Characterization of best naringinase producing fungus strain isolated from palmyrah (Borrasus flabellifer) fruit pulp

  • Authors

    • Sinthuja Karuppaija
    • Kapilan Ranganathan Department of BotanyUniversity of JaffnaSri Lanka
    • Vasantharuba Seevaratnam
    2016-07-19
    https://doi.org/10.14419/ijbr.v4i2.6289
  • Naringinase, Paddy Husk, Palmyrah Pulp, Rhizophus stolonifer.
  • Background: The Palmyrah (Borrasus flabellifer L.) fruit pulp has the bitter compound flabelliferin (a tetraglycoside) which can be hydrolyzed by naringinase enzyme. The diverse groups of filamentous fungi and bacteria that live in different substrates have the capacity of producing extracellular naringinase enzyme which is of tremendous industrial value.

    Objective: The objective of the study was to isolate the naringinase producing fungal strains from Palmyrah and to identify the best naringinase producer under liquid and solid state fermentation systems.

    Methods: Fungal strains isolated from Palmyrah fruit pulp and the soil where pulp is allowed to decay, were grown on naringin agar selective medium at pH 6.0 at room temperature and the production of extracellular naringinase was measured in the liquid fermentation media and solid state fermentation system using paddy husk as support.

    Results: Five fungal strains isolated from the palmyrah pulp and the pulp decaying in sand designated as PF1,PF2,PF3,PF4 & PF5 had the ability to produce extracellular naringinase enzyme in liquid fermentation media. Fungal strain PF4 that showed highest naringinase enzyme activity (1.769U/ml) was selected among the isolated five fungal strains and identified as Rhizophus stolonifer based on the morphological and biochemical characteristics. When this strain was grown in the solid state fermentation system using paddy husk as media, narininase production was higher (269.84 U/gram of dry substrate) in seven days.

    Conclusion: Rhizophus stolonifer could be used to produce large scale naringinase enzyme under solid state fermentation system using very cheap, easily available, agricultural waste paddy husk as support without the need of expensive and well equipped laboratories.

  • References

    1. [1] Arasaratnam, V., Mylvaganam, K., &Balasubramaniam, K. (2001). Glucoamylase production by Aspergillusniger in solid state fermentation with paddy husk as support. Journal of food science and technology, 38(4), 334-338.

      [2] Barrios-González, J., and Tarragó-Castellanos, M. R. (2015). Solid-State Fermentation: Special Physiology of Fungi.

      [3] Bram, B., &Solomons, G. L. (1965). Production of the enzyme naringinase by Aspergillusniger. Applied microbiology, 13(6), 842-845.

      [4] CO, O. (2011). Rhizopusstolonifer exhibits dimorphism. Afri. J. Biotechnol, 10 (20), 4269-4275.

      [5] Elinbaum, S., Ferreyra, H., Ellenrieder, G., & Cuevas, C. (2002). Production of Aspergillusterreusβâ€Lâ€rhamnosidase by solid state fermentation. Letters in applied microbiology, 34(1), 67-71.http://dx.doi.org/10.1046/j.1472-765x.2002.01039.x.

      [6] Goulart, A. J., Carmona, E. C., &Monti, R. (2005). Partial purification and properties of cellulase-free alkaline xylanase produced by Rhizopusstolonifer in solid-state fermentation. Brazilian Archives of Biology and Technology, 48 (3), 327-333.http://dx.doi.org/10.1590/s1516-89132005000300001.

      [7] Hernández-Lauzardo, A. N., Bautista-Baños, S., Velázquez-del Valle, M. G., & Trejo-Espino, J. L. (2006). Identification of Rhizopusstolonifer (Ehrenb: Fr.) Vuill, causal agent of Rhizopus rot disease of fruits and vegetables. Revista Mexicana de Fitopatología, 24(1), 65-69.

      [8] Jansz, E. R., Nikawela, J. K., Gooneratne, J., &Theivendirarajah, K. (1994). Studies on the bitter principle and debittering of Palmyrah fruit pulp. Journal of the Science of Food and Agriculture, 65(2), 185-189.http://dx.doi.org/10.1002/jsfa.2740650210.

      [9] Jayaratnam, M. (2015). The chemistry and biochemistry of palmyrah products (Doctoral dissertation).

      [10] Kapilan, R., and Arasaratnam, V. (2011). Paddy husk as support for solid state fermentation to produce xylanase from Bacillus pumilus. Rice Science, 18 (1), 36-45.http://dx.doi.org/10.1016/S1672-6308(11)60006-1.

