Expression and Purification of OsLEA5 c in Escherichia coli and Its Protective Effect on Proteins
HU Tingzhang
CHEN Zaigang
QIN Juan
HUANG Xiaoyun
Abstract：In order to investigate protective effect of OsLEA5c protein on other proteins,OsLEA5c protein was heterologously expressed in Escherichia coli DL21,and purified using HiTrapTM chelating HP column. The purified OsLEA5 c protein was used to study the protective effect of the OsLEA5 c protein on lactate dehydrogenase( LDH) activity under heating,drying,and freeze-thaw stresses. LDH was incubated in PBS buffer at 50 ℃for 10,20,30 min,its activity was decreased to 43. 20%,24. 53% and 17. 55%,respec-tively. However,when OsLEA5c protein was added into LDH solution at a mass ratio of 1∶1 (OsLEA5c∶LDH),enzyme activity remained at 85. 77%,74. 24% and 65. 27%,respectively,after treatment in the same way. After air-drying for 5 h,the residual activity of LDH were 2. 55%—4. 19%; while OsLEA5c was added into LDH solution at mass ratios of 2∶1,5∶1 and 10∶1,its residual activity were 17. 59%, 24. 73% and 36. 39%,respectively. After 5 cycles of freeze-thaw treatments,the activity of residual LDH was decreased to 9. 41%—12. 14%,while OsLEA5c was added to LDH solution at mass ratios of 2∶1, 5∶1 and 10∶1,its residual activity were 28. 09%,69. 44% and 95. 16 %,respectively,after freeze-thaw treatments. Therefore,the result suggested that OsLEA5c protein could protect other protein and decrease damage from heating,drying,and freeze-thaw stresses.
Keywords：late embryogenesis abundant proteinOsLEA5c proteinlactate dehydrogenaseprotein activity
Publication Date：2015-01-01
Online Publishing Date：2026-09-12(First online date of this platform, not the publication date of the document)
Pages：4( 11-14 )