubation at 85 °C. Its thermostability, resistance to heavy metal ions and high specific activity make endoglucanase a potential and promising candidate for various industrial applications such as in textile industry (Biostoning and Biofinishing) in animal feed production, in processing of beer and fruit juice, in biomass hydrolysis (bioethanol production) and in plant oil, detergent, pulp and paper industry.","PeriodicalId":354602,"journal":{"name":"Journal of Proteomics & Bioinformatics","volume":"34 1","pages":"0"},"PeriodicalIF":0.0,"publicationDate":"2016-04-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"128908055","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}
E. Mostovenko, H. C. Scott, O. Klychnikov, H. Dalebout, A. Deelder, Magnus Palmblad
Blood plasma is a highly complex mixture of proteins, metabolites and lipids, and a rich source of potential biomarkers for a range of diseases and conditions. The wide range in protein abundance poses a tremendous challenge for plasma proteomics. However, as a relatively small number of proteins make up most of the total protein pool, the concentration range can be compressed by depletion of abundant proteins, such as albumin. To reduce sample complexity and increase the protein coverage, we have developed a sample preparation method based on semi-selective precipitation with acetonitrile at different pH and built a data analysis pipeline, combining different search strategies. The method we propose is reproducible and easily parallelised (high throughput), and may be well suited to fractionate plasma for label-free quantitative proteomics in large clinical studies. Up to 90% of albumin and other abundant proteins were removed by adding an equal volume of acetonitrile to the samples adjusted to pH 5.
{"title":"Protein Fractionation for Quantitative Plasma Proteomics by Semi-Selective Precipitation","authors":"E. Mostovenko, H. C. Scott, O. Klychnikov, H. Dalebout, A. Deelder, Magnus Palmblad","doi":"10.4172/JPB.1000239","DOIUrl":"https://doi.org/10.4172/JPB.1000239","url":null,"abstract":"Blood plasma is a highly complex mixture of proteins, metabolites and lipids, and a rich source of potential biomarkers for a range of diseases and conditions. The wide range in protein abundance poses a tremendous challenge for plasma proteomics. However, as a relatively small number of proteins make up most of the total protein pool, the concentration range can be compressed by depletion of abundant proteins, such as albumin. To reduce sample complexity and increase the protein coverage, we have developed a sample preparation method based on semi-selective precipitation with acetonitrile at different pH and built a data analysis pipeline, combining different search strategies. The method we propose is reproducible and easily parallelised (high throughput), and may be well suited to fractionate plasma for label-free quantitative proteomics in large clinical studies. Up to 90% of albumin and other abundant proteins were removed by adding an equal volume of acetonitrile to the samples adjusted to pH 5.","PeriodicalId":354602,"journal":{"name":"Journal of Proteomics & Bioinformatics","volume":"59 1","pages":"0"},"PeriodicalIF":0.0,"publicationDate":"2012-09-03","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"132878903","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：