Advances in Biochemistry
Volume 7, Issue 1, March 2019, Pages: 15-21
Received: Apr. 6, 2019;
Accepted: May 23, 2019;
Published: Jun. 11, 2019
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Pierre Alexandre Eric Djifaby Sombié, Department of Crop Production, Institute of Environment and Agricultural Research (INERA), Ouagadougou, Burkina Faso
Ahmed Yacouba Coulibaly, Unit of formation and Research in Sciences and Technology, University Norbert Zongo, Koudougou, Burkina Faso
Adama Hilou, Laboratory of Biochemistry and Chemistry Applied (LABIOCA), Department of Biochemistry-Microbiology, University of Ouagadougou, Ouagadougou, Burkina Faso
Martin Kiendrebéogo, Laboratory of Biochemistry and Chemistry Applied (LABIOCA), Department of Biochemistry-Microbiology, University of Ouagadougou, Ouagadougou, Burkina Faso
Cowpea is an important protein crop widespread in Africa. The purpose of this research was to determine the content of trypsin and chymotrypsin inhibitors in different genotypes of cowpea seeds. Trypsin percentage inhibition showed about 13.5-fold variation (5.12% ± 1.47 to 70.52% ± 6.58) between the cowpea genotypes respectively for KVx 421-2J and Kondèsyoungo local. The chymotrypsin inhibitory activity varies among cowpea genotypes from 21.19 to 76.94%. The highest percent inhibitory activity was exhibited by KVx 396-4-5-2D on chymotrypsin. This study also showed significant correlations between type of cowpea genotype and trypsin inhibition potential and also between colour and chymotrypsin inhibition potential of cowpea seeds. Kondèsyoungo local, a landraceae genotype exhibited the high potential to inhibit the trypsin enzyme. Coloured seeds of cowpea genotypes possess higher percentage inhibition of chymotrypsin than the colourless ones (p < 0.05). The calculated mean of trypsin and chymotrypsin inhibition activities showed that Labagela local genotype possess the highest inhibition activity of both protease enzymes. The PCA components analysis and the dendrogram performed basis on the protease inhibitory activities divided the thirty-one genotypes of cowpea used in this study into three classes. The results presented in this work can contribute greatly to the planning of a cowpea breeding program aimed at reducing the content of proteases inhibitors in order to improve the nutritional value of seeds or to increase PI content for tolerance to stored grain pests.
Pierre Alexandre Eric Djifaby Sombié,
Ahmed Yacouba Coulibaly,
Influence of Different Cowpea (Vigna unguiculata (L.) Walp.) Genotypes from Burkina Faso on Proteases Inhibition, Advances in Biochemistry.
Vol. 7, No. 1,
2019, pp. 15-21.
A. Baptista, O. Pinho, E. Pinto, S. Casal, C. Mota, I. M. P. L. V. O. Ferreira, “Characterization of protein and fat composition of seeds from common beans (Phaseolus vulgaris L.), cowpea (Vigna unguiculata L. Walp) and bambara groundnuts (Vigna subterranea L. Verdc) from Mozambique”, Food Measure 2016. doi 10.1007/s11694-016-9412-2.
Y. Weng, A. Shi, W. S. Ravelombola, W. Yang, J. Qin, D. Motes, D. O. Moseley, P. Chen, “A Rapid method for measuring seed protein content in cowpea (Vigna unguiculata (L.) Walp)”, American Journal of Plant Sciences, vol. 8, pp. 2387-2396, 2017. doi: 10.4236/ajps.2017.810161.
G. Ddamulira, C. A. Santos, M. Alanyo, I. Ramathani, M. Maphosa, “Maturity, protein content and yield stability of cowpea in Uganda”, South African Journal of Plant and Soil pp. 1–7, 2017. http://dx.doi.org/10.1080/02571862.2016.1274919
K. D. E. M. G Frota, L. A. R Lopes, I. C. V Silva, J. A. G Arês, “Molecular profile, purity and presence of trypsin inhibitors in cowpea protein isolates”, Revista Caatinga, vol. 31 no. 1, pp. 202-208, 2018. http://dx.doi.org/10.1590/1983-21252018v31n123rc
P. A. E. D Sombié, I. Ouedraogo, J. B. D. L. S Tignegré, A. Hilou, T. J. Ouedraogo, M. Kiendrébéogo, “Genotypic variation of mineral elements and phytate levels of thirty cowpeas (Vigna unguiculata L. walp.) varieties cultivated in Burkina Faso”, J Food Chem Nutr 2018.
