Structural, physicochemical, and immune-enhancing properties of edible insect protein isolates from Protaetia brevitarsis larvae
Edible insects are promising future food resources globally. Herein, the structural, physicochemical, and bio-functional properties of edible insect protein isolates (EPIs) extracted from Protaetia brevitarsis larvae were investigated. The results showed that EPIs have a high total essential amino a...
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| Format: | Article |
| Language: | English |
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Elsevier
2023-06-01
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| Series: | Food Chemistry: X |
| Subjects: | |
| Online Access: | http://www.sciencedirect.com/science/article/pii/S2590157523001657 |
| _version_ | 1797798674406834176 |
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| author | Jae Hoon Lee Tae-Kyung Kim Yun Jeong Kim Min-Cheol Kang Kyung-Mo Song Bum-Keun Kim Yun-Sang Choi |
| author_facet | Jae Hoon Lee Tae-Kyung Kim Yun Jeong Kim Min-Cheol Kang Kyung-Mo Song Bum-Keun Kim Yun-Sang Choi |
| author_sort | Jae Hoon Lee |
| collection | DOAJ |
| description | Edible insects are promising future food resources globally. Herein, the structural, physicochemical, and bio-functional properties of edible insect protein isolates (EPIs) extracted from Protaetia brevitarsis larvae were investigated. The results showed that EPIs have a high total essential amino acid content; moreover, β-sheet is the major secondary protein structure. The EPI protein solution was highly soluble and electrically stable and did not aggregate easily. In addition, EPIs exhibited immune-enhancing properties; EPI treatment of macrophages induced the activation of macrophages and consequently promoted the production of pro-inflammatory mediators (NO, TNF-α, and IL-1β). Moreover, macrophage activation of EPIs was confirmed to occur through the MAPK and NF-κB pathways. In conclusion, our results suggest that the isolated P. brevitarsis protein can be fully utilized as a functional food material and alternative protein source in the future food industry. |
| first_indexed | 2024-03-13T04:07:25Z |
| format | Article |
| id | doaj.art-80da69f4a97e472db7836788c3cdfa63 |
| institution | Directory Open Access Journal |
| issn | 2590-1575 |
| language | English |
| last_indexed | 2024-03-13T04:07:25Z |
| publishDate | 2023-06-01 |
| publisher | Elsevier |
| record_format | Article |
| series | Food Chemistry: X |
| spelling | doaj.art-80da69f4a97e472db7836788c3cdfa632023-06-21T06:59:39ZengElsevierFood Chemistry: X2590-15752023-06-0118100722Structural, physicochemical, and immune-enhancing properties of edible insect protein isolates from Protaetia brevitarsis larvaeJae Hoon Lee0Tae-Kyung Kim1Yun Jeong Kim2Min-Cheol Kang3Kyung-Mo Song4Bum-Keun Kim5Yun-Sang Choi6Research Group of Food Processing, Korea Food Research Institute, Wanju 55365, Republic of KoreaResearch Group of Food Processing, Korea Food Research Institute, Wanju 55365, Republic of KoreaResearch Group of Food Processing, Korea Food Research Institute, Wanju 55365, Republic of Korea; Department of Food Biotechnology, University of Science and Technology, Daejeon 34113, Republic of KoreaResearch Group of Food Processing, Korea Food Research Institute, Wanju 55365, Republic of KoreaResearch Group of Food Processing, Korea Food Research Institute, Wanju 55365, Republic of KoreaResearch Group of Food Processing, Korea Food Research Institute, Wanju 55365, Republic of Korea; Department of Food Biotechnology, University of Science and Technology, Daejeon 34113, Republic of KoreaResearch Group of Food Processing, Korea Food Research Institute, Wanju 55365, Republic of Korea; Corresponding author.Edible insects are promising future food resources globally. Herein, the structural, physicochemical, and bio-functional properties of edible insect protein isolates (EPIs) extracted from Protaetia brevitarsis larvae were investigated. The results showed that EPIs have a high total essential amino acid content; moreover, β-sheet is the major secondary protein structure. The EPI protein solution was highly soluble and electrically stable and did not aggregate easily. In addition, EPIs exhibited immune-enhancing properties; EPI treatment of macrophages induced the activation of macrophages and consequently promoted the production of pro-inflammatory mediators (NO, TNF-α, and IL-1β). Moreover, macrophage activation of EPIs was confirmed to occur through the MAPK and NF-κB pathways. In conclusion, our results suggest that the isolated P. brevitarsis protein can be fully utilized as a functional food material and alternative protein source in the future food industry.http://www.sciencedirect.com/science/article/pii/S2590157523001657Edible insect proteinProtaetia brevitarsisStructural propertyPhysicochemical propertiesImmune-enhancing property |
| spellingShingle | Jae Hoon Lee Tae-Kyung Kim Yun Jeong Kim Min-Cheol Kang Kyung-Mo Song Bum-Keun Kim Yun-Sang Choi Structural, physicochemical, and immune-enhancing properties of edible insect protein isolates from Protaetia brevitarsis larvae Food Chemistry: X Edible insect protein Protaetia brevitarsis Structural property Physicochemical properties Immune-enhancing property |
| title | Structural, physicochemical, and immune-enhancing properties of edible insect protein isolates from Protaetia brevitarsis larvae |
| title_full | Structural, physicochemical, and immune-enhancing properties of edible insect protein isolates from Protaetia brevitarsis larvae |
| title_fullStr | Structural, physicochemical, and immune-enhancing properties of edible insect protein isolates from Protaetia brevitarsis larvae |
| title_full_unstemmed | Structural, physicochemical, and immune-enhancing properties of edible insect protein isolates from Protaetia brevitarsis larvae |
| title_short | Structural, physicochemical, and immune-enhancing properties of edible insect protein isolates from Protaetia brevitarsis larvae |
| title_sort | structural physicochemical and immune enhancing properties of edible insect protein isolates from protaetia brevitarsis larvae |
| topic | Edible insect protein Protaetia brevitarsis Structural property Physicochemical properties Immune-enhancing property |
| url | http://www.sciencedirect.com/science/article/pii/S2590157523001657 |
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