Alcalase assisted production of novel high alpha-chain gelatin and the functional stability of its hydrogel as influenced by thermal treatment

Int J Biol Macromol. 2018 Oct 15;118(Pt B):2278-2286. doi: 10.1016/j.ijbiomac.2018.07.114. Epub 2018 Jul 18.

Abstract

High alpha-chain (α-chain) content is associated with superior quality gelatin. In this study, a production process involving mild alcalase treatment was optimized by response surface methodology, and the α-chain was quantified based on SDS-PAGE. A novel fish skin gelatin high in α-chain (32% of total protein, 45 mg/g fish skin of yield) was produced at optimum conditions, i.e., 2.3 U/g alcalase addition to fish skin for 0.5 h at 25 °C, followed by water extraction at 67 °C for 7 h. The novel gelatin contained 34% glycine and 16% imino acids as determined by UPLC. FTIR analysis disclosed four characteristic infra-red amide absorption bands. DSC and TGA analysis revealed thermal decomposition at 215 °C. Novel gelatin hydrogel (1%, w/v) could withstand a wide range of temperatures, and exhibited high emulsifying activity and viscosity, as well as stable gel clarity from 35 °C to 80 °C. The high temperature treatment (95 °C) produced hydrogel with lower clarity and emulsifying activity but higher viscosity than at the other temperatures. All heat-treated gelatin hydrogels behaved as non-Newtonian fluids as per the Ostwald de Waele model. The novel high α-chain fish skin gelatin has potential broad application in food, pharmaceutical and biological industries.

Keywords: Alpha-chain gelatin; Enzymatic; Functional properties of hydrogels.

MeSH terms

  • Amino Acids / analysis
  • Animals
  • Emulsions / chemistry
  • Fishes
  • Gelatin / metabolism*
  • Hydrogels / chemistry*
  • Rheology
  • Skin / chemistry
  • Spectroscopy, Fourier Transform Infrared
  • Subtilisins / metabolism*
  • Temperature*
  • Viscosity

Substances

  • Amino Acids
  • Emulsions
  • Hydrogels
  • Gelatin
  • Subtilisins