P. A. E. D Sombié, M. Compaoré, A. Coulibaly, J. T. Ouédraogo, J. B. D. L. S Tignégré, M Kiendrébéogo, Antioxidant and phytochemical studies of 31 cowpeas (Vigna unguiculata (L. Walp.)) genotypes from Burkina Faso”, Foods, vol. 7 no 9, 143, 2018. doi: 10.3390/foods7090143
V. C. Silvestrini, D. B. Gonçalves, P. A. Granjeiro, J. A. D. Silva, “Anti-nutritional factors and digestibility of protein in Cayocar brasiliense seeds”, Food Sci Technol., Vol 37, no 4, pp. 632-639, 2017. doi: http://dx.doi.org/10.1590/1678-457X.28716.
M. A. Ojo, B. I. O Ade-Omowaye, P. O. Ngoddy,“Processing effects of soaking and hydrothermal methods on the components and in vitro protein digestibility of Canavalia ensiformis”, International Food Research Journal, Vol. 25, no 2, pp. 720-729, 2018.
J. Ruan, Y. H. C Jun Yan, C. Jianping, W. Sun, G. Zhao, “Purification and properties of the chymotrypsin inhibitor from wild emmer wheat (Triticum dicoccoides) of Israel and its toxic effect on beet armyworm, Spodoptera exigua”, Pesticide Biochemistry and Physiology 2017. doi: 10.1016/j. pestbp.2017.06.013.
S. S. Mohanraj, S. D. Tetali, N. Mallikarjuna, A. Dutta-Gupta, K. Padmasree, “Biochemical properties of a bacterially-expressed Bowman-Birk inhibitor from Rhynchosia sublobata (Schumach.) Meikle seeds and its activity against gut proteases of Achaea janata”, Phytochemistry, Vol 151, pp. 78-90, 2018. https://doi.org/10.1016/j.phytochem.2018.02.009.
L. P. Dias, J. T. A. Oliveira, L. C. B Rocha-Bezerra, D. O. B Sousa, H. P. S Costa, N. M. S Araujo, A. F. U Carvalho, P. M. S Tabosa, A. C. O Monteiro-Moreira, M. D. P Lobo, F. B. M. B Moreno, B. A. M Rocha, J. L. S Lopes, L. M Beltramini, I. M Vasconcelos, “A trypsin inhibitor purified from Cassia leiandra seeds has insecticidal activity against Aedes aegypti”, Process Biochemistry, Vol 57, pp. 228–238, 2017. http://dx.doi.org/doi:10.1016/j.procbio.2017.03.015
A. Nautiyal, N. Gaur, K. Singh, “Effect of soybean leaf protease inhibitor on the mean leaf area consumed by Spodopetra litura and Spilosoma obliqua larvae”, Int J Curr Microbiol App Sci, Vol. 6, no 11, pp. 1435-1444, 2017, doi: https://doi.org/10.20546/ijcmas.2017.611.171
M. Xiang, X. Zhang, Y. Deng, Y. Li, J. Yu, J. Zhu, X. Huang, J. Zhou, H. Liao, “Comparative transcriptome analysis provides insights of anti-insect molecular mechanism of Cassia obtusifolia trypsin inhibitor against Pieris rapae”, Archives of Insect Biochemistry and Physiology, Vol. 97, no 1, e21427, 2018. https://doi.org/10.1002/arch.21427
E. Guillamon, M. M. Pedrosa, C. Burbano, C. Cuadrado, M. D. C. Sanchez, M. Muzquiz, “The trypsin inhibitors present in seed of different grain legume species and cultivar”, Food Chemistry, Vol. 107, pp. 68–74, 2008. doi: 10.1016/j.foodchem.2007.07.029
N. Nikmaram, S. Y. Leong, M. Koubaa, Z. Zhu, F. J. Barba, R. Greiner, I. Oey, S. Roohinejad, “Effect of extrusion on the anti-nutritional factors of food products: An overview”, Food Control 2017. doi: 10.1016/j.foodcont.2017.03.027.
