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A thermostable bacterial lytic polysaccharide monooxygenase with high operational stability in a wide temperature range
Biotechnology for Biofuels ( IF 6.3 ) Pub Date : 2020-11-30 , DOI: 10.1186/s13068-020-01834-5
Tina Rise Tuveng , Marianne Slang Jensen , Lasse Fredriksen , Gustav Vaaje-Kolstad , Vincent G. H. Eijsink , Zarah Forsberg

Lytic polysaccharide monooxygenases (LPMOs) are oxidative, copper-dependent enzymes that function as powerful tools in the turnover of various biomasses, including lignocellulosic plant biomass. While LPMOs are considered to be of great importance for biorefineries, little is known about industrial relevant properties such as the ability to operate at high temperatures. Here, we describe a thermostable, cellulose-active LPMO from a high-temperature compost metagenome (called mgLPMO10). MgLPMO10 was found to have the highest apparent melting temperature (83 °C) reported for an LPMO to date, and is catalytically active up to temperatures of at least 80 °C. Generally, mgLPMO10 showed good activity and operational stability over a wide temperature range. The LPMO boosted cellulose saccharification by recombinantly produced GH48 and GH6 cellobiohydrolases derived from the same metagenome, albeit to a minor extent. Cellulose saccharification studies with a commercial cellulase cocktail (Celluclast®) showed that the performance of this thermostable bacterial LPMO is comparable with that of a frequently utilized fungal LPMO from Thermoascus aurantiacus (TaLPMO9A). The high activity and operational stability of mgLPMO10 are of both fundamental and applied interest. The ability of mgLPMO10 to perform oxidative cleavage of cellulose at 80 °C and the clear synergy with Celluclast® make this enzyme an interesting candidate in the development of thermostable enzyme cocktails for use in lignocellulosic biorefineries.

中文翻译:

在宽温度范围内具有高操作稳定性的热稳定细菌裂解多糖单加氧酶

溶菌多糖单加氧酶(LPMO)是氧化性的铜依赖性酶,在各种生物质(包括木质纤维素植物生物质)的周转中充当强大的工具。尽管认为LPMO对生物精炼厂非常重要,但对工业相关性能(如在高温下运行的能力)知之甚少。在这里,我们描述了来自高温堆肥元基因组(称为mgLPMO10)的热稳定,具有纤维素活性的LPMO。迄今为止,发现MgLPMO10具有最高的表观熔融温度(83°C),并且在至少80°C的温度下具有催化活性。通常,mgLPMO10在较宽的温度范围内显示出良好的活性和操作稳定性。LPMO通过重组生产的来源于同一基因组的GH48和GH6纤维二糖水解酶促进了纤维素的糖化作用,尽管程度很小。用市售纤维素酶混合物(Celluclast®)进行的纤维素糖化研究表明,这种热稳定细菌LPMO的性能可与奥氏嗜热曲霉(TaLPMO9A)经常使用的真菌LPMO媲美。mgLPMO10的高活性和操作稳定性是基础性的和应用性的。mgLPMO10能够在80°C的温度下进行纤维素的氧化裂解,并具有与Celluclast®明显的协同作用,使得该酶成为开发用于木质纤维素生物炼制厂的热稳定酶混合物的有趣候选者。用市售纤维素酶混合物(Celluclast®)进行的纤维素糖化研究表明,这种热稳定细菌LPMO的性能可与奥氏嗜热曲霉(TaLPMO9A)经常使用的真菌LPMO媲美。mgLPMO10的高活性和操作稳定性是基础性的和应用性的。mgLPMO10能够在80°C的温度下进行纤维素的氧化裂解,并具有与Celluclast®的明显协同作用,使该酶成为开发用于木质纤维素生物炼制厂的热稳定酶混合物的有趣候选者。用市售纤维素酶混合物(Celluclast®)进行的纤维素糖化研究表明,这种热稳定细菌LPMO的性能可与奥氏嗜热曲霉(TaLPMO9A)经常使用的真菌LPMO媲美。mgLPMO10的高活性和操作稳定性是基础性的和应用性的。mgLPMO10能够在80°C的温度下进行纤维素的氧化裂解,并具有与Celluclast®明显的协同作用,使得该酶成为开发用于木质纤维素生物炼制厂的热稳定酶混合物的有趣候选者。mgLPMO10的高活性和操作稳定性是基础性的和应用性的。mgLPMO10能够在80°C的温度下进行纤维素的氧化裂解,并具有与Celluclast®的明显协同作用,使该酶成为开发用于木质纤维素生物炼制厂的热稳定酶混合物的有趣候选者。mgLPMO10的高活性和操作稳定性是基础性的和应用性的。mgLPMO10能够在80°C的温度下进行纤维素的氧化裂解,并具有与Celluclast®的明显协同作用,使该酶成为开发用于木质纤维素生物炼制厂的热稳定酶混合物的有趣候选者。
更新日期:2020-12-01
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