Effect of Mechanically Deboned Chicken Meat Hydrolysates on the Physicochemical Properties of Imitation Fish Paste

被引:9
作者
Jin, Sang-Keun [1 ]
Go, Gwang-woong [1 ]
Jung, Eun-Young [1 ]
Lim, Hyun-Jung [1 ]
Yang, Han-Sul [1 ]
Park, Jae-Hong [1 ]
机构
[1] Gyeongnam Natl Univ Sci & Technol, Dept Anim Resources Technol, Jinju 660758, Gyeongnam, South Korea
来源
ASIAN-AUSTRALASIAN JOURNAL OF ANIMAL SCIENCES | 2014年 / 27卷 / 01期
基金
新加坡国家研究基金会;
关键词
Surimi; Imitation Fish Paste; Mechanically Deboned Chicken Meat Hydrolysates; Gel Properties; Lipid Oxidation; I-CONVERTING-ENZYME; LIPID OXIDATION; SOY PROTEIN; ANTIOXIDANT ACTIVITY; GEL PROPERTIES; SURIMI; PEPTIDES; WATER; BEEF; FRANKFURTERS;
D O I
10.5713/ajas.2013.13284
中图分类号
S8 [畜牧、 动物医学、狩猎、蚕、蜂];
学科分类号
0905 ;
摘要
This study investigated on the effects of adding mechanically deboned chicken meat (MDCM) hydrolysates on the quality properties of imitation fish paste (IFP) during storage. IFP was prepared from Alaska Pollack, spent laying hens surimi and protein hydrolysates which were enzymatically extracted from MDCM. The study was designed as a 3x4 factorial design with three MDCM hydrolysate content groups (0%, 0.4%, and 0.8%) and four storage times (0, 2, 4, and 6 weeks). Addition of MDCM hydrolysates increased crude fat content but lowered water content (p<0.05). The breaking force of IFP, an indicator of gel formation, increased in treated groups compared to control (p<0.05). Angiotensin I-converting enzyme (ACE) activity was inhibited and free radical scavenging activity increased with increasing MDCM hydrolysate content (p<0.05). In conclusion, the addition of MDCM to IFP improves gel characteristics. Additionally, protein hydrolysates from MDCM serve as a potential source of ACE inhibiting peptides.
引用
收藏
页码:115 / 122
页数:8
相关论文
共 44 条
  • [1] AHHMED MA, 2009, P 55 INT C MEAT SCI
  • [2] OXYGEN AVAILABILITY AFFECTS PROOXIDANT CATALYZED LIPID OXIDATION OF COOKED TURKEY PATTIES
    AHN, DU
    AJUYAH, A
    WOLFE, FH
    SIM, JS
    [J]. JOURNAL OF FOOD SCIENCE, 1993, 58 (02) : 278 - +
  • [3] [Anonymous], 1987, J Assoc Anal Chem, V70, P393
  • [4] [Anonymous], 2000, SAS/STAT User's Guide
  • [5] Peptide inhibitors for angiotensin I-converting enzyme from enzymatic hydrolysates of porcine skeletal muscle proteins
    Arihara, K
    Nakashima, Y
    Mukai, T
    Ishikawa, S
    Itoh, M
    [J]. MEAT SCIENCE, 2001, 57 (03) : 319 - 324
  • [6] Antioxidants from a heated histidine-glucose model system. I: Investigation of the antioxidant role of histidine and isolation of antioxidants by high-performance liquid chromatography
    Bersuder, P
    Hole, M
    Smith, G
    [J]. JOURNAL OF THE AMERICAN OIL CHEMISTS SOCIETY, 1998, 75 (02) : 181 - 187
  • [7] Utilization of meat industry by products: Protein hydrolysate from sheep visceral mass
    Bhaskar, N.
    Modi, V. K.
    Govindaraju, K.
    Radha, C.
    Lalitha, R. G.
    [J]. BIORESOURCE TECHNOLOGY, 2007, 98 (02) : 388 - 394
  • [8] Buege J A, 1978, Methods Enzymol, V52, P302
  • [9] New antibacterial peptide derived from bovine hemoglobin
    Daoud, R
    Dubois, V
    Bors-Dodita, L
    Nedjar-Arroume, N
    Krier, F
    Chihib, NE
    Mary, P
    Kouach, M
    Briand, G
    Guillochon, D
    [J]. PEPTIDES, 2005, 26 (05) : 713 - 719
  • [10] Angiotensin I-Converting Enzyme Inhibitory Peptides Generated from in Vitro Gastrointestinal Digestion of Pork Meat
    Escudero, Elizabeth
    Angel Sentandreu, Miguel
    Arihara, Keizo
    Toldra, Fidel
    [J]. JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY, 2010, 58 (05) : 2895 - 2901