Antioxidant and functional properties of gelatin hydrolysates obtained from skin of sole and squid

被引:252
作者
Gimenez, B. [1 ]
Aleman, A. [1 ]
Montero, P. [1 ]
Gomez-Guillen, M. C. [1 ]
机构
[1] CSIC, Inst Frio, E-28040 Madrid, Spain
关键词
Gelatin hydrolysates; Antioxidant properties; Functional properties; EMULSIFYING PROPERTIES; PROTEIN; PEPTIDES; MUSCLE; COLLAGEN; DIGESTS; EXTRACT; PH;
D O I
10.1016/j.foodchem.2008.10.050
中图分类号
O69 [应用化学];
学科分类号
070301 [无机化学];
摘要
Antioxidant and functional properties were evaluated for gelatin hydrolysates obtained from sole and squid skin gelatin by Alcalase. with a degree of hydrolysis of similar to 35% and similar to 50%, respectively. Both hydrolysates mainly consisted of peptides below 6.5 kDa, together with peptidic material from around 16 to 6.5 kDa. Moreover, the squid hydrolysate showed a peptide band of around 26 kDa. Antioxidant properties of both gelatins were highly increased by hydrolysis, especially ABTS and metal chelating abilities, The squid hydrolysate showed the highest antioxidant capacity by FRAP, ABTS and metal chelating assays in spite of the lower content in hydrophobic amino acids. Both gelatin hydrolysates had a good solubility (over 95%). The emulsifying activity index (EAI) decreased with increasing concentration. Conversely, the foam expansion increased with increasing concentration. However, both foam and emulsion stabilities were not apparently affected by the concentration of hydrolysate. In the case of the sole hydrolysate, which showed a lower degree Pro and Lys hydroxylation, foam stability was very poor, and 50% of foam expansion was lost after 5 min at all concentrations. (C) 2008 Elsevier Ltd. All rights reserved.
引用
收藏
页码:976 / 983
页数:8
相关论文
共 52 条
[1]
ALDERNISSEN J, 1986, ENZYMIC HYDROLYSIS F, P110
[2]
Antioxidant activity of peptide fractions of capelin protein hydrolysates [J].
Amarowicz, R ;
Shahidi, F .
FOOD CHEMISTRY, 1997, 58 (04) :355-359
[3]
[4]
[Anonymous], [No title captured], Patent No. [WO 2004/071202, 2004071202]
[5]
[Anonymous], J AGR FOOD CHEM
[6]
The ferric reducing ability of plasma (FRAP) as a measure of ''antioxidant power'': The FRAP assay [J].
Benzie, IFF ;
Strain, JJ .
ANALYTICAL BIOCHEMISTRY, 1996, 239 (01) :70-76
[7]
Antioxidant activity of designed peptides based on the antioxidative peptide isolated from digests of a soybean protein [J].
Chen, HM ;
Muramoto, K ;
Yamauchi, F ;
Nokihara, K .
JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY, 1996, 44 (09) :2619-2623
[8]
Antioxidative properties of histidine-containing peptides designed from peptide fragments found in the digests of a soybean protein [J].
Chen, HM ;
Muramoto, K ;
Yamauchi, F ;
Fujimoto, K ;
Nokihara, K .
JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY, 1998, 46 (01) :49-53
[9]
Antioxidative activity and safety of the 50% ethanolic extract from red bean fermented by Bacillus subtilis IMR-NK1 [J].
Chung, YC ;
Chang, CT ;
Chao, WW ;
Lin, CF ;
Chou, ST .
JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY, 2002, 50 (08) :2454-2458
[10]
Dickinson E, 1994, FOOD MACROMOL COLLOI, P201