Your browser doesn't support javascript.
loading
Effect of pH-Shifting Process on the Cathepsin Activity, Muddy Off-Odor Compounds' Content and Gelling Properties of Isolated Protein from Silver Carp.
Guo, Weidan; Zhan, Miao; Liu, Hui; Fu, Xiangjin; Wu, Wei.
Afiliação
  • Guo W; College of Food Science and Engineering, Central South University of Forestry and Technology, Changsha 410004, China.
  • Zhan M; College of Food Science and Engineering, Central South University of Forestry and Technology, Changsha 410004, China.
  • Liu H; College of Food Science and Engineering, Central South University of Forestry and Technology, Changsha 410004, China.
  • Fu X; College of Food Science and Engineering, Central South University of Forestry and Technology, Changsha 410004, China.
  • Wu W; Hunan Provincial Key Laboratory of Processed Food for Special Medical Purpose, Changsha 410004, China.
Foods ; 12(5)2023 Feb 22.
Article em En | MEDLINE | ID: mdl-36900456
ABSTRACT
Silver carp (Hypophthalmichthys molitrix) is a potential source for making surimi products. However, it has the disadvantages of bony structures, high level of cathepsines and muddy off-odor which is mainly caused by geosmin (GEO) and 2-methylisoborneol (MIB). These disadvantages make the conventional water washing process of surimi inefficient (low protein recovery rate, and high residual muddy off-odor). Thus, the effect of the pH-shifting process (acid-isolating process and alkali-isolating process) on the cathepsins activity, GEO content, MIB content, and gelling properties of the isolated proteins (IPs) was investigated, comparing it with surimi obtained through the conventional cold water washing process (WM). The alkali-isolating process greatly boosted the protein recovery rate from 28.8% to 40.9% (p < 0.05). In addition, it removed 84% GEO and 90% MIB. The acid-isolating process removed about 77% GEO and 83% MIB. The acid-isolated protein (AC) displayed the lowest elastic modulus (G'), the highest TCA-peptide content (90.89 ± 4.65 mg/g) and the highest cathepsin L activity (65.43 ± 4.91 U/g). The AC modori (60 °C for 30 min) gel also demonstrated the lowest breaking force (226.2 ± 19.5 g) and breaking deformation (8.3 ± 0.4 mm), indicating that proteolysis caused by the cathepsin deteriorated the gel quality of AC. The setting (40 °C for 30 min) considerably increased the breaking force (386.4 ± 15.7 g) and breaking deformation (11.6 ± 0.2 mm) of the gel made from the alkali-isolated protein (AK) (p < 0.05). In AC and AK gel, a clearly visible cross-linking protein band with a molecular weight greater than MHC was seen, demonstrating the presence of endogenous trans-glutaminase (TGase) activity, that improved the gel quality of AK. In conclusion, the alkali-isolating process was an effective alternative method for making water-washed surimi from silver carp.
Palavras-chave

Texto completo: 1 Base de dados: MEDLINE Idioma: En Ano de publicação: 2023 Tipo de documento: Article

Texto completo: 1 Base de dados: MEDLINE Idioma: En Ano de publicação: 2023 Tipo de documento: Article