期刊
BIOSCIENCE BIOTECHNOLOGY AND BIOCHEMISTRY
卷 74, 期 4, 页码 727-735出版社
TAYLOR & FRANCIS LTD
DOI: 10.1271/bbb.90773
关键词
acid phosphatase; recombinant phosphatase; Thermus thermophilus
类别
资金
- National Science Council of Taiwan [NSC96-2313-B-006-003-MY3]
A recombinant putative acid phosphatase from Thermus thermophilus was expressed and purified from Escherichia coli. The recombinant phosphatase displayed activities in a broad range of temperature, from 40 to 90 degrees C, with optimal temperature at 70 degrees C. In addition, the recombinant enzyme had activities in a wide range of pH, from 3.6 to 9.1, with optimal pH at 6 in acetate butler and with optimal pH at 6.5 in Hepes butler. Furthermore, it showed significant thermal stability and still possessed 44% residual activity after 70 degrees C treatment for 15 min. Moreover, the recombinant phosphatase showed broad substrates specificities for monophosphate esters, p-nitrophenyl phosphate (pNPP) being the most preferred substrate, and it was able to resist inhibition by sodium tartrate. Additionally, the recombinant protein formed stable oligomer under partially denatured conditions and required calcium ions for enzymic activity.
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