Studies on proteolytic inhibitory peptides from the seeds Ricinus communis
DOI:
https://doi.org/10.56511/JIPBS.2017.v4.i04.pp112-116Abstract
The search for dietary compounds that prevent many life style diseases is deemed crucial to tackle this major health problem worldwide, and recent developments in the field of health have suggested that increased protein consumption, particularly from plant sources, might reduce many life style diseases. Nowadays, interest among researchers has been emerging to identify, isolate and characterize bioactive peptides from plant and animal sources. Bioactive peptides are considered as specific protein fragments that are inactive within the sequence of the parent protein and they exhibit various physiological functions after released from their parent protein. Bioactive peptides were produced by germination, fermentation and cold storage from the seeds of Ricinus communis. The seeds were germinated for various days and germinated seedlings were subjected to fermentation for different period of time using Bacillus substilis. The total protein and protease inhibitor activity were monitored during germination. The fermented soluble protein content was further subjected to cold storage (0 – 4oC) for seven days. The protein content was gradually increased from first day of germination (9.18%) and it was maximum on the third day (11.73%) followed by gradual decrease their onwards. It was observed that proteolytic inhibitory activity was less in the initial period of germination (23.32 TIU/mg of protein) followed by gradual increase up to fourth day (32.04 TIU/mg of protein) and decrease their onwards during the germination. Similarly, fourth day Fermented and fifth day cold stored sample showed high proteolytic inhibitory activity, 408 TIU/mg and 286 TIU/mg respectively.
Keywords:
Ricinus communis seeds, food processing methods, bioactive peptides, protease inhibitor peptidesDownloads
References
Jin-Young Kim, Seong-Cheol Park, Indeok Hwang , Hyeonsook Cheong, Jae-Woon Nah, Kyung-SooHahm and Yoonkyung Park: Protease Inhibitors from Plants with Antimicrobial Activity. Int. J. Mol. Sci 2009; 10: 2860-2872.
Lingaraju, M.H. and Gowda, LR: A Kunitz trypsin inhibitor of Entadascandens seeds: Another member with single disulfide bridge. BiochemBiophysActa. 2008; 1784 (5): 850-5.
Kempohalli S. Chandrashekharaiah: Storage Proteins and Trypsin Inhibitors of an Underutilized Legume, Mucuna: Variability and Their Stability during Germination. American Journal of Plant Sciences 2013; 4: 910-916.
Kennedy, AR: The Bowman-Birk inhibitor from soybeans as an anticarcinogenic agent. American Journal of Clinical Nutrition.1998; 68, 1406S – 1412S.
Oliva MLV, Souza-Pinto JC, Batista IF, Araujo MS, Silveria VF, Auerswald EA, Menrele R, Eckerskorn C, SampaioMU, &Sampaio CAM: Leucenaleucocephala serine protease performance and feed utilization. Aquaculture 2000; 196, 105-123.
SyedRakashanda, Ishaq, M., Masood, A. and Amin, S: Antibacterial activity of a trypsin-chymotrypsinelastaseinhibitor isolated from Lavateracashmerianacamb. Seeds. The Journal of Animal & Plant Sciences 2012; 22(4): 983-986.
Valueva TA, Mosolov VV: Protein inhibitors of proteinases in seeds: Classification, distribution, structure and properties. Russ. J. Plant Physiol 1999; 46:307 – 321.
Carlini CR, Grossi – de – sa MF: Plant toxic proteins with insecticidal properties. A review on their potentialities as bioinsecticides. Toxicon 2002; 40:1515 – 1539.
Breiteneder H, Radauer CA.: Classification of plant food allergens. J. Allergy Cln. Immun 2004; 113(5): 821 – 830.
Kim JY, Park SC, Kim MH, Lim HT, Park Y, Hahm KS: Antimicrobial activity studies on a trypsin – chymotrypsin protease inhibitor obtained from potato. Biochem. Bioph. Res. Co 2005; 330 (3): 921 – 927.
Kataoka H, Itoh H, Koono, M: Emerging multifunctional aspects of cellular serine proteinase inhibitors in tumor progression and tissue regeneration. Pathol. Int. 2002; 252: 89-102.
Fumagalli L, Rita Businaro, Stefania LN, Toesca A, Pompili E, Evangelisti E, Giannetti S, Flora Ippoliti, De Renzis G: Protease inhibitors in mouse skeletal muscle: tissue-associated components of serum inhibitors and calpastatin. Cellular and molecular biology 1996; 42(4): 535-546.
Thompson MG, Palmer RM: Signalling pathways regulating protein turnover in skeletal muscle 1998; 10(1): 1-11.
Kato GJ: Human genetic diseases of proteolysis. Hum Mutat 1999; 13(2): 87-98.
Asztalos Bela F, Ernst Schaefer J, Katalin Horvath V, Caitlin Cox E, Sally Skinner, Jul Gerrior, Sherwood Gorbach L, Christine Wanke. Protease inhibitor-based HAART, HDL, and CHD-risk in HIV-infected patients. Atherosclerosis 2006; 184(1): 7277.
Yeni P: Update on HAART in HIV. J. Hepatol 2006; 44 (1): 100 – 103.
Lopes JLS, Valadares NF, Moraes DI, Rosa JC, Araujo HSS, Beltramini LM: Physico-chemical and antifungal properties of protease inhibitors from Acacia plumose. Phytochemistry 2009; 70: 871-879.
Ricinuscommunis, Natural Resources Conservation Service PLANTS Database. USDA . Retrieved 1 February 2016.
BSBI List 2007, Botanical Society of Britain and Ireland. Archived from the original (xls) on 2015-02-25.
