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Original Articles

Propiedades tecnofuncionales y biológicas de harina, aislado y fracciones proteicas mayoritarias de semillas de Inga paterno

Techno-functional and biological properties of flour, isolated and majority protein fractions from seeds of Inga paterno

, , &
Pages 400-408 | Received 07 Sep 2016, Accepted 19 Jan 2017, Published online: 26 Apr 2017

References

  • Aguilar-Raymundo, V.G., & Vélez-Ruiz, J.F. (2013). Propiedades nutricionales y funcionales del garbanzo. (Cicer arietinum L.). Temas Selectos De Ingeniería De Alimentos, 7(2), 25–34.
  • Ahmed, S.H., Ahmed, I.A.M., Eltayeb, M.M., Ahmed, S.O., & Babiker, E.E. (2011). Functional properties of selected legumes flours as influenced by pH. Journal of Agricultural Technology, 7, 1291–1302.
  • Aluko, R., & Yada, R. (1995). Structure-function relationships of cowpea (Vigna unguiculata) globulin isolate: Influence of pH and NaCl on physicochemical and functional properties. Food Chemistry, 53(3), 259–265. doi:10.1016/0308-8146(95)93931-G
  • AOAC. (2000). official method of analysis (17th ed.). Washington, D. C.: United States of America: Association of Official Analytical Chemists.
  • Badui Dergal, S. (2006). Química de los alimentos (4ª Edicion.). México: Ed Person.
  • Birk, Y., & Peri, I. (1980). Saponins. In I.E. Liener (Ed.), Toxic constituents of plant foodstuffs (pp. 161–182). New Yok and London: Academic Press.
  • Boye, J., Zare, F., & Pletch, A. (2010). Pulse proteins: Processing, characterization, functional properties and applications in food and feed. Food Research International, 43(2), 414–431. doi:10.1016/j.foodres.2009.09.003
  • Bradford, M.M. (1976). A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Analytical Biochemistry, 72(1), 248–254. doi:10.1016/0003-2697(76)90527-3
  • Butt, M.S., & Batool, R. (2010). Nutritional and functional properties of some promising legumes protein isolates. Pakistan Journal of Nutrition, 9(4), 373–379. doi:10.3923/pjn.2010.373.379
  • Chau, C.-F., Cheung, P.C.K., & Wong, Y.-S. (1997). Functional properties of protein concentrates from three chinese indigenous legume seeds. Journal of Agricultural and Food Chemistry, 45(7), 2500–2503. doi:10.1021/jf970047c
  • Chavan, U.D., McKenzie, D.B., & Shahidi, F. (2001). Functional properties of protein isolates from beach pea (Lathyrus maritimus L.). Food Chemistry, 74(2), 177–187. doi:10.1016/S0308-8146(01)00123-6
  • Deng, Q., Wang, L., Wei, F., Xie, B., Huang, F., Huang, W., et al. (2011). Functional properties of protein isolates, globulin and albumin extracted from Ginkgo biloba seeds. Food Chemistry, 124(4), 1458–1465. doi:10.1016/j.foodchem.2010.07.108
  • Deshphande, U.S., & Deshpande, S.S. (1991). Legumes. In D.K. Salunkhe & S.S. Deshpande (Eds.), Foods of plant origin: Production, Technology and human Nutrition (pp. 137–300). New York, NY: Van Nostrand Reinhold.
  • El Nasri, N.A., & El Tinay, A.H. (2007). Functional properties of fenugreek (Trigonella foenum graecum) protein concentrate. Food Chemistry, 103(2), 582–589. doi:10.1016/j.foodchem.2006.09.003
  • Gallegos Tintorè, S. M., Chel-Guerrero, L. A., Corzo Rios, L. J., & Martìnez Ayala, A. L. (2013). Peptidos bioactivos de proteínas vegetales. En Maira Segura Campos, Luis Chel Guerrero, David Betancur Ancona (Eds.), Bioactividad de péptidos derivados de proteínas alimentarias (pp. 111–122). Yucatán Mex: OmniaScience.
  • García, O., Mazzarri Aiello, C., & Chirino Peña, M. (2012). Caracterización físico-química y propiedades funcionales de la harina obtenida de granos de quinchoncho (Cajanus cajan (L.) Millsp.) sometidos a diferentes procesamientos. Revista Científica UDO Agrícola, 12(4), 919–928.