      [11] Keerthini, S., Kapilan, R., Vasantharuba, S. (2016a). Characterization of best naringinase producing fungus isolated from the citrus fruits. International Journal of Biological Research, 4(2), 83-87. http://dx.doi.org/10.14419/ijbr.v4i2.6281.

      [12] Keerthini, S, Kapilan, R., Vasantharuba, S. (2016b). Optimization of naringinase production from Aspergillusflavus in solid state fermentation media using citrus peel as support, Scholars Academic Journal of Biosciences, 4 (6), 535-543. DOI: 10.21276/sajb.2016.4.6.16

      [13] Kumar, V. V. (2015). Comparative studies on inducers in the production of naringinase from Aspergillusniger MTCC 1344. African Journal of Biotechnology, 9(45), 7683-7686.

      [14] Kwon, J. H., Kang, S. W., Kim, J. S., & Park, C. S. (2001). Rhizopus soft rot on cherry tomato caused by Rhizopusstolonifer in Korea. Mycobiology, 29(3), 176-178.

      [15] Mendoza-Cal, A., Cuevas-Glory, L., Lizama-Uc, G., & Ortiz-Vázquez, E. (2010). Naringinase production from filamentous fungi using grapefruit rind in solid state fermentation. African Journal of Microbiology Research, 4(19), 1964-1969.

      [16] Navaratnam, P., Ketheeswary, N., Senthuran, A., &Arasaratnam, V. (2003). Preliminary studies on the isolation of naringinase producing fungus.

      [17] Ni, H., Li, L., Xiao, A., Cao, Y., Chen, Y., &Cai, H. (2011). Identification and characterization of a new naringinase-producing strain, Williopsiscalifornica Jmudeb007. World Journal of Microbiology and Biotechnology, 27(12), 2857-2862.http://dx.doi.org/10.1007/s11274-011-0766-7.

      [18] Nikawela, J. K., Abeysekara, A. M., &Jansz, E. R. (2011). Flabelliferins-steroidal saponins from palmyrah (Borasus flabellifer L.) fruit pulp isolation by flash chromatography, quantification and saponin related activity. Journal of the National Science Foundation of Sri Lanka, 26(1).http://dx.doi.org/10.4038/jnsfsr.v26i1.3080.

      [19] Nikawala, J. K., Jansz, E. R., Baeckstrom, P., Abeysekera, A. M., &Wijeyaratne, S. C. (2000). Flabelliferins of naringinase debittered palmyrah fruit pulp.

      [20] Norouzian, D., Hosseinzadeh, A., Inanlou, D. N., &Moazami, N. (2000). Production and partial purification of naringinase by Penicilliumdecumbens PTCC 5248. World Journal of Microbiology and Biotechnology, 16(5), 471-473.http://dx.doi.org/10.1023/A:1008962131271.

      [21] Pandey, A. (1992). Recent process developments in solid-state fermentation. Process Biochemistry, 27(2), 109-117.http://dx.doi.org/10.1016/0032-9592(92)80017-W.

      [22] Radhakrishnan, I., &Sampath, S. Isolation and characterization of enzyme naringinase from Aspergillusflavus. International Journal of Advanced Biotechnology and Research, 1(4), 208-212.

      [23] Ribeiro, M. H. (2011). Naringinases: occurrence, characteristics, and applications. Applied microbiology and biotechnology, 90(6), 1883-1895.http://dx.doi.org/10.1007/s00253-011-3176-8.

      [24] Sinthuja, K., Kapilan, R., Vasantharuba, S. (2016). Optimization of naringinase production by Rhizophus stolonifer in solid state fermentation media using paddy husk as support, Scholars Academic Journal of Biosciences, 4(6), 507-514. DOI: 10.21276/sajb.2016.4.6.10

      [25] Sumuduni, K. A. V., Jansz, E. R, and Wickremasekara, N. T. (2002). A review of the chemistry and biochemistry of seed shoot flour and fruit pulp of the palmyrah palm (Borassus flabellifer L.).

      [26] Thammawat, K., Pongtanya, P., Juntharasri, V., &Wongvithoonyaporn, P. (2008). Isolation, preliminary enzyme characterization and optimization of culture parameters for production of naringinase isolated from Aspergillusniger BCC 25166. Kaestsart J Nat Sci, 42, 61-72.

  • Downloads

  • How to Cite

    Karuppaija, S., Ranganathan, K., & Seevaratnam, V. (2016). Characterization of best naringinase producing fungus strain isolated from palmyrah (Borrasus flabellifer) fruit pulp. International Journal of Biological Research, 4(2), 97-101. https://doi.org/10.14419/ijbr.v4i2.6289