Anionic peroxidase production by Arnebia euchroma callus

作者: Sahar Farhadi , Kamahldin Haghbeen , Mohammad-Javad Marefatjo , Marjan Ghiyami Hoor , Hossein Shahbani Zahiri

DOI: 10.1002/BAB.42

关键词: PeroxidaseChemistryIsoelectric focusingKinetinBiochemistrySugarDoubling timeCell cultureCallusHorseradish peroxidase

摘要: Arnebia euchroma callus, obtained from the root cell culture of an Iranian native specimen, has gained a doubling time 63 H after regular subculturing on Linsmaier-Skoog (LS) medium containing sugar (50 g/L), 2,4-dichlorophenoxyacetic acid (10(-6) M), and kinetin (10(-5) M) under darkness at 25°C. Despite observed somaclonal variations, peroxidase production by A. calli been stable over 4 years aforementioned conditions. Isoelectric focusing experiments revealed that partially purified peroxidases (AePoxs) are mainly anionic with pI values about 5.5 6.6. AePox reaches its optimal activity 55°C pH 7.5. Results various kinetic studies suggest belongs to type III plant no for oxidation 3-indoleacetic acid, but seems play role in lignin biosynthesis H(2) O(2) regulation during proliferation cells LS medium. Comparing biochemical properties horseradish view ease solid culture, callus could be considered as source some biotechnological applications.

参考文章(32)
V. Bouque, F. Bourgaud, C. Nguyen, A. Guckert, Production of daidzein by callus cultures of Psoralea species and comparison with plants Plant Cell Tissue and Organ Culture. ,vol. 53, pp. 35- 40 ,(1998) , 10.1023/A:1006057211490
Y. Maeda, Y. Fujita, Y. Yamada, Callus formation from protoplasts of cultured Lithospermum erythrorhizon cells Plant Cell Reports. ,vol. 2, pp. 179- 182 ,(1983) , 10.1007/BF00270097
John Ruyack, Michael R. Downing, Judy Su Chang, Earl D. Mitchell, Growth of callus and suspension culture cells from cotton varieties (Gossypium hirsutum L.) resistant and susceptible toxanthomonas malvacearum (E. F. Sm.) dows In Vitro Cellular & Developmental Biology – Plant. ,vol. 15, pp. 368- 373 ,(1979) , 10.1007/BF02616144
Angela Mika, Sabine Lüthje, Properties of guaiacol peroxidase activities isolated from corn root plasma membranes. Plant Physiology. ,vol. 132, pp. 1489- 1498 ,(2003) , 10.1104/PP.103.020396
A. Mahmoudi, K. Nazari, M. Khosraneh, B. Mohajerani, V. Kelay, A.A. Moosavi-Movahedi, Can amino acids protect horseradish peroxidase against its suicide-peroxide substrate? Enzyme and Microbial Technology. ,vol. 43, pp. 329- 335 ,(2008) , 10.1016/J.ENZMICTEC.2008.06.003
Hager Jouili, Houda Bouazizi, Michel Rossignol, Gisèle Borderies, Elisabeth Jamet, Ezzeddine El Ferjani, Partial purification and characterization of a copper-induced anionic peroxidase of sunflower roots. Plant Physiology and Biochemistry. ,vol. 46, pp. 760- 767 ,(2008) , 10.1016/J.PLAPHY.2008.04.006
Vassilios P. Papageorgiou, Andreana N. Assimopoulou, Elias A. Couladouros, David Hepworth, K. C. Nicolaou, The Chemistry and Biology of Alkannin, Shikonin, and Related Naphthazarin Natural Products Angewandte Chemie International Edition. ,vol. 38, pp. 270- 301 ,(1999) , 10.1002/(SICI)1521-3773(19990201)38:3<270::AID-ANIE270>3.0.CO;2-0