  • Hailing, P.J., & Walstra, P. (1981). Protein‐stabilized foams and emulsions. Critical Reviews in Food Science & Nutrition, 15(2), 155–203. doi:10.1080/10408398109527315
  • Hayakari, M., Kondo, Y., & Izumi, H. (1978). A rapid and simple spectrophotometric assay of angiotensin-converting enzyme. Analytical Biochemistry, 84(2), 361–369. doi:10.1016/0003-2697(78)90053-2
  • Hermannson, A. (1973). Determination of functional properties of food proteins. London: Academic Press.
  • Herrera Chalé, F.G., Ruiz Ruiz, J.C., Acevedo Fernández, J.J., Betancur Ancona, D.A., & Segura Campos, M.R. (2014). ACE inhibitory, hypotensive and antioxidant peptide fractions from Mucuna pruriens proteins. Process Biochemistry, 49(10), 1691–1698. doi:10.1016/j.procbio.2014.06.021
  • Hojilla-Evangelista, M.P., Evangelista, R.L., & Victor, W.Y. (2009). Characterization of milkweed (Asclepias spp.) seed proteins. Industrial Crops and Products, 29(2–3), 275–280. doi:10.1016/j.indcrop.2008.05.013
  • Jitngarmkusol, S., Hongsuwankul, J., & Tananuwong, K. (2008). Chemical compositions, functional properties, and microstructure of defatted macadamia flours. Food Chemistry, 110(1), 23–30. doi:10.1016/j.foodchem.2008.01.050
  • Khalid, E.K., Babiker, E.E., & El Tinay, A.H. (2003). Solubility and functional properties of sesame seed proteins as influenced by pH and/or salt concentration. Food Chemistry, 82(3), 361–366. doi:10.1016/S0308-8146(02)00555-1
  • Klompong, V., Benjakul, S., Yachai, M., Visessanguan, W., Shahidi, F., & Hayes, K. (2009). Amino acid composition and antioxidative peptides from protein hydrolysates of yellow stripe trevally (Selaroides leptolepis). Journal of Food Science, 74(2), C126–C133. doi:10.1111/jfds.2009.74.issue-2
  • Lawal, O.S., Adebowale, K.O., Ogunsanwo, B.M., Sosanwo, O.A., & Bankole, S.A. (2005). On the functional properties of globulin and albumin protein fractions and flours of African locust bean (Parkia biglobossa). Food Chemistry, 92(4), 681–691. doi:10.1016/j.foodchem.2004.08.043
  • Li, G.H., Le, G.W., Liu, H., & Shi, Y.H. (2005). Mung-bean protein hydrolysates obtained with alcalase exhibit angiotensin I-converting enzyme inhibitory activity. Food Science and Technology International, 11(4), 281–287. doi:10.1177/1082013205056781
  • Li, Y., Jiang, B., Zhang, T., Mu, W., & Liu, J. (2008). Antioxidant and free radical-scavenging activities of chickpea protein hydrolysate (CPH). Food Chemistry, 106(2), 444–450. doi:10.1016/j.foodchem.2007.04.067
  • Lin, C., & Zayas, J. (1987). Functionality of defatted corn germ proteins in a model system: Fat binding capacity and water retention. Journal of Food Science, 52(5), 1308–1311. doi:10.1111/jfds.1987.52.issue-5
  • Mao, X., & Hua, Y. (2012). Composition, structure and functional properties of protein concentrates and isolates produced from walnut (Juglans regia L.). International Journal of Molecular Sciences, 13(2), 1561–1581. doi:10.3390/ijms13021561
  • Meng, G., & Ma, C.-Y. (2002). Characterization of globulin from Phaseolus angularis (red bean). International Journal of Food Science & Technology, 37(6), 687–695. doi:10.1046/j.1365-2621.2002.00601.x
  • Molina, E., Papadopoulou, A., & Ledward, D.A. (2001). Emulsifying properties of high pressure treated soy protein isolate and 7S and 11S globulins. Food Hydrocolloids, 15(3), 263–269. doi:10.1016/S0268-005X(01)00023-6
  • Molina Ortiz, S.E., & Wagner, J.R. (2002). Hydrolysates of native and modified soy protein isolates: Structural characteristics, solubility and foaming properties. Food Research International, 35(6), 511–518. doi:10.1016/S0963-9969(01)00149-1
  • Navarrete-Tindall, N., & Aragon, H. (2002). Inga paterno harms. In: J. A. Vozzo (Ed.), Tropical tree seed manual: Part II, species descriptions.  Agriculture Handbook (pp. 523–525). Washington, DC: Department of Agriculture (USDA), Forest Service.
