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Changes in Antioxidative Enzymes in Resistant and Susceptible Genotypes of Tomato Infected with Root-Knot Nematode (Meloidogyne Incognita)

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Changes in Antioxidative Enzymes in Resistant and Susceptible Genotypes of Tomato Infected with Root-Knot Nematode (Meloidogyne Incognita) Antioxidative enzymes in resistant and susceptible genotypes of tomato infected with root-knot nematode Vol. 43, No. 1, pp. 1-12 Indian Journal of Nematology June, 2013 Changes in Antioxidative Enzymes in Resistant and Susceptible Genotypes of Tomato Infected with Root-Knot Nematode (Meloidogyne incognita) NEENA CHAWLA, KAVITA CHOUDHARY**, SUKHJEET KAUR* AND SALESH JINDAL Department of Vegetable Crops, **Department of Biochemistry, Punjab Agricultural University, Ludhiana-141004, India *Corresponding author, E-mail: [email protected] Received on 17-05-2012 and Accepted on 06-01-2013 ABSTRACT: Changes in activities of antioxidative enzymes (Catalase, Peroxidase, Superoxide dismutase, Polyphenol oxidase, esterase, monodehydro ascorbate reductase, and dehydro ascorbate reductase) after nematode inoculation were investigated in four varieties of tomatoes, (two resistant i.e. Hisar Lalit, PNR- 7 and two susceptible i.e. Punjab Varkha Bahar-1 and Punjab Varkha Bahar- 2. These four varieties were infected at the nursery stage with root-knot nematode (Meloidogyne incognita). The egg masses of M. incognita were taken from the infected brinjal plants. Tomato roots and leaves from un-inoculated and inoculated plants were evaluated for their antioxidative enzyme activities after 7 days and 20 days of infection. The activity of antioxidant enzymes increased after infection with root-knot nematode in the resistant varieties of tomato as compared to that of susceptible varieties. The activities of all enzymes increased after inoculation except the activity of CAT enzyme where a decrease was observed. The isozyme banding patterns of peroxidase and esterase showed that the intensity of bands was more in the resistant genotypes as compared to that of susceptible genotypes, which means that the activity of antioxidant enzymes were more after inoculation in the resistant genotypes as compared to that of susceptible genotypes. An additional band was obtained in the isozyme banding pattern of esterase in the resistant genotypes. Keywords: Tomato, nematode, Meloidogyne incognita, antioxidant enzymes, isozyme Tomato (Lycopersicon esculentum Mill.) a member usually associated with hypersensitive reaction (HR), a of family Solanaceae, is universally known as a protective rapid and localized cell death in the infected plant in food. It is used directly as raw vegetable, in sandwiches, response to nematode attack. salads etc. and also as purees, chutneys and pickles in processed forms. Tomato fruit has undoubtedly assumed Reactive oxygen species (ROS) play an important the status of a functional food considering the role in plant defense and during pathogen attack, levels overwhelming epidemiological evidence for its anti- of ROS detoxifying enzymes like peroxidase (POX) and cancer activity. Root-knot nematode (Meloidogyne catalase (CAT) are often suppressed in resistant plants incognita) causes considerable damage to tomato plants (Klessing et al., 2000). As a result, plants produce more (Kamalvanshi et al., 2004) and results in extensive ROS and accumulation of these components leads to HR losses in yield and quality (Mahajan & Singh, 2001). in plant cells. For example, hydrogen peroxide plays a Though the nematicides are effective against nematodes, major role in triggering HR in incompatible interactions yet they are hazardous for health, soil and environment. (Dangl & Jones 2001). Antioxidant enzymes such as Plant resistance is one of the eco-friendly options for the SOD, POD and CAT are considered to be the main management of nematode diseases. A series of protective enzymes engaged in the removal of free biochemical and physical reactions occur in plants in radicals and activated oxygen species (Blokhina et al., response to root-knot nematode infection. Plants 2003, Devi et al., 2000). Oxidative enzymes such as synthesize certain compounds that are toxic to root-knot POX and pro are reported to be involved in the mechanism nematode. In the family of solanaceae, resistance is of disease resistance. 