Callus cell culture of Pothomorphe umbellata (L.) under stress condition leads to high content of peroxidase enzyme

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Najeh Maissar Khalil
Miriam Alves Morais Mello
Suzelei de Castro França
Luiz Antonio Andrade de Oliveira
Olga Maria Mascarenhas de Faria Oliveira

Abstract

Pothomorphe umbellata (L.) known on Brazil as Caapeba has a number of popular medicinal
use, and it has been studied in relation to its pharmacological activity. Peroxidase specific activity
(units/mg protein) was evaluated in callus cell culture samples of the P.umbellata, grown in two different
MS medium (media 1 and media 2), submitted to 16 hours photoperiod or kept in darkness. Cell growth
rate curve showed that the best growth indices were observed when media 2 submitted to the photoperi-
od regime was used, followed by the same media kept in darkness (stress condition). The results obtained
also showed that the cell culture grown under stress conditions (darkness) lead to high content of peroxi-
dase enzyme (an increase of 700% was observed). Kinetic constant values of 3.3 mmol.L-1 and 2,8 sec-1
were obtained for k M and v max ,, respectively, using guaiacol as enzyme substrate.

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How to Cite
Khalil, N. M., Mello, M. A. M., França, S. de C., de Oliveira, L. A. A., & Oliveira, O. M. M. de F. (2006). Callus cell culture of Pothomorphe umbellata (L.) under stress condition leads to high content of peroxidase enzyme. Eclética Química, 31(3), 61–65. https://doi.org/10.26850/1678-4618eqj.v31.3.2006.p61-65
Section
Original articles

References

I. Felzenszwalb, J.O.Valsa, A.C.Araujo, R. Alcantara-

Gomes, Braz. J. Med. Biol. Res. 20 (1987) 403.

M. de Ferreira-da-Cruz, Y.L.Adami, E. da Espinola-

Mendes, M.R. Figueiredo, C.T. Daniel-Ribeiro, Exp.

Parasitol. 94 (2000) 243.

S.B.M.Barros, D.S.Teixeira, A.E. Aznar, J.A.J. Moreira,

I.E. Ishii, P.C.D. Freitas, Ciência e Cultura 48 (1996) 114.

C.Z. Amorim, C.A. Flores, B.E. Gomes, A.D. Marques,

S.B. Cordeiro, J. Ethnopharmacol. 24 (1988) 101.

C. Desmarchelier, S. Barros, M. Repetto, L.R. Latorre, M.

Kato, J. Coussio, G. Ciccia, Planta Med. 63 (1997) 561.

B. Deus, M.H. Zenk, Biotechnol.Bioengin. 24 (1982)

P.J. O’Brien, Chem. Biol. Inter. 129 (2000) 113.

I.L. Brunetti, O.M.M. Faria-Oliveira, Rev. Ciênc. Farm.

(1995) 55.

M.A. Duarte-Vazquez, B.E. Garcia-Almendárez, C.

Regalado, J.R. Whitaker, J. Agric. Food Chem. 49 (2001)

J.H. Dawson, Science 240 (1988) 433.

B. Chance, Arch. Biochem. Biophys. 41 (1952) 416.

D. Dolphin, A. Forman, D.C. Borg, J. Fajer, R.H. Felton,

Proc Natl Acad Sci U S A 68 (1971) 614.

C. Capeillere-Blandin, Biochem. J. 336 (1998) 395.

M.S. Moraes, F. Oliveira, B. Mancini, M.K. Akissue, G.

Akissue, Rev. Ciênc. Farm. 9 (1987) 77.

T. Murashige, F. Skoog, Biochem. 8 (1962) 4159.

Y. Yamada, F. Sato, Plant Cell Physiol. 19 (1978) 691.

R.F. Itzhaki, D.M. Gill, Anal Biochem. 9 (1964) 401.

E. Heidrich, G. Lorenz, P. Schreier, Food Chem. 10

(1983) 285.

M.Y. Lee, S.S. Kim, Phytochem. 35 (1994) 287.

M. Krsnik-Rasol M., Int. J. Devel. Biol. 35 (1991) 259.

K.K. Makinen, J. Tenovuo, Anal.Biochem. 126 (1982)

B. Balen, M. Krsnik-Rasol, V. Simeon-Rudolf, J. Plant.

Physiol. 160 (2003) 1401.