Proteomics analysis reveals that HSP70 interacts with estrogen receptor alpha in the nucleus of human breast cancer

N. VarunC, R. Ravikumar
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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.
蛋白质组学分析表明,HSP70在人乳腺癌细胞核中与雌激素受体α相互作用
近年来,生物乙醇的生产受到了广泛的关注,许多国家在基础设施、工艺开发和生产设施方面进行了大量投资。能源危机是发达国家和发展中国家的主要经济制约因素。随着不可再生资源以指数级的速度枯竭,开发成本效益高、环境友好、产量高的替代可再生资源是时间的需要。近年来,随着能源需求的不断增长,利用纤维素酶将木质纤维素植物生物质转化为还原糖以生产生物乙醇的研究日益活跃。内切葡聚糖酶主要负责水解内部糖苷键以减少纤维素链的长度。获得高效、耐热的内切葡聚糖酶已成为国内外研究的目标。因此,寻找耐高温、催化效率高的内切葡聚糖酶的新资源是我们的研究重点。本文重点研究了嗜油热菌(Thermotoga petrophila) RKU-1耐热内源性-1,4β-葡聚糖酶基因的克隆及其在大肠杆菌BL21 CodonPlus菌株中的过表达,以期在木质纤维素生物质的水解和不同的工业应用中具有潜在的应用价值。耐热内切葡聚糖酶可同时直接用于糖化过程,无需生物质预冷过程。纯化后的酶在pH 6.0和95°C条件下对CMC的比活性为530 μ g-1,在温度高达97°C时半衰期(t1/2)为6.6 min,在80°C条件下稳定8小时。重组酶在85℃条件下培养6小时后,将预处理的麦秸和baggase分别糖化至3.32%和3.2%。内切葡聚糖酶的耐热性、抗重金属离子性和高比活性使其成为各种工业应用的潜在和有前途的候选者,如纺织工业(生物制石和生物精加工)、动物饲料生产、啤酒和果汁加工、生物质水解(生物乙醇生产)以及植物油、洗涤剂、纸浆和造纸工业。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
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