Stabilization of cold-adapted protease MCP-01 promoted by trehalose: prevention of the autolysis.
Protease MCP-01 is similar to other cold-adapted enzymes in that it is a cold-adapted serine protease having high specific activity and low thermostability at low and moderate temperature. Its thermolability and self-autolysis has resulted in difficulties in its purification, preservation and research on its structure and function. The disaccharide trehalose is known to effectively stabilize proteins. Its prevention effect on the autolysis of cold-adapted protease MCP-01 was monitored by capillary electrophoresis. In the absence of trehalose, protease MCP-01 autolyzed rapidly at 35 degrees C. However, when trehalose was added, autolysis was remarkably prevented and the loss of activity reduced. MCP-01 may be a useful model for basic research on the interaction of protein and trehalose.
Pan
Jun
J
State Key Lab of Microbial Technology, Shandong University, Jinan, China.
Chen
Xiu-Lan
XL
Shun
Cai-Yun
CY
He
Hai-Lun
HL
Zhang
Yu-Zhong
YZ
D019075:Electrophoresis, Capillary; D010450:Endopeptidases / Q000737:chemistry / Q000378:metabolism*; D004795:Enzyme Stability; D013696:Temperature; D014199:Trehalose / Q000494:pharmacology*
D014199:Trehalose; D010450:Endopeptidases; C477696:protease MCP-01, Pseudoaltermonas