Phillips, Roger; Rix, Martyn. Annuals and Biennials. London: Macmillan. 1999; 106. ISBN 0-333-74889-1 .
OloyedeGaniyat K.: Antioxidant activities of Methyl Ricinoleate and Ricinoleic Acid Dominated Ricinuscommunis seeds Extract Using Lipid Peroxidation and Free Radical Scavenging Methods; Research Journal of Medicinal Plant 2012; 6(7): 511-520.
Singh Ramesh Kumar.; Gupta M K.; Katiyar Deepti; Srivastava Anshul.; Singh Parul.: In-vitro antioxidant activity of the successive extracts of ricinus communis stems; IJPSR 2010; 1(8):100-103.
Dnyaneshwar J Taur et al.: Antinociceptive activity of Ricinuscommunis L. leaves; Asian Pacific Journal of Tropical Biomedicine 2011; 139-141.
AbhishekMathur; Satish K. Verma, SajadYousuf, Santosh K. Singh, Gbks Prasad and V. K. Dua; Antimicrobial potential of roots of Riccinuscommunis against pathogenic microorganisms; International journal of pharma and bio sciences 2011; 2(1): 545-548.
Shokeen P., Anand P., Murali Y. K., Tandon V: Antidiabetic activity of 50% ethanolic extract of Ricinuscommunis and its purified fractions. In Food and Chemical Toxicology 2008; 46: 3458 – 3466.
Ilavarasan R, Mallika M, Venkataraman S: Anti-inflammatory and free radical scavenging activity of Ricinuscommunis root extract. J Ethnopharmacol. 2006; 103: 478-80.
Adriana Cristina Valderramas; Sérgio Henrique Pereira Moura; MairaCouto, SilvanaPasetto ; Gilberto OrivaldoChierice; Sergio Augusto Catanzaro Guimarães5; Ana Claudia Bensuaski de Paula Zurron; Antiinflammatory activity of Ricinuscommunis derived polymer. Braz J Oral Sci. 2008; 7(27):1666-1672.
Anil Kumar Saini; RohitGoyal; Vinod Kumar Gauttam; AjudhiaNathKalia; Evaluation of anti-inflammatory potential of Ricinuscommunis Linn leaves extracts and its flavonoids content in Wistar rats. Journal of Chemical and Pharmaceutical Research 2010; 2(5):690-695.
Sharma S, Singh T and Vijayvergia R: Molluscicidal activity of some medicinal plants. In Journal of Herbal Medicine and Toxicology 2009; 3(2):155-157.
Upasani, S. M., Kotkar, H. M., Mendki, P. S, Maheshwar, V. L: Partial characterization and insecticidal properties of RicinuscommunisL foliage flavonoids. In Pest Management Science 2003; 59(12):1349-1354.
Ramos-Lopez, M. A., Perez-G, S., Rodriguez-Hernandez, C., Guevarafefer, P. and Zavala-Sanchez, M. A: Activity of Ricinus communis (Euphorbiaceae) against Spodopterafrugiperda (Lepidoptera: Noctuidae). In African Journal of Biotechnology 2010; 9(9):1359-1365.
Sani et al.: Nig. Anti-fertility activity of methanol extracts of three different seed varieties of Ricinuscommunislinn (Euphorbiaceae). Journ. Pharm. Sci. 2007; 6(2):78 – 83.
Sandhyakumary, K., Bobby, R.G., Indira, M.: Antifertility effects of Ricinuscommunis Linn. On rats. Phytother. Res. 2003; 17: 508 – 511.
Vargas-Olvera CY, Sanchez-Gonzalez DJ, Solano JD, AguilarAlonso FA, Montalvo-Munoz F, Martinez-Martinez CM, et al: Characterization of Ndiethylnitrosamine-initiated and ferric nitrilotriacetate-promoted renal cell carcinoma experimental model and effect of a tamarind seed extract against acute nephrotoxicity and carcinogenesis. Mol Cell Biochem 2012; 369(1-2): 105-117.
Havinga RM, Hartl A, Putscher J, Prehsler S, Buchmann C, Vogl CR: Tamarindusindica L. (Fabaceae): patterns of use in traditional African medicine. J Ethnopharmacol 2010; 127(3): 573-588.
Bhadoriya SS, Ganeshpurkar A, Narwaria J, Rai G, Jain AP: Tamarindusindica: extent of explored potential. Pharmacogn Rev 2011; 5(9): 73-81.
De Caluw E, Halamov K, Van Damme P: Tamarindusindica L.: a review of traditional uses, phytochemistry and pharmacology. Afrika Focus 2010; 23(1): 53-83.
Syed Azmal Ali, GrishmaBendre, ShraddhaOjha, V Krishnamurthy, N RamachandraSwamy, Kempohalli S Chandrashekharaiah: Esterases from the Seeds of an Edible Legume, Phaseolus vulgaris L.; Variability and Stability during Germination. American Journal of Plant Sciences 2013; 4(4): 905-909.
Agyei D, Danquah K: Industrial-scale manufacturing of pharmaceutical gradebioactive peptides. Biotechnol Adv 2011; 29:272-7.
Megumi KUBA, Kumi TANAKA, Shinkichi TAWATA, Yasuhito TAKEDA, Masaaki YASUDA: Angiotensin IConverting Enzyme Inhibitory Peptides Isolated from Tofuyo Fermented Soybean. Food, Bioscience, Biotechnology, and Biochemistry 2003; 67(6):1278-1283.
Lone Khaliq Jafar, M A Leekha, K S Chandrashekharaiah: Studies of trypsin inhibitors from the seeds of Tamarindus indica. Journal of Innovations in Pharmaceutical and Biological Sciences (JIPBS) 2017: 4:4, 39-42.
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