Renaturation of Lysozyme with a Protein Disulfide Isomerase Chaperone Results in Enzyme Super Activity

被引：2
|
作者：
Takezawa, Aya [1 ]
Ohshima, Yuji [1 ]
Sudo, Tomoya [1 ]
Asami, Osamu [2 ]
Nohara, Daisuke [1 ]
机构：
[1] Gifu Univ, Fac Engn, Dept Biomol Sci, Gifu 5011193, Japan
[2] Toyota Cent Res & Dev Labs Inc, Aichi 4801192, Japan
来源：
JOURNAL OF BIOSCIENCE AND BIOENGINEERING | 2008年 / 106卷 / 05期
关键词：
chaperoned lysozyme; lysozyme refolding; protein disulfide isomerase; super activity;
D O I：
10.1263/jbb.106.503
中图分类号：
Q81 [生物工程学（生物技术）]; Q93 [微生物学];
学科分类号：
071005 ; 0836 ; 090102 ; 100705 ;
摘要：
When the oxidative refolding of lysozyme (Lyzm) was carried out in the presence of protein disulfide isomerase (PDI) an increased refolding rate and a recovered activity exceeding 100% were reproducibly observed. The origin of this excess activity was investigated by HPLC, SDS-PAGE, and mass spectrometry and assessed using an assay for Lyzm activity. The refolding of Lyzm was achieved through the formation of PDI-Lyzm intermediates and the excess activity was derived from the nascent lysozyme released from these complexes. The released lysozyme exhibited a higher molecular activity than observed for the native protein.
引用
收藏
页码：503 / 506
页数：4
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