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Screening of Medicinal Plants for Potential Source of l-Asparaginase and Optimization of Conditions for Maximum Extraction and Assay of l-Asparaginase from Asparagus racemosus

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Abstract

Different medicinal plants were screened for l-asparaginase. Asparagus racemosus exhibited highest activity (10.11 ± 0.12 U/ml) and specific activity (22.78 ± 0.28 U/mg of protein). A. racemosus was collected from Padmapuram garden of Araku valley, Visakhapatnam district. l-asparaginase activity was detected from the extracts of leaves and rhizome. Enzyme activity was maximum in the extract of rhizome (9.58 ± 0.12 U/ml) with specific activity (21.73 ± 0.28 U/mg of protein) compared with leaves which have the enzyme activity (1.85 ± 0.06 U/ml) with specific activity (2.68 ± 0.14 U/mg of protein). Optimum conditions for the extraction and assay of l-asparaginase from plant rhizomes were studied. Results showed maximum activity of l-asparaginase when the sample to buffer ratio was 3:6, sample weight (g)/buffer volume (ml) using 0.02 M of potassium phosphate buffer solution pH 8.2 at 40 °C. The l-asparaginase activity was 16.01 ± 0.06 U/ml with specific activity (26.81 ± 0.42 U/mg of protein) under optimum conditions.

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References

  • Abdel Hameed AM (2005)’Production and Characterization of l-asparaginase from local isolate of Serratia marcescens bacteria’. In: Dissertation, College of Science, Baghdad University, Iraq

  • Ajila CM, Rao LJ, Rao UP (2010) Characterization of bioactive compounds from raw and ripe Mangifera indica L. peel extracts. Food Chem Toxicol 48:3406–3411

    Article  Google Scholar 

  • Bano Mozeena, Sivaramakrishnan VM (1980) Preparation and properties of l-asparaginase from green chillies (Capsicum annum L.). J Biosci 2:291–297

    Article  Google Scholar 

  • Bansal S, Gnaneswari D, Mishra P, Kundu B (2010) Structural stability and functional analysis of l-asparaginase from Pyrococcus furiosus. Biochemistry (Mosc) 75(3):375–381

    Article  Google Scholar 

  • Borek D, Jaskolski M (2001) Sequence analysis of enzymes with asparaginase activity. Acta Biochim Pol 48:893–902 (no. 4/2001)

    Google Scholar 

  • Broome JD (1961) Evidence that the l-asparaginase activity of guinea pig serum is responsible for its antilymphoma effects. Nat Lond 191:1114–1115

    Article  Google Scholar 

  • Chibnall AC (1939) Protein metabolism in plants. Yale University Press, New Haven

    Google Scholar 

  • Clementi A (1922) La desamidation enzymatique de l’asparagine chez les differentes especes animals et la signification physiologique de sa presence dans l’organisme(Asparginase in vivo in Merschnicinchen serum). Arch Intern Physiol 19:369–398

    Google Scholar 

  • Copeland RA (2000) Enzymes in antiquity. Practical introduction to structure, mechanism and data analysis Enzymes, 2nd edn. John Wiley-VCH, New York

    Google Scholar 

  • Hosamani R, Kaliwal BB (2011) Isolation, molecular identification and optimization of fermentation parameters for the production of l-asparaginase, an anticancer agent by Fusarium equiseti. Int J Microbiol Res 3:108–193

    Article  Google Scholar 

  • Kidd J (1953) Regression of transplanted lymphomas induced in vivo by means of normal guinea pig serum. I. Course of transplanted cancers of various kinds in mice and rats given guinea pig serum, horse serum or rabbit serum. J Exp Med 98:565–582

    Article  Google Scholar 

  • Lees EM, Blackeney AB (1970) The distribution of asparaginase activity in legumes. Biochim Biophys Acta (BBA) Gen Subject 215:145–151

    Article  Google Scholar 

  • Lough TJ, Reddington BD, Grant MR, Hill DF, Reynolds PH, Farnden KJ (1992) The isolation and characterization of a cDNA clone encoding l-asparaginase from developing seeds of Lupin (Lupinus arboreus). Plant Molec Biol 19:391–399

    Article  Google Scholar 

  • Lowry OH, Rosebrough NJ, Farr AL, Randall RJ (1951) Protein measurement with Folin phenol reagent. J Biol che 193:265–275

    Google Scholar 

  • Majeed AMD (2011) Extraction, purification and characterization of l-asparaginase from Withania somnifera ripe fruits. In: Ph. D thesis, Department of Biotechnology, College of Science, University of Baghdad, Iraq

  • Manning GB, Campbell LL (1957) The asparagine deaminase of Bacillus coagulans and Bacillus strearothermophilus. Can J Microbiol 3:1001–1009

    Article  Google Scholar 

  • Michalska K, Jaskolski M (2006) Structural aspects of l-asparaginases, their friends relations. Acta Biochim Pol 53(4):627–640

    Google Scholar 

  • NPGS/GRIN (1799) “Asparagus racemosus information from NPGS/GRIN (National Plant Germ plasm System/Germ plasm Information Network)” USDA.Sp. pl. 2(1):152. August 6, 2002. Retrieved April 25, 2009

  • Oza VP, Parmar PP, Kumar S, Subramanian RB (2010) Anti cancer Properties of highly purified l-asparaginase from Withania somnifera L. against Acute Lymphoblastic Leukemia. Appl Biochem Biotechnol 160:1833–1840

    Article  Google Scholar 

  • Peter MPJ, Raj JY, Sicis VP, Joy V, Saravanan J, Sakthivel S (2012) GC-MS analysis of bioactive components on the leaves extract of Stylosanthes fruticosa—a potential folklore medicinal plant. Asian J Plant Sci Res 2:243–253

    Google Scholar 

  • Sarker SD, Nahar L (2012) An introduction to natural products isolation. Nat Prod Isol Methods Mol Biol 864:1–25

    Article  Google Scholar 

  • Sieciechowicz KA, Joy KW, Ireland RJ (1988) The metabolism of asparagine in plants. Phytochemistry 27:663–671

    Article  Google Scholar 

  • Sodek L, Lea PJ, Miflin BJ (1980) Distribution and Properties of a potassium-dependent asparaginase isolated from developing seeds of Pisum sativum and other plants. J Plant Physiol 65:22–26

    Article  Google Scholar 

  • Stecher AL, Morgantetti P, De Deus I, Polikarpov LA (1999) Stability of l-asparaginase: an enzyme used in leukemia treatment. J Pharm Acta Helv 74(1):1–9

    Article  Google Scholar 

  • Velmurugan P, Kamaraj M, Prema D (2010) Phytochemical constituents of Cadaba trifoliata Roxb. root exctract. Int J Phytomed 2:379–874

    Google Scholar 

  • Verma N, Kumar K, Kaur G, Anand S (2007) l-Asparaginase: a promising chemotherapeutic agent. Critical Rev Biotechnol 27:45–62

    Article  Google Scholar 

  • Warangkar SC, Khobragade CN (2010) Purification, characterization and effect of thiol compounds on activity of the Erwinia carotovora l-asparaginase. Enz Res 1:1–10

    Google Scholar 

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Beulah, K., Hemalatha, K.P.J. Screening of Medicinal Plants for Potential Source of l-Asparaginase and Optimization of Conditions for Maximum Extraction and Assay of l-Asparaginase from Asparagus racemosus. Iran J Sci Technol Trans Sci 43, 1–6 (2019). https://doi.org/10.1007/s40995-017-0359-x

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  • DOI: https://doi.org/10.1007/s40995-017-0359-x

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