Journal
FOOD HYDROCOLLOIDS
Volume 91, Issue -, Pages 117-126Publisher
ELSEVIER SCI LTD
DOI: 10.1016/j.foodhyd.2019.01.017
Keywords
Edible insects; Apis mellifera; Gel; Coagulation; Protein; Novel food
Categories
Funding
- Israel Ministry of Agriculture and Rural Development [21-4200022]
Ask authors/readers for more resources
Edible insects offer a huge potential as a new source of proteins for food and feed and as a promising functional agent. In this regard, our study aimed to evaluate the effect of pH and temperature on aggregation and gelation of honey bee brood (Apis mellifera). Aggregation of soluble proteins was dependent on temperature and pH value and the highest coagulation was reached at 85 degrees C at pH 5 and 7 (73.7 and 68.4%, respectively). Changes in protein surface hydrophobicity, net charge and amount of available and buried sulfhydryl groups demonstrated the contribution of either covalent or non-covalent intermolecular interactions resulted in aggregation at various pH. The least gelation concentration of raw powder from honey bee brood varied from 5 to 11% on raw powder basis at pH 7 and 3, respectively. Moreover, the effect of pH on rheological and textural properties, as well as gel microstructure from honey bee brood is discussed. Therefore, freeze dried raw powder of honey bee brood has rich nutritional value and demonstrated gelation concentration comparable to conventional protein sources that reveal its potential as an ingredient for insect-based gel product.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available