Effect of Polyphenols of Aronia melanocarpa on the Gel Properties of Fish Surimi
CSTR:
Author:
Affiliation:

(1.College of Food Science and Technology, Hebei Normal University of Science and Technology, Changli 066600, Hebei;2.Hebei Fruit Processing Technology Innovation Center, Changli 066600, Hebei)

Clc Number:

Fund Project:

  • Article
  • |
  • Figures
  • |
  • Metrics
  • |
  • Reference
  • |
  • Related
  • |
  • Cited by
  • |
  • Materials
  • |
  • Comments
    Abstract:

    In order to improve the quality and taste of freshwater fish surimi products, fourier transform infrared spectroscopy, low field nuclear magnetic resonance and scanning electron microscopy were used to explore the effects of different levels of Aronia melanocarpa polyphenols on surimi gel properties, and the water retention, whole texture, chemical force, total sulfhydryl content, relaxation time, protein secondary structure and scanning electron microscopy of surimi gel were measured. The results showed that when the content of polyphenols was 0.375%, surimi gel had the best water holding capacity, gel properties, elasticity, and chewability. In the relaxation spectrum, the peak of the group with 0.375% of polyphenols was the highest and shifted to the left the most, indicating that the surimi gel with 0.375% of polyphenols had the most difficult flowing water and promoted structural stability. In the scanning electron microscope, the structure of surimi gel became denser with the increase of polyphenol addition. The surimi gel in 0.375% group was the densest with smooth surface. When the amount of polyphenol added increased to 0.500%, the structure of surimi gel became loose again. The disulfide bond in the chemical force gradually increased and was inversely proportional to the total sulfhydryl content. The disulfide bond hydrophobic interaction played an important role in surimi gel. Fourier transform infrared spectroscopy indicated that alpha helical structure gradually transformed into a beta folded structure, and the area of the beta folded peak gradually increased indicating that the protein secondary structure of the protein was more regular and orderly, which promoted the enhancement of surimi gel properties. In SDS-PAGE, myosin heavy chain (MHC) and actin (AC) of surimi gel gradually weakened, indicating that a stable surimi gel network structure was formed.

    Reference
    Related
    Cited by
Get Citation
Share
Article Metrics
  • Abstract:
  • PDF:
  • HTML:
  • Cited by:
History
  • Received:November 24,2023
  • Revised:
  • Adopted:
  • Online: December 25,2024
  • Published:
Article QR Code
Copyright :Journal of Chinese Institute of Food Science and Technology     京ICP备09084417号-4
Address :9/F, No. 8 North 3rd Street, Fucheng Road, Haidian District, Beijing, China      Postal code :100048
Telephone :010-65223596 65265376      E-mail :chinaspxb@vip.163.com
Supported by : Beijing E-Tiller Technology Development Co., Ltd.