Sea bream bones and scales as a source of gelatin and ACE inhibitory peptides

被引:75
作者
Akagunduz, Yesim [1 ]
Mosquera, Mauricio [1 ]
Gimenez, Begona [1 ]
Aleman, Allen [1 ]
Montero, Pilar [1 ]
Carmen Gomez-Guillen, Maria [1 ]
机构
[1] CSIC, Inst Ciencia & Tecnol Alimentos & Nutr, Madrid INST28040, Spain
关键词
Scales; Bones; Fish gelatin; ACE-inhibitory peptides; Alcalase; I-CONVERTING-ENZYME; VISCOELASTIC PROPERTIES; BIOCHEMICAL-PROPERTIES; PROTEIN HYDROLYSATE; PHYSICAL-PROPERTIES; BLACK DRUM; COLLAGEN; SKIN; ACID; PURIFICATION;
D O I
10.1016/j.lwt.2013.10.026
中图分类号
TS2 [食品工业];
学科分类号
0832 ;
摘要
Sea bream scales and bones were used as sources of gelatin. Scales gave a higher gelatin yield than bones pretreated with HCl or Alcalase. Demineralization with EDTA was effective especially in the case of scale gelatin that showed the lowest ash content. The pretreatment of bones with HCl led to an increase in the removal of minerals. The gel strength and viscoelastic properties of sea bream scale gelatins were higher than those of bone gelatins, and only slight differences were found between gelatin extracted from bones pretreated with HCl or Alcalase, although the amino acid profile was similar in the three gelatins. The gel strength of scale gelatins was higher than that of a commercial bovine gelatin used for comparative purpose (Bloom 200-220). When the scales gelatin was hydrolyzed with Esperase, a high ACE-inhibitory activity was found in the peptide fraction below 3 kDa, and the amount of this peptide fraction required to inhibit 50% of the ACE activity (IC50) was around 60 mu g/mL. (C) 2013 Elsevier Ltd. All rights reserved.
引用
收藏
页码:579 / 585
页数:7
相关论文
共 46 条
  • [1] ADLERNISSEN J, 1977, PROCESS BIOCHEM, V12, P18
  • [2] Squid gelatin hydrolysates with antihypertensive, anticancer and antioxidant activity
    Aleman, A.
    Perez-Santin, E.
    Bordenave-Juchereau, S.
    Arnaudin, I.
    Gomez-Guillen, M. C.
    Montero, P.
    [J]. FOOD RESEARCH INTERNATIONAL, 2011, 44 (04) : 1044 - 1051
  • [3] ATKINSON AB, 1979, LANCET, V2, P836
  • [4] Purification and characterization of angiotensin I converting enzyme (ACE) inhibitory peptides from Alaska pollack (Theragra chalcogramma) skin
    Byun, HG
    Kim, SK
    [J]. PROCESS BIOCHEMISTRY, 2001, 36 (12) : 1155 - 1162
  • [5] Physicochemical and sensory characteristics of fish gelatin
    Choi, SS
    Regenstein, JM
    [J]. JOURNAL OF FOOD SCIENCE, 2000, 65 (02) : 194 - 199
  • [6] Optimizing angiotensin I-Converting enzyme inhibitory activity of pacific hake (Merluccius productus) fillet hydrolysate using response surface methodology and ultrafiltration
    Cinq-Mars, Crystal D.
    Li-Chan, Eunice C. Y.
    [J]. JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY, 2007, 55 (23) : 9380 - 9388
  • [7] The possible roles of food-derived bioactive peptides in reducing the risk of cardiovascular disease
    Erdmann, Kati
    Cheung, Belinda W. Y.
    Schroeder, Heirming
    [J]. JOURNAL OF NUTRITIONAL BIOCHEMISTRY, 2008, 19 (10) : 643 - 654
  • [8] Production of angiotensin I converting enzyme inhibitory peptides from sea bream scales
    Fahmi, A
    Morimura, S
    Guo, HC
    Shigematsu, T
    Kida, K
    Uemura, Y
    [J]. PROCESS BIOCHEMISTRY, 2004, 39 (10) : 1195 - 1200
  • [9] EXTENSION OF A MODEL FOR CROSSLINKING POLYMER AT THE GEL POINT
    FRIEDRICH, C
    HEYMANN, L
    [J]. JOURNAL OF RHEOLOGY, 1988, 32 (03) : 235 - 241
  • [10] Influence of hydrolysis degree on the functional properties of salmon byproducts hydrolysates
    Gbogouri, GA
    Linder, M
    Fanni, J
    Parmentier, M
    [J]. JOURNAL OF FOOD SCIENCE, 2004, 69 (08) : C615 - C622