TY - JOUR
T1 - Directed breeding of an Arthrobacter mutant for high-yield production of cyclic adenosine monophosphate by N+ ion implantation
AU - Song, He
AU - Chen, Xiaochun
AU - Cao, Jiaming
AU - Fang, Ting
AU - Bai, Jianxin
AU - Xiong, Jian
AU - Ying, Hanjie
PY - 2010/8
Y1 - 2010/8
N2 - To obtain a cyclic adenosine monophosphate (cAMP) high-yield production strain, Arthrobacter NG-1 was mutated by N+ ion implantation with an energy level of 10keV and dose of 7×1015ions/cm2. Combined with directed screening methods, a xanthine-defective and 8-azaguanine (8-AG)-resistant mutant Arthrobacter A302 was selected. The concentration of cAMP produced by this mutant was 41.7% higher than that of the original strain and reached 9.78g/L. Through ten-generation investigation, the capability of cAMP production of A302 was found to be stable. Compared with the original strain, the special activities of key enzymes in A302, which influenced the cAMP biosynthesis, was analyzed. IMP dehydrogenase activity was defective, whereas PRPP amidotransferase, sAMP synthetase and adenylate cyclase activities were increased by 61.5%, 147% and 21.7%, respecitively, which might explain the mutagenesis mechanism by N+ ions implantation under the enzymatic level.
AB - To obtain a cyclic adenosine monophosphate (cAMP) high-yield production strain, Arthrobacter NG-1 was mutated by N+ ion implantation with an energy level of 10keV and dose of 7×1015ions/cm2. Combined with directed screening methods, a xanthine-defective and 8-azaguanine (8-AG)-resistant mutant Arthrobacter A302 was selected. The concentration of cAMP produced by this mutant was 41.7% higher than that of the original strain and reached 9.78g/L. Through ten-generation investigation, the capability of cAMP production of A302 was found to be stable. Compared with the original strain, the special activities of key enzymes in A302, which influenced the cAMP biosynthesis, was analyzed. IMP dehydrogenase activity was defective, whereas PRPP amidotransferase, sAMP synthetase and adenylate cyclase activities were increased by 61.5%, 147% and 21.7%, respecitively, which might explain the mutagenesis mechanism by N+ ions implantation under the enzymatic level.
KW - Arthrobacter A302
KW - Cyclic adenosine monophosphate
KW - Enzymatic analysis
KW - Mutation breeding
KW - N ion implantation
UR - http://www.scopus.com/inward/record.url?scp=77952673854&partnerID=8YFLogxK
U2 - 10.1016/j.radphyschem.2010.03.005
DO - 10.1016/j.radphyschem.2010.03.005
M3 - 文章
AN - SCOPUS:77952673854
SN - 0969-806X
VL - 79
SP - 826
EP - 830
JO - Radiation Physics and Chemistry
JF - Radiation Physics and Chemistry
IS - 8
ER -