http://chineseinput.net/에서 pinyin(병음)방식으로 중국어를 변환할 수 있습니다.
변환된 중국어를 복사하여 사용하시면 됩니다.
Mingchang Li,Shuyi Guo,Xiaomin Li,Quan Wang,Lin Zhu,Chunyan Yin,Wei Wang 한국생물공학회 2017 Biotechnology and Bioprocess Engineering Vol.22 No.6
Thermophilic or hyperthermophilic SODs (superoxide dismutase) usually offer substantial biotechnological advantages over mesophilic SODs. Previously a 244-amino acid N-terminal domain (NTD) from a heatresistant SOD of Geobacillus thermodenitrificans NG80-2 was discovered and demonstrated to be able to confer thermostability to homologous mesophilic SODs, which revealed a new type of heat resistance mechanism. To further improve the heat resistance and stress tolerance of thermophilic cambialistic superoxide dismutase (Fe/Mn- SODAp) from Aeropyrum pernix K1 through metal incorporation and fusion with the newly found peptide NTD for broadening its industrial application, the wildtype SODAp and NTD-fused ntdSODAp were expressed in E. coli BL21 and incorporated with metal cofactors by two ways. Recombinant fusion SOD obtained by in vitro reconstitution (Mn-rec ntdSODAp) exhibited improved optimum temperature at 70oC and dramatically enhanced thermostability especially at 110oC with enhanced pH stability from 4 to 10 and higher tolerance for denaturants and organic media than Mn-rec SODAp. To the best of our knowledge, Mn-rec ntdSODAp could be the most heat resistant SOD. In addition, metal incorporation of SODAp and ntdSODAp via in vivo modification have been developed and proved to be more practical for industrial use. These results indicate that fusion with NTD along with metal incorporation can generate superimposed effect and be applied to enhance the stability of cambialistic thermophilic SODs, thus providing a universal and convenient bioengineering method for generating extremely stable SODs.