Journal of Food and Nutrition Research
ISSN (Print): 2333-1119 ISSN (Online): 2333-1240 Website: Editor-in-chief: Prabhat Kumar Mandal
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Journal of Food and Nutrition Research. 2013, 1(6), 138-144
DOI: 10.12691/jfnr-1-6-5
Open AccessArticle

Comparison the Chemical and Functional Properties of Protein Hydrolysates from Different Mature Degree Hawk Teas

Xuejing Jia1, Chunbang Ding1, Lihua Dong1, Shu Yuan2, Zhongwei Zhang2, Yanger Chen1 and Ming Yuan1,

1College of Life and Basic Sciences, Sichuan Agricultural University, Ya’an, China

2College of Resources and Environmental Science, Sichuan Agricultural University, Chengdu, China

Pub. Date: December 05, 2013

Cite this paper:
Xuejing Jia, Chunbang Ding, Lihua Dong, Shu Yuan, Zhongwei Zhang, Yanger Chen and Ming Yuan. Comparison the Chemical and Functional Properties of Protein Hydrolysates from Different Mature Degree Hawk Teas. Journal of Food and Nutrition Research. 2013; 1(6):138-144. doi: 10.12691/jfnr-1-6-5


Hawk tea is one of the most popular beverage in southwest of China. In the present study, the effects of alkaline protease on the formation and characteristics of protein hydrolysates from different mature degree Hawk teas were investigated. For antioxidant activity in vitro, Hawk mature leaf tea protein hydrolysates (MPH) had the strongest 2, 2-diphenyl-1-picryl-hydrazyl (DPPH) radical scavenging activity and reducing power. And MPH also showed the highest iron chelating activity among the three samples. With regard to functional property, MPH and Hawk primary leaf tea protein hydrolysates (PPH) had higher solubility than that of Hawk bud tea protein hydrolysates (BPH). And the same trend was found in emulsifying property. The amino acid composition of MPH, PPH and BPH was very dissimilar. MPH and PPH mainly contained low molecular weight peptides, while BPH majorly included high molecular weight peptides. MPH may have potential applications in food industries as natural antioxidants.

Hawk tea antioxidant activity metal chelating activity functional property amino acid composition