1 Neena Chawla et al. Peroxidases are heme containing enzymes that growing in 30 cm diameter earthen pots for further catalyse one electron oxidation of several substrates at multiplication. One week old seedlings of tomato genotypes the expense of hydrogen peroxide and are located in cell sown in pots were inoculated with freshly hatched larvae walls and vacuoles. The role of peroxidase in producing of root knot nematode (M. incognita) @ 1 J2s/cc of soil. active oxygen species (AO) is controversial. In cell wall Leaf and root samples were collected at 7 and 20 days peroxidase oxidizes NAD(P)H to produce O2- and H2O2 after inoculation with root-knot nematode. (Elstner and Heupel 1976). Peroxidase in its activity uses Simultaneously, root and leaf samples were also collected H2O2 as the main oxidant and reduces it into H2O, thus from uninoculated plants and carried to the laboratory in acting as an active AO scavenger. Electrophoretic an ice box and analyzed for anti oxidative enzymes. analysis of peroxidase revealed that both the resistant and susceptible plants responded to parasitic invasion by Sample was homogenized in 5ml of cold (40 C) synthesizing new peroxidases isozymes. SOD, the family extraction buffer using pre chilled pestle and mortar. The of metallo-enzymes, catalyses the disproportionation of mixture was then centrifuged at 20,000g for 10 minutes and supernatant was collected and was analyzed for superoxide O2- to molecular oxygen and H2O2 (Scandalios 1993). enzyme activity. Catalase- To chilled sodium phosphate buffer added Catalase catalyses breakdown of H2O2 using one enzyme extract. The reaction was started by adding molecule of H2O2 as substrate donor and another molecule H O to the reaction mixture. The rate of decrease in of H2O2 as oxidant or electron acceptor. Since catalase 2 2 absorbance at 240 nm was measured at 10 second repression results in H2O2 accumulation, this molecule may be responsible for the production of defense signals intervals for 1 min (Chance and Mahley 1955). that directly trigger HR. Two enzymes are involved in the regeneration of reduced ascorbate, namely mono- Superoxide Dismutase- The reaction mixture contained dehydro-acsorbate reductase (MDHAR) which uses methionine, NBT , EDTA, Na2CO3, phosphate buffer NAD(P)H directly to recycle ascorbate and dehydro- and distilled water. The enzyme extract was added at ascorbate-reductase (DHAR). However, the situation is last and the reaction was started by adding 0.1ml riboflavin. further complicated because mono-dehydro-ascorbate The intensity of the color developed was read at 560nm itself is an efficient electron acceptor (Foyer and (Xing et al., 2008). Lelandais 1993, Miyake and Asada 1992). Mono- dehydro-ascorbate is reduced directly to ascorbate using Polyphenol Oxidase- To enzyme extract, phosphate electrons derived from the photosynthetic electron buffer was added. Reaction was started by adding 2% of transport chain. catechol. PPO activity was assayed by measuring the linear increase in absorbance at 410nm (Augustin et al., MATERIALS AND METHODS 1985). The seeds of tomato genotypes viz: (Hisar lal, PNR- Dehydroascorbate Reductase- The reaction mixture 7, Punjab Varkha Bahar-l and Punjab Varkha Bahar-2) contained 0.1M phosphate buffer, ImM EDTA, 2.5mM were procured from the Department of Vegetables glutathione reduced, 0.2mM DHA. To this enzyme Crops, Punjab Agricultural University, Ludhiana. extract was added. DHAR was assayed by measuring the reduction of dehydro-ascorbate at 265nm with an Egg masses of Meloidogyne incognita were extinction coefficient of 14 (Foyer et al., 1989). collected from pure culture already maintained on brinjal plants. These egg masses were transferred to tissue Esterase- To enzyme extract, phosphate buffer was paper kept on wire gauge suspended in water in petri added. Reaction was started by adding 10-3 M indophenyl plate, to allow the eggs to hatch. The second stage acetate. Esterase activity was assayed by change in juveniles (J2s) were then inoculated to brinjal plants absorbance at 625 nm (Sae et al., 1971). 2 Antioxidative enzymes in resistant and susceptible genotypes of tomato infected with root-knot nematode Table 1: Superoxide dismutase (SOD) activity (unit SOD g-l FW) in tomato roots (R) and leaves (L) of resistant and susceptible genotypes against root-knot nematode Genotype Days after inoculation (Specific activity of SOD) 720 UIUI Resistant genotypes Hissar lalit (R) 0.301±0.007 0.311±0.012 0.316±0.013 0.623±0.015 (0.071±0.005) (0.076±0.006) (0.074±0.007) (0.134±0.008) PNR-7 (R) 0.416±0.014 0.42800.016 0.527±0.015 0.831±0.016 (0.104±0.007) (0.113±0.006) (0.132±0.007) (0.205±0.005) Hisar lalit (L) 0.361±0.014 0.372±0.013 0.431±0.017 0.798±0.018 (0.069±0.006) (0.072±0.006) (0.082±0.006) (0.148±0.008) PNR-7 (L) 0.346±0.016 0.35100.015 0.398±0.016 0.842±0.014 (0.059±0.004) (0.061±0.005) (0.068±0.006) (0.134±0.008) Susceptible genotypes Varkha Bahar 1 (R) 0.211±0.016 0.223±0.010 0.275±0.016 0.301±0.007 (0.032±0.002) (0.034±0.002) (0.042±0.003) (0.051±0.004) Varkha Bahar 2 (R) 0.239±0.013 0.251±0.012 0.306±0.014 0.377±0.014 (0.033±0.002) (0.03500.003) (0.043±0.003) (0.054±0.004) Varkha Bahar 1 (L) 0.224±0.015 0.235±0.014 0.268±0.015 0.303±0.016 (0.028±0.001) (0.031±0.002) (0.034±0.002) (0.042±0.003) Varkha Bahar 2 (L) 0.271±0.017 0.280±0.015 0.298±0.016 0.316±0.015 (0.031±0.002) (0.035±0.002) (0.045±0.003) (0.052±0.004) R= Roots; L= Leaves; U= Uninoculated plants; I= Inoculated plants CD (P<0.05) R L R L R L A 0.792 0.907 C 0.792 0.907 ABC 0.224 0.256 B 0.112 0.128 AC 0.112 0.128 AB 0.158 0.181 BC 0.158 0.181 Values are mean ± S.E.
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