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Abstract

Based on the preparation of sesame peptides, the effect of Maillard reaction on antioxidant activity of sesame polypeptides was studied. The results showed that the suitable ratio of peptide to sugar was 1∶2 for Maillard reaction of sesame polypeptide. The Maillard reaction could significantly improve the antioxidant activity of sesame polypeptide, and the reducing power, ABTS+ radical scavenging rate, DPPH radical scavenging rate and hydroxyl radical scavenging rate were increased by 121.4%, 304.5%, 81.2% and 103.2%, respectively. The contents of lysine methionine and tyrosine were reduced, but the contents of alanine and valine were increased, moreover, aspartic acid, glutamic acid, cysteine and glycine were produced by Maillard reaction of sesame peptides. Browning degree and graft degree increased with the prolongation of Maillard reaction time. When the reaction was carried out for 4 hours, the browning degree and graft degree were 1.42%and 26.4% respectively. The Maillard reaction products have absorption peaks at 210 nm and 260 nm, and with the increase of reaction time, the absorption peak intensity was increased gradually. It was related to the change of peptide bond and the increase of melanoidin content in the Maillard reaction products. Therefore, the Maillard reaction had a certain effect on the antioxidant activity of sesame peptides.

Publication Date

8-28-2018

First Page

24

Last Page

28,88

DOI

10.13652/j.issn.1003-5788.2018.08.006

References

[1] LPEZ-FANDIO R, OTTE J, CAMP J V. Physiological, chemical and technological aspects of milk-protein-derived peptides with antihypertensive and ACE-inhibitory activity[J]. International Dairy Journal, 2006, 16(11): 1 277-1 293.
[2] 彭惠惠, 李吕木, 钱坤, 等. 发酵芝麻粕中芝麻小肽的分离纯化及其体外抗氧化活性[J]. 食品科学, 2013, 34(9): 66-69.
[3] 李旸, 张莉, 陈文帮, 等. 发酵芝麻粕小肽体内抗氧化和免疫活性[J]. 食品科学, 2014, 35(19): 251-254.
[4] KIM D Y, SHIN W S. Functional improvements in bovine serum albumin-fucoidan conjugate through the Maillard reaction[J]. Food Chemistry, 2016, 190: 974-981.
[5] JAEGER H, JANOSITZ A, KNORR D. The Maillard reaction and its control during food processing. The potential of emerging technologies[J]. Pathologie Biologie, 2010, 58(3): 207-213.
[6] DITTRICH R, DRAGONAS C, KANNENKERIL D, et al. A diet rich in Maillard reaction products protects LDL against copper induced oxidation ex vivo, a human intervention trial[J]. Food Research International, 2009, 42(9): 1 315-1 322.
[7] 陈贵堂, 周琼飞, 朱艳丽, 等. 采用美拉德反应提高灰树花多肽的抗氧化活性[J]. 食品科学, 2013, 34(14): 26-29.
[8] 赵谋明, 刘洋, 张佳男, 等. 木糖-草鱼肽美拉德反应产物的抗氧化性[J]. 农业工程学报, 2014, 30(9): 279-286.
[9] MATMAROH K, BENJAKUL S, TANAKA M. Effect of reactant concentrations on the Maillard reaction in a fructose-glycine model system and the inhibition of black tiger shrimp polyphenoloxidase[J]. Food Chemistry, 2006, 98(1): 1-8.
[10] LI Xi-can, LIN Jing, GAO Yao-xiang, et al. Antioxidant activity and mechanism of Rhizoma Cimicifugae[J]. Chemistry Central Journal, 2012, 6(1): 1-10.
[11] AI S, TANABE S, NISHIMURA T. Antioxidant Activity of Peptides Obtained from Porcine Myofibrillar Proteins by Protease Treatment[J]. Journal of Agricultural & Food Chemistry, 2003, 51(12): 3 661-3 667.
[12] CHEN Hua-ming, MURAMOTO K, YAMAUCHI F, et al. Antioxidative properties of histidine-containing peptides designed from peptide fragments found in the digests of a soybean protein[J]. Journal of Agricultural & Food Chemistry, 1998, 46(1): 49-53.
[13] CORZO-MART-NEZ M, MONTILLA A, MEG-AS-PREZ R, et al. Impact of high-intensity ultrasound on the formation of lactulose and Maillard reaction glycoconjugates[J]. Food Chemistry, 2014, 157(8): 186-192.
[14] JIANG Zhan-mei, WANG Li-zhe, WU Wei, et al. Biological activities and physicochemical properties of Maillard reaction products in sugar-bovine casein peptide model systems[J]. Food Chemistry, 2013, 141(4): 3 837-3 845.
[15] WANG Wen-qiong, BAO Yi-hong, CHEN Ying. Characteris-tics and antioxidant activity of water-soluble Maillard reaction products from interactions in a whey protein isolate and sugars system[J]. Food Chemistry, 2013, 139(1/2/3/4): 355-361.
[16] JIANG Zhan-mei, WANG Li-zhe, CHE Hong-xia, et al. Effects of temperature and pH on angiotensin-I-converting enzyme inhibitory activity and physicochemical properties of bovine casein peptide in aqueous Maillard reaction system[J]. LWT-Food Science and Technology, 2014, 59(1): 35-42.
[17] ZENG Yan, ZHANG Xiao-xi, GUAN Yu-ping, et al. Characteristics and antioxidant activity of Maillard reaction products from psicose-lysine and fructose-lysine model systems[J]. Journal of Food Science, 2011, 76(3): C398-C403.
[18] JIANG Zhan-mei, RAI D K, O'CONNOR P M, et al. Heat-induced Maillard reaction of the tripeptide IPP and ribose: Structural characterization and implication on bioactivity[J]. Food Research International, 2013, 50(1): 266-274.
[19] 张严, 汪何雅, 钱和. 美拉德反应产物的褐变、荧光吸收及抗氧化性的研究[J]. 食品工业科技, 2012, 33(6): 193-196.
[20] 卢彬, 王忠合, 王军, 等. 温度对金带细鲹鱼肉水解物美拉德反应及其产物抗氧化性的影响[J]. 食品与机械, 2015, 31(1): 25-29.
[21] VHANGANI L N, VAN W J. Antioxidant activity of Maillard reaction products (MRPs) derived from fructose-lysine and ribose-lysine model systems[J]. Food Chemistry, 2013, 137(1/2/3/4): 92-98.
[22] KUCHLYAN J, KUNDU N, BANIK D, et al. Spectroscopy and fluorescence lifetime imaging microscopy to probe the interaction of bovine serum albumin with graphene oxide[J]. Langmuir the Acs Journal of Surfaces & Colloids, 2015, 31(51): 13 793-13 801.
[23] KIM J S, LEE Y S. Enolization and racemization reactions of glucose and fructose on heating with amino-acid enantiomers and the formation of melanoidins as a result of the Maillard reaction[J]. Amino Acids, 2008, 108(2): 582-592.

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