2019
DOI: 10.5851/kosfa.2019.e24
|View full text |Cite
|
Sign up to set email alerts
|

Effects of Heating Time and Temperature on Functional Properties of Proteins of Yellow Mealworm Larvae (Tenebrio molitor L.)

Abstract: Although the yellow mealworm ( Tenebrio molitor L.) is a promising alternative protein source, the effects of processing conditions on functional properties are unclear. In this study, a protein extract of yellow mealworm larvae (PEYM) was subjected to different heat temperature (55°C, 75°C, and 95°C) with different time (20, 40, and 60 min) to evaluate the functional properties and protein oxidation. Different heat temperature treatment significantly affected the exposure of surface hyd… Show more

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
2
1
1
1

Citation Types

8
27
0
1

Year Published

2020
2020
2024
2024

Publication Types

Select...
7
2
1

Relationship

0
10

Authors

Journals

citations
Cited by 54 publications
(36 citation statements)
references
References 36 publications
8
27
0
1
Order By: Relevance
“…The EC and ES of non-fermented mealworm powder are in line with those of other studies on mealworm flours [9,33]. In addition, their emulsification properties were not significantly different from commercial egg albumen powder, indicating its potential as an alternative source of protein emulsifier for food formulations.…”
Section: Emulsion Capacity and Stabilitysupporting
confidence: 88%
“…The EC and ES of non-fermented mealworm powder are in line with those of other studies on mealworm flours [9,33]. In addition, their emulsification properties were not significantly different from commercial egg albumen powder, indicating its potential as an alternative source of protein emulsifier for food formulations.…”
Section: Emulsion Capacity and Stabilitysupporting
confidence: 88%
“…The EC and ES of non-fermented mealworm powder are in line with those of other studies on mealworm flours (Lee et al, 2019; Zielińska et al, 2018). In addition, their emulsification properties were not significantly different from commercial egg albumen powder, indicating its potential as alternative source of protein emulsifier for food formulations.…”
Section: Resultssupporting
confidence: 90%
“…The decreasing solubility of PPI may be due to the structure denaturation of PPI caused by high temperature drying, which increased exposure of hydrophobic groups and reduced the protein-water interactions. These results corresponded with the studies of Ziegler et al 42 and Lee et al 43 .…”
Section: Functional Properties Of Peanut Protein Isolate Ppisupporting
confidence: 93%