Language : English
Songwen Tan

论文成果

Encapsulation of caffeine in spray-dried micro-eggs for controlled release: The effect of spray-drying (cooking) temperature

Affiliation of Author(s):The University of Sydney

Journal:Food Hydrocolloids

Key Words:Caffeine Egg albumen Spray-drying temperature Microencapsulation Controlled release Release model

Abstract:This work has found that the spray-drying temperature affects the microencapsulation and release behaviour ofcaffeine from spray-dried egg albumen in the form of a powder (“micro-eggs”, filled in a gelatine capsule), not in the form of compressed tablets. The spray-dried micro-eggs are more spherical when spray-dried at 60–120 ℃ but are more crumpled when spray-dried at 140–200℃, which is related to the critical denaturation temperature of 56 ℃ for egg albumen. At low inlet temperatures, the particle size of spray-dried micro-eggs and the yield are small while the free moisture content is high. A free moisture content of less than 4.2% is required for high yields. FTIR-ATR (for surface analysis) and Raman (for bulk analysis) spectra indicate greater surface enrichment of protein for higher inlet temperatures. DSC spectra show greater denaturation of protein for the spray-dried micro-eggs produced at higher inlet temperatures, and the spectra also suggest that caffeine is amorphous in the spray-dried micro-eggs. Moreover, the release rate of caffeine has been controlled by changing the inlet temperature. The releases last for 2.5–14 h with inlet temperatures of 60–200 ℃. The release profiles have been found to fit the first-order, Higuchi, Hixson-Crowell, and Korsmeyer-Peppas release models, well. The release mechanisms of caffeine are suggested to be non-Fickian (more release occurs when the protein matrices areeroded) for the spray-dried micro-eggs produced at low inlet temperatures, whereas Fick’s law (corresponding to the molecular diffusion of caffeine) is followed more closely for the spray-dried micro-eggs denatured/cooked at high inlet temperatures, due to the characteristics of the protein shell.

Volume:108

Issue:2020

Translation or Not:no

Links to published journals:https://doi.org/10.1016/j.foodhyd.2020.105979