Full metadata record
DC Field | Value | Language |
---|---|---|
dc.contributor.author | 정병문 | * |
dc.contributor.author | 김진흥 | * |
dc.date.accessioned | 2016-08-28T12:08:20Z | - |
dc.date.available | 2016-08-28T12:08:20Z | - |
dc.date.issued | 2009 | * |
dc.identifier.issn | 0141-0229 | * |
dc.identifier.other | OAK-5896 | * |
dc.identifier.uri | https://dspace.ewha.ac.kr/handle/2015.oak/220242 | - |
dc.description.abstract | Fructose-1,6-bisphosphate (FBP) aldolase, is a glycolytic enzyme that catalyzes the reversible condensation reaction of FBP to dihydroxyacetone phosphate (DHAP) and glyceraldehyde-3-phosphate (G3P). The aldolase gene from Aquifex aeolicus was subcloned, overexpressed in E. coli and purified to 95% homogeneity. The purified enzyme was activated by high concentrations of NH4+ and low concentrations of Co2+. The native molecular weight of the purified FBP aldolase was identified as 67 kDa (dimer) by gel filtration chromatography. The enzyme exhibits optimum pH at 6.5 and temperature at 90 °C. Based on the kinetic characterizations, the apparent Km was calculated to be 4.4 ± 0.07 mM, while Vmax was found to be 100 ± 0.02 μM min-1 mg protein-1. The recombinant protein showed extreme heat stability; no activity loss was observed even at 100 °C for 2 h. In addition, the thermophilic enzyme also showed higher stability against several organic solvents viz. acetonitrile, 1,4-dioxane, and methanol. With higher stability against both heat and organic solvents than any other class II aldolase, the A. aeolicus FBP aldolase is an attractive enzyme for use as a biocatalyst for industrial applications. © 2009 Elsevier Inc. All rights reserved. | * |
dc.language | English | * |
dc.title | Characterization of a extreme thermostable fructose-1,6-bisphosphate aldolase from hyperthermophilic bacterium Aquifex aeolicus | * |
dc.type | Article | * |
dc.relation.issue | 4 | * |
dc.relation.volume | 45 | * |
dc.relation.index | SCI | * |
dc.relation.index | SCIE | * |
dc.relation.index | SCOPUS | * |
dc.relation.startpage | 261 | * |
dc.relation.lastpage | 266 | * |
dc.relation.journaltitle | Enzyme and Microbial Technology | * |
dc.identifier.doi | 10.1016/j.enzmictec.2009.06.012 | * |
dc.identifier.wosid | WOS:000270016100004 | * |
dc.identifier.scopusid | 2-s2.0-68349157652 | * |
dc.author.google | La I.-J. | * |
dc.author.google | Eum D.-Y. | * |
dc.author.google | Gedi V. | * |
dc.author.google | Kim J. | * |
dc.author.google | Jeong B. | * |
dc.author.google | Yoon M.-Y. | * |
dc.contributor.scopusid | 정병문(7102237959) | * |
dc.contributor.scopusid | 김진흥(8580015800) | * |
dc.date.modifydate | 20240118155902 | * |