  • Ogunwolu, S.O., Henshaw, F.O., Mock, H.-P., Santros, A., & Awonorin, S.O. (2009). Functional properties of protein concentrates and isolates produced from cashew (Anacardium occidentale L.) nut. Food Chemistry, 115(3), 852–858. doi:10.1016/j.foodchem.2009.01.011
  • Osborne, T.B., & Mendel, L.B. (1914). Nutritive properties of proteins of the maize kernel. Journal of Biological Chemistry, 18, 1–16.
  • Oyaizu, M. (1986). Studies on products of browning reaction–antioxidative activities of products of browning reaction prepared from glucosamine. Eiyogaku Zasshi= Japanese Journal of Nutrition, 44, 307–315. doi:10.5264/eiyogakuzashi.44.307
  • Paredes-López, O., Ordorica-Falomir, C., & Olivares-Vázquez, M.R. (1991). Chickpea protein isolates: Physicochemical, functional and nutritional characterization. Journal of Food Science, 56(3), 726–729. doi:10.1111/j.1365-2621.1991.tb05367.x
  • Pedroche, J., Yust, M.M., Girón‐Calle, J., Alaiz, M., Millán, F., & Vioque, J. (2002). Utilisation of chickpea protein isolates for production of peptides with angiotensin I‐converting enzyme (ACE)‐inhibitory activity. Journal of the Science of Food and Agriculture, 82(9), 960–965. doi:10.1002/jsfa.v82:9
  • Pedroche, J., Yust, M.M., Lqari, H., Girón-Calle, J., Alaiz, M., Vioque, J., et al. (2004). Brassica carinata protein isolates: Chemical composition, protein characterization and improvement of functional properties by protein hydrolysis. Food Chemistry, 88(3), 337–346. doi:10.1016/j.foodchem.2004.01.045
  • Qayyum, M., Butt, M., Anjum, F., & Nawaz, H. (2012). Composition analysis of some selected legumes for protein isolates recovery. The Journal of Animal and Plant Sciences, 22(4), 1156–1162.
  • Ragab, D.M., Babiker, E.E., & Eltinay, A.H. (2004). Fractionation, solubility and functional properties of cowpea (Vigna unguiculata) proteins as affected by pH and/or salt concentration. Food Chemistry, 84(2), 207–212. doi:10.1016/S0308-8146(03)00203-6
  • Rakashanda, S., Mubashir, S., Qurishi, Y., Hamid, A., Masood, A., & Amin, S. (2013). Trypsin inhibitors from Lavatera cashmeriana Camb. seeds: Isolation, characterization and in-vitro cytoxicity activity. International Journal of Pharmaceutical Science Invention, 2(5), 55–65.
  • Rodríguez-Ambriz, S.L., Martínez-Ayala, A.L., Millán, F., & Dávila-Ortíz, G. (2005). Composition and functional properties of lupinus campestris protein isolates. Plant Foods for Human Nutrition, 60(3), 99–107. doi:10.1007/s11130-005-6835-z
  • Ruiz Ruiz, J., Segura Campos, M., Betancur Ancona, D., & Chel Guerrero, L. (2013). Proteínas y péptidos biológicamente activos con potencial nutracéutico. In M.S. Campos, L.C. Guerrero, & D.B. Ancona (Eds.), Bioactividad de péptidos derivados de proteínas alimentarias (pp. 11–27). Barcelona: OmniaScience.
  • Ruiz-Carrera, V., Peña-López, E., Lau-Vázquez, S., Maldonado-Mares, F., Ascencio-Rivera, J., & Guadarrama-Olivera, M. (2004). Macronutrimentos de fitorrecursos alimenticios de especies aprovechadas por grupos étnicos en Tabasco, México. Universidad Y Ciencia Número Especial, 1, 27–31.