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[1]  Young, I.S. and J.V. Woodside, “Antioxidants in health and disease,” Journal of Clinical Pathology, 54(3), 176-186, 2001.
[2]  Deetae, P., P. Parichanon, P. Trakunleewatthana, C. Chanseetis, and S. Lertsiri, “Antioxidant and anti-glycation properties of Thai herbal teas in comparison with conventional teas,” Food Chemistry, 133(3), 953-959, 2012.
[3]  Maryline Abert Vian, Z.H., A.S. Fabiano-Tixier, M. Elmaataoui, O. Dangles, and F. Chemat, “A remarkable influence of microwave extraction: Enhancement of antioxidant activity of extracted onion varieties,” Food Chemistry, 127(4), 1472-1480, 2011.
[4]  Najafian, L. and A.S. Babji, “A review of fish-derived antioxidant and antimicrobial peptides: their production, assessment, and applications,” Peptides, 33(1), 178-185, 2011.
[5]  Vercruysse, L., J. Van Camp, and G. Smagghe, “ACE inhibitory peptides derived from enzymatic hydrolysates of animal muscle protein: a review,” Journal of Agricultural and Food Chemistry, 53(21), 8106-8115, 2005.
[6]  Pihlanto-Leppälä, A., “Bioactive peptides derived from bovine whey proteins: opioid and ace-inhibitory peptides,” Trends in Food Science & Technology, 11(9), 347-356, 2000.
[7]  Gauthier, S.F., Y. Pouliot, and D. Saint-Sauveur, “Immunomodulatory peptides obtained by the enzymatic hydrolysis of whey proteins,” International Dairy Journal, 16(11), 1315-1323, 2006.
[8]  Intarasirisawat, R., S. Benjakul, W. Visessanguan, and J.P. Wu, “Antioxidative and functional properties of protein hydrolysate from defatted skipjack (Katsuwonous pelamis) roe,” Food Chemistry, 135(4), 3039-3048, 2012.
[9]  Sarmadi, B.H. and A. Ismail, “Antioxidative peptides from food proteins: A review,” Peptides, 31(10), 1949-1956, 2010.
[10]  Zhao, Q., H. Xiong, C. Selomulya, X.D. Chen, H.L. Zhong, S.Q. Wang, W.J. Sun, and Q. Zhou, “Enzymatic hydrolysis of rice dreg protein: Effects of enzyme type on the functional properties and antioxidant activities of recovered proteins,” Food Chemistry, 134(3), 1360-1367, 2012.
[11]  Jia, X.J., L.H. Dong, Y. Yang, S. Yuan, Z.W. Zhang, and M. Yuan, “Preliminary structural characterization and antioxidant activities of polysaccharides extracted from Hawk tea (Litsea coreana var. lanuginosa),” Carbohydrate Polymers, 95(1), 195-199, 2013.
[12]  Carrasco-Castilla, J., A.J. Hernández-Álvarez, C. Jiménez-Martínez, C. Jacinto-Hernández, M. Alaiz, J. Girón-Calle, J. Vioque, and G. Dávila-Ortiz, “Antioxidant and metal chelating activities of peptide fractions from phaseolin and bean protein hydrolysates,” Food Chemistry, 135(3), 1789-1795, 2012.
[13]  Carrasco-Castilla, J., A.J. Hernández-Álvarez, C. Jiménez-Martínez, C. Jacinto-Hernández, M. Alaiz, J. Girón-Calle, J. Vioque, and G. Dávila-Ortiz, “Antioxidant and metal chelating activities of Phaseolus vulgaris L. var. Jamapa protein isolates, phaseolin and lectin hydrolysates,” Food Chemistry, 131(4), 1157-1164, 2012.
[14]  Razali, N., R. Razab, S.M. Junit, and A.A. Aziz, “Radical scavenging and reducing properties of extracts of cashew shoots,” Food Chemistry, 111(1), 38-44, 2008.
[15]  Zhu, K.X., C.X. Lian, X.N. Guo, W. Peng, and H.M. Zhou, “Antioxidant activities and total phenolic contents of various extracts from defatted wheat germ,” Food Chemistry, 126(3), 1122-1126, 2011.
[16]  He, R., A.T. Girgih, S.A. Malomo, X.R. Ju, and R.E. Aluko, “Antioxidant activities of enzymatic rapeseed protein hydrolysates and the membrane ultrafiltration fractions,” Journal of Functional Foods, 5(1), 219-227, 2013.
[17]  Castellani, O., V. Martinet, E. David-Briand, C. Guerin-Dubiard, and M. Anton, “Egg yolk phosvitin: preparation of metal-free purified protein by fast protein liquid chromatography using aqueous solvents,” Journal of Chromatography B, 791(1), 273-284, 2003.
[18]  Adler-Nissen, J., “Determination of the degree of hydrolysis of food protein hydrolysates by trinitrobenzenesulfonic acid,” Journal of Agricultural and Food Chemistry, 27(6), 1256-1262, 1979.
[19]  Li, X., H. Xiong, K.W. Yang, D.W. Peng, H.L. Peng, and Q. Zhao, “Optimization of the biological processing of rice dregs into nutritional peptides with the aid of trypsin,” Journal of Food Science and Technology, 49(5), 537-546, 2012.
[20]  Saiga, A., S. Tanabe, and T. Nishimura, “Antioxidant activity of peptides obtained from porcine myofibrillar proteins by protease treatment,” Journal of Agricultural and Food Chemistry, 51(12), 3661-3667, 2003.
[21]  Kim, E.K., S.J. Lee, B.T. Jeon, S.H. Moon, B. Kim, T.K. Park, J.S. Han, and P.J. Park, “Purification and characterisation of antioxidative peptides from enzymatic hydrolysates of venison protein,” Food Chemistry, 114(4), 1365-1370, 2009.
[22]  Wu, H.C., H.M. Chen, and C.Y. Shiau, “Free amino acids and peptides as related to antioxidant properties in protein hydrolysates of mackerel (Scomber austriasicus),” Food Research International, 36(9), 949-957, 2003.
[23]  Kumar, N.S.S., R.A. Nazeer, and R. Jaiganesh, “Purification and identification of antioxidant peptides from the skin protein hydrolysate of two marine fishes, horse mackerel (Magalaspis cordyla) and croaker (Otolithes ruber),” Amino Acids, 42(5), 1641-1649, 2012.
[24]  Pownall, T.L., C.C. Udenigwe, and R.E. Aluko, “Amino acid composition and antioxidant properties of pea seed (Pisum sativum L.) enzymatic protein hydrolysate fractions,” Journal of Agricultural and Food Chemistry, 58(8), 4712-4718, 2010.
[25]  Chen, N., H.M. Yang, Y. Sun, J. Niu, and S.Y. Liu, “Purification and identification of antioxidant peptides from walnut (Juglans regia L.) protein hydrolysates,” Peptides, 38(2), 344-349, 2012.
[26]  Peng, X.Y., B.H. Kong, X.F. Xia, and Q. Liu, “Reducing and radical-scavenging activities of whey protein hydrolysates prepared with Alcalase,” International Dairy Journal, 20(5), 360-365, 2010.
[27]  Storcksdieck, S., G. Bonsmann, and R.F. Hurrell, “Iron-binding properties, amino acid composition, and structure of muscle tissue peptides from in vitro digestion of different meat sources,” Journal of Food Science, 72(1), S019-S029, 2007.
[28]  Trevino, S.R., J.M. Scholtz, and C.N. Pace, “Amino acid contribution to protein solubility: Asp, Glu, and Ser contribute more favorably than the other hydrophilic amino acids in RNase Sa,” Journal of Molecular Biology, 366(2), 449-460, 2007.
[29]  Ktari, N., M. Jridi, I. Bkhairia, N. Sayari, R.B. Salah, and M. Nasri, “Functionalities and antioxidant properties of protein hydrolysates from muscle of zebra blenny (Salaria basilisca) obtained with different crude protease extracts,” Food Research International, 49(2), 747-756, 2012.
[30]  Chobert, J.M., C. Bertrand-Harb, and M.G. Nicolas, “Solubility and emulsifying properties of caseins and whey proteins modified enzymically by trypsin,” Journal of Agricultural and Food Chemistry, 36(5), 883-892, 1988.