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Novel thermostable enzymes for industrial biotechnology (THERMOGENE)

Novel thermostable enzymes for industrial biotechnology (THERMOGENE)
用于工业生物技术的新型热稳定酶 (THERMOGENE)
批准号:
BB/L002035/1
负责人:
Jennifer Littlechild
金额:
$29.97万
依托单位:
依托单位国家:
英国
项目类别:
Research Grant
财政年份:
2013
资助国家:
英国
项目状态:
已结题
起止时间:
2013 至 --

项目摘要

项目成果

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中文摘要
翻译
对具有增强性能和/或新功能的新型耐热酶的需求不断增加,这些酶可以为高价值化学生产领域的工业过程和许多其他“白色”生物技术应用节省时间、金钱和能源。酶化学可以使目前使用传统化学方法无法实现的反应变得可行。在化学过程中使用酶是降低能源消耗和减少废物产生的途径。此外,酶促过程的选择性降低了原材料成本和围绕浪费的副产品生产的安全问题。优化的酶生产将导致经济上可行、成本效益高、可持续的生产。THERMOGENE将专注于发现具有已知和潜在商业应用的选定转移酶。这些包括能够转移2碳单位的酶,转酮酶;能转移胺基,转氨酶;能够转移异戊烯基或戊烯基,戊烯基转移酶,能够转移甲基和羟甲基,甲基和羟甲基转移酶。酶在绿色化学和生物技术中的应用越来越重要。这在一定程度上是由制药部门在开发新的治疗剂方面所推动的,这些治疗剂需要是光学纯化合物。酶生产的新药中间体的数量预计将在未来几年内显著增加。使用酶的一个缺点是,在工业过程所需的反应条件下,蛋白质往往不稳定。这仍然是酶催化剂商业应用的主要瓶颈。该提案将集中于从海洋和陆地环境中发现新的酶。这将使用新测序的嗜热细菌和古细菌基因组以及从嗜热环境中分离出来的宏基因组。后者将使我们能够从无法在实验室培养的生物体中取样DNA,也可以从病毒中提取遗传物质。从能够在高温下生长的生物体中分离出来的酶在工业过程所需的水基和溶剂基条件下具有更高的稳定性。它还将寻求发现具有新活性的酶,这些酶通常存在于这些生物体中,这些生物体已经进化到细胞膜中具有不同的脂肪和不同的代谢途径。在项目结束时,我们将确定许多新的生物催化剂,可用于取代传统的化学过程并与之协同工作。这将为子孙后代创造一个更绿色、更可持续的环境。
英文摘要
There is an increasing demand for new thermostable enzymes with enhanced performance and/or novel functionalities that could provide savings in time, money and energy for industrial processes in the areas of high value chemical production and many other "white" biotechnology applications.Enzyme chemistry can make reactions feasible that are currently unavailable using conventional chemical methods. Use of enzymes for chemical processes is a route to lower energy consumption and reduced waste generation. In addition the selectivity of enzymatic processes reduces raw material costs and the safety issues surrounding the production of wasteful bi-products. Optimised enzyme production will lead to economically viable and cost effective, sustainable production.THERMOGENE will focus on the discovery of selected transferase enzymes with known and potential commercial applications. These include enzymes able to transfer 2-carbon units, transketolases; able to transfer amine groups, transaminases; able to transfer isoprenyl or prenyl groups, prenyltransferases and able to transfer methyl and hydroxymethyl groups, methyl and hydroxymethyl transferases. The use of enzymes in green chemistry and biotechnology is increasingly important. This is partially driven by the pharmaceutical sector in the development of new therapeutic agents that are required to be optically pure compounds. The number of new drug intermediates produced by enzymes is expected to rise significantly in the next few years.One disadvantage of using enzymes is that proteins are often not stable during the reaction conditions required for the industrial process. This is still a major bottleneck in the commercial use of enzyme catalysts.This proposal will concentrate on discovery of novel enzymes from marine and terrestrial environments. This will use newly sequenced genomes of thermophilic bacteria and archaea and metagenomes isolated from thermophilic environments. The latter will allow us to sample the DNA from organisms not able to be cultured in the laboratory and also the genetic material from viruses. The enzymes isolated from organisms able to grow at high temperatures will have higher stability in water based and solvent based conditions which are required for the industrial processes. It will also seek to discover enzymes with new and novel activities which are often found in these organisms that have evolved to have different fats in their cell membrane and different pathways in their metabolism.At the end of the project we will identify many new biological catalysts that can be used to replace and work together with traditional chemical processes. This will lead to a greener and more sustainable environment for future generations.
期刊论文(10)
专著(0)
科研奖励(0)
会议论文
The oxygenating constituent of 3,6-diketocamphane monooxygenase from the CAM plasmid of Pseudomonas putida : the first crystal structure of a type II Baeyer-Villiger monooxygenase. Corrigendum
来自恶臭假单胞菌 CAM 质粒的 3,6-二酮莰烷单加氧酶的氧化成分:II 型 Baeyer-Villiger 单加氧酶的第一个晶体结构。
DOI: 10.1107/s205979831800150x
发表时间: 2018
期刊: Acta Crystallographica Section D Structural Biology
影响因子: --
作者: [Isupov M]
通讯作者: Isupov M
DOI: 10.3389/fmicb.2020.592353
发表时间: 2020
期刊: Frontiers in microbiology
影响因子: 5.2
作者: [James P, Isupov MN, De Rose SA, Sayer C, Cole IS, Littlechild JA]
通讯作者: Littlechild JA
Preface to Special Issue on Biocatalysis as Key to Sustainable Industrial Chemistry.
生物催化作为可持续工业化学关键的特刊序言。
DOI: 10.1002/cssc.202200640
发表时间: 2022
期刊: ChemSusChem
影响因子: 8.4
作者: [Alcántara AR]
通讯作者: Alcántara AR
17-ERACoBioTech Thermophilic bacteria and archaeal chassis for extremolyte production -HotSolute
  • 批准号:
    BB/R02166X/1
  • 项目类别:
    Research Grant
  • 资助金额:
    $52.5万
  • 财政年份:
    2018
  • 负责人:
    Jennifer Littlechild
  • 依托单位:
Novel enzyme diversity for improving cleaning and hygiene
  • 批准号:
    BB/N023838/1
  • 项目类别:
    Research Grant
  • 资助金额:
    $12.72万
  • 财政年份:
    2016
  • 负责人:
    Jennifer Littlechild
  • 依托单位:
海外基金