S. Banerjee, A. P. Giri, V. S. Gupta, S. K. Dutta, “Structure-function relationship of a bio-pesticidal trypsin/chymotrypsin inhibitor from winged bean”, International Journal of Biological Macromolecules 2016. http://dx.doi.org/10.1016/j.ijbiomac.2016.12.018
S. Klomklao, S. Benjakul, H. Kishimura, K. Osako, M. Tanaka, “A heat-stable trypsin inhibitor in adzuki bean (Vigna angularis), effect of extraction media, purification and biochemical characteristics”, International Journal of Food Science & Technology., Vol 45 no 1, pp. 163-169, 2009. doi: 10.1111/j.1365-2621.2009.02117.x.
L. B Bueno-Borges, M. A Sartim, C. C Gil, S. V. Sampaio, P. H. V. Rodrigues, M. A. B. Regitano-d’Arce, “Sacha inchi seeds from sub-tropical cultivation: effects of roasting on antinutrients, antioxidant capacity and oxidative stability”, Journal of Food Science and Technology, Vol 55, no 10, pp. 4159-4166, 2018. https://doi.org/10.1007/s13197-018-3345-1
K. F Shireen, R. D. Pace, M. Egnin, C. S. Prakash, “Effects of dietary proteins and trypsin inhibitor on growth and lipid metabolism in hamsters”, Mal J Nutr., Vol 7, no 1 & 2, pp.: 1-14, 2001.
L. Shi, K. Mu, S. D. Arntfield, M. T. Nickerson, “Changes in levels of enzyme inhibitors during soaking and cooking for pulses available in Canada”, Journal of Food Science and Technology., Vol 54, no 4, 1014-1022, 2017. doi 10.1007/s13197-017-2519-6.
G. A Joanitti, R. S. Sawant, V. P. Torchilin, S. M. D. Freitas, R. B. Azevedo, “Optimizing liposomes for delivery of Bowman-Birk protease inhibitors—Platforms for multiple biomedical applications”, Colloids and Surfaces B: Biointerfaces 2018. https://doi.org/10.1016/j.colsurfb.2018.04.033.
B. Bijina, S. Chellappan, J. G. Krishna, S. M. Basheer, K. K. Elyas, A. H. Bahkali, M. Chandrasekaran, “Protease inhibitor from Moringa oleifera with potential for use as therapeutic drug and as seafood preservative”, Saudi Journal of Biological Sciences., Vol. 18, no 3, pp. 273-281, 2011. doi: 10.1016/j.sjbs.2011.04.002.
H. Kaur, A. Kaur, A. P. Kaur, P. J. Rup, S. K. Sohal, “Assessment of soybean inhibitor as a biopesticide against melon fruit fly, Bactrocera cucurbitae (Coquillett)”, J Plant Dis Prot 2017. doi: 10.1007/s41348-017-0108-6.
D. T. Prasad, N. S. Umpathv, R. Veeranna, “Genotypic variation in cowpea (Vigna unguiculata) cultivars in relation to insect resistance”, J Plant Biochemistry & Biotechnology., Vol 5, pp. 47- 49, 1996.
V. G. M. Krishnan, K. Murugan,“Purification, characterization and kinetics of protease inhibitor from fruits of Solanum aculeatissimum Jacq”, Food Science and Human Wellness 2015, Vol 4, no (3), pp. 97-107. http://dx.doi.org/10.1016/j.fshw.2015.06.003.
Z. Lv, Y. Chu, Y. Wang, “HIV protease inhibitors: a review of molecular selectivity and toxicity”, HIV AIDS (Auckl), Vol. 7, pp. 95-104, 2015. http://dx.doi.org/10.2147/HIV.S79956.
S. P. Stanojević, M. B. Barać, M. B. Pešić, B. V. Vucelić-Radović, “The influence of soybean genotypes and HTC processing method on trypsin inhibitor activity of soymilk”. Journal of Agricultural Sciences, Vol 61, no 3, pp. 271-279, 2016. doi: 10.2298/JAS1603271S.
D. D. D. Souza, R. M. P. Brandão-Costa, W. W. C. Albuquerque, A. L. F. Porto, “Partial purification and characterization of a trypsin inhibitor isolated from Adenanthera pavonina L. seeds”, South African Journal of Botany., Vol. 104, pp. 30-34, 2016. http://dx.doi.org/10.1016/j.sajb.2015.11.008.