期刊
INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES
卷 164, 期 -, 页码 1267-1274出版社
ELSEVIER
DOI: 10.1016/j.ijbiomac.2020.07.222
关键词
Thermoprotei archaeon; D-lyxose isomerase; D-mannose; Thermostable; Nickel ion dependent
资金
- National Natural Science Foundation of China [31801583, 31922073]
- Natural Science Foundation of Jiangsu Province [BK20180607]
- Independent Projects for Young Scholars at Jiangnan University [JUSRP11966]
Recently, production of D-mannose becomes a hotspot owing to it exhibiting many physiological functions on people's health and wide applications in food and pharmaceutical field. The use of biological enzymes to production of D-mannose is of particular receiving considerable concerns due to it possessing many merits over chemical synthesis and plant extraction strategies. D-Lyxose isomerase (D-LIase) plays a pivotal role in preparation of D-mannose from D-fructose through isomerization reaction. Thus, a novel putative D-LIase from thermophiles strain Thermoprotei archaeon which was expressed in E. coli BL21(DE3) was first identified and biochemically characterized. The recombinant D-LIase showed an optimal temperature of 80 and 85 degrees C and pH of 6.5. It was highly thermostable at 70 degrees C and 80 degrees C after incubating for 48 h and 33 h, respectively, with retaining over 50% of the initial activity. A lower concentration of Ni2+ (0.5 mM) could greatly increase the activity by 25-fold, which was rare reported in other D-LIases. It was a dimer structure with melting temperature of 88.3 degrees C. Under the optimal conditions, 15.8 g L-1 of D-mannose and 33.8 g L-1 of D-xylulose were produced from 80 g L-1 of D-fructose and D-lyxose, respectively. This work provided a promising candidate sugar isomerase T. archaeon D-LIase for the production of D-mannose and D-xylulose. (C) 2020 Elsevier B.V. All rights reserved.
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