  • Rutherfurd-Markwick, K.J., & Moughan, P.J. (2005). Bioactive peptides derived from food. Journal of AOAC International, 88(3), 955–966.
  • Sánchez-Vioque, R., Clemente, A., Vioque, J., Bautista, J., & Millán, F. (1999). Protein isolates from chickpea (Cicer arietinum L.): Chemical composition, functional properties and protein characterization. Food Chemistry, 64(2), 237–243. doi:10.1016/S0308-8146(98)00133-2
  • Sathe, S.K., Deshpande, S.S., & Salunkhe, D.K. (1982). Functional properties of lupin seed (Lupinus mutabilis) proteins and protein concentrates. Journal of Food Science, 47(2), 491–497. doi:10.1111/j.1365-2621.1982.tb10110.x
  • Singh, N., Kaur, M., & Sandhu, K.S. (2005). Physicochemical and functional properties of freeze-dried and oven dried corn gluten meals. Drying Technology, 23(4), 975–988. doi:10.1081/drt-200054253
  • Skeggs, L.T., Kahn, J.R., & Shumway, N.P. (1956). The preparation and function of the hypertensin-converting enzyme. The Journal of Experimental Medicine, 103(3), 295–299. doi:10.1084/jem.103.3.295
  • Sze-Tao, K.W.C., & Sathe, S.K. (2000). Functional properties and in vitro digestibility of almond (Prunus dulcis L.) protein isolate. Food Chemistry, 69(2), 153–160. doi:10.1016/S0308-8146(99)00244-7
  • Sze‐Tao, K.W.C., & Sathe, S.K. (2000). Walnuts (Juglans regia L): Proximate composition, protein solubility, protein amino acid composition and protein in vitro digestibility. Journal of the Science of Food and Agriculture, 80(9), 1393–1401. doi:10.1002/1097-0010(200007)80:9<1393::AID-JSFA653>3.0.CO;2-F
  • Tang, C.-H., Peng, J., Zhen, D.-W., & Chen, Z. (2009). Physicochemical and antioxidant properties of buckwheat (Fagopyrum esculentum Moench) protein hydrolysates. Food Chemistry, 115(2), 672–678. doi:10.1016/j.foodchem.2008.12.068
  • Tian, S. (1998). The isolation, modification and evaluation of field pea proteins and their applications in foods. (PhD thesis) Victoria University of Technology. Retrieved from http://vuir.vu.edu.au/id/eprint/15713
  • Torruco-Uco, J., Domínguez-Magaña, M., Davila-Ortiz, G., Martínez-Ayala, A., Chel-Guerrero, L., & Betancur-Ancona, D. (2008). Péptidos antihipertensivos, una alternativa de tratamiento de origen natural: Una revisión/Antihypertensive peptides, an alternative for treatment of natural origin: A review. CYTA – Journal of Food, 6(2), 158–168.
  • Wu, H., Wang, Q., Ma, T., & Ren, J. (2009). Comparative studies on the functional properties of various protein concentrate preparations of peanut protein. Food Research International, 42(3), 343–348. doi:10.1016/j.foodres.2008.12.006
  • Yu, J., Ahmedna, M., & Goktepe, I. (2007). Peanut protein concentrate: Production and functional properties as affected by processing. Food Chemistry, 103(1), 121–129. doi:10.1016/j.foodchem.2006.08.012
  • Zhu, K.-X., Sun, X.-H., Chen, Z.-C., Peng, W., Qian, H.-F., & Zhou, H.-M. (2010). Comparison of functional properties and secondary structures of defatted wheat germ proteins separated by reverse micelles and alkaline extraction and isoelectric precipitation. Food Chemistry, 123(4), 1163–1169. doi:10.1016/j.foodchem.2010.05.081
  • Zia-Ul-Haq, M., Iqbal, S., Ahmad, S., Imran, M., Niaz, A., & Bhanger, M.I. (2007). Nutritional and compositional study of Desi chickpea (Cicer arietinum L.) cultivars grown in Punjab, Pakistan. Food Chemistry, 105(4), 1357–1363. doi:10.1016/j.foodchem.2007.05.004