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Culture Conditions and Character of Extracellular Enzyme ACC Deaminase Excreted by Bacterium Strain XG32(PDF)

《南京师大学报（自然科学版）》[ISSN:1001-4616/CN:32-1239/N]

Issue:
2008年01期
Page:
104-108
Research Field:
生命科学
Publishing date:

Info

Title:
Culture Conditions and Character of Extracellular Enzyme ACC Deaminase Excreted by Bacterium Strain XG32
Author(s):
Shen Ping;  Liu Weihong;  Yan Shuzhen;  Chen Shuanglin
School of Life Science, Nanjing Normal University, Nanjing 210046, China
Keywords:
bacter ium;  ACC deam inase;  enzym atic activ ity
PACS:
Q93
DOI:
-
Abstract:
In orde r to investigate optim al cu lture conditions and the charac ter o fACC( 1-am inocy clopropane- 1 carboxy-l ic ac id) deam inase excreted by bac terium stra in XG32, exper im ents were done to de term ine the e ffect on the enzym a tic ac tiv ity under different cond itions, inc luding concentration of inducerACC in cu lture m ed ium, culture tem pera ture and pH, w hile tim e process o f ACC deam inase w as a lso assayed. Then we m easured the activ ity and stability of the enzym e under d ifferent temperatures, pH and m eta ls. The results ind icated tha t the ACC deam inase could be induced on ly when the inducer ex isted and the tem peraturew as abov e 5℃ , and pH w as above 5.5. The enzym atic y ield reached the highest when the cu lture temperature w as 25℃ and cu lture pH was 7.0 to 8. 0. The enzym a tic y ie ld constantly increased in 24 hours after inducer was added, and then dec lined. A s for activ ity, the optim al temperatu re of ACC deam inase was 30℃approx im ately. The enzym atic activ ity a lm ost d isappeared w hen it was 65℃ . The enzym e had a preferab le stab ility a t pH 7. 5~ 9. 5. M oreov er, ions Cu 2+ and Zn 2+ cou ld activate the ACC deam inase, w hileH g 2+ and Ag+ cou ld inhib it the enzym e ac tiv ity. In conc lusion, theACC deam inase is sensitive to the substance. Thatm eans a little o f this kind o f enzym e can decom pose ACC in natural env ironm ent. How ever, the enzym e is sensitive to the circumstance, and its stab ility is on ly a t a certa in ex tens ion.

References:

[ 1] G lick B R, Karaturov ic D M, New ell P C. A nove l procedure fo r rapid isolation of plant grow th-prom oting pseudom onads[ J] . C an JM icrob io ,l 1995, 41( 2): 533-536.
[ 2] M aW, Penrose D M, G lick B R. Strateg ies used by rhizobia to low er p lant ethy lene leve ls and inc rease nodu lation[ J]. Can JM icrobio,l 2002, 48( 11): 947-954.
[ 3] Glick B R, Jacobson C B, Schw arzeM K, e t a.l 1-Am ino cyc lopropane-1- carboxy lic ac id deam inase m utants of the p lant grow th prom oting rh izobacte rium P seudom onas putida GR12- 2 do no t stim ulate cano la root e long ation [ J]. Can JM icrob io,l1994, 40: 911-915.
[ 4] 刘维红, 闫淑珍, 杨启银, 等. ACC 脱氨酶活性细菌筛选及其对番茄初生苗生长的影响[ J]. 江苏农业科学, 2006,2( 6): 80-84.
[ 5] H onm aM, Sh im om ura T. M etabolism of 1-am inocyc lopropance-1-carboxy lic acid[ J]. Agr ic B io l Chem, 1978, 42( 10): 1 825-1 831.
[ 6] Sa leh S S, G lick B R. Invo lvem ent of gacs and rpos in enhancem ent o f the plan t g row th-prom oting capab ies Enterobacter cloacae CAL2 and UW 4 [ J]. Can JM icrobio ,l 2001, 47: 698-705.
[ 7] Jacobson C B, Pasternak J J, G lick B R. Partia l pur ification and charac terization of the enzyme ACC deam inase from the p lant grow th-prom oting rhizobacterium P seudom onas putida GR12- 2[ J]. Can JM icrob io,l 1994, 40( 2) : 1 019-1 025.
[ 8] Penrose D M, G lick B R. M ethods for iso lating and character izing ACC deam inase-conta in- ing plant g row th-prom oting rhizobacte ria[ J] . Phy sio log ia Plantarum, 2003, 118( 1): 10-15.

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Last Update: 2013-05-05