Comparative Characterization of Protein Hydrolysates from Three Edible Insects: Mealworm Larvae, Adult Crickets, and Silkworm Pupae
A comparative characterization of proteins from three edible insects—<i>Tenebrio molitor</i> (mealworm) larvae, <i>Gryllus bimaculatus</i> (cricket), and <i>Bombyx mori</i> (silkworm) pupae—was performed in this study. Proteins were extracted f...
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| Format: | Article |
| Language: | English |
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MDPI AG
2019-11-01
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| Series: | Foods |
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| Online Access: | https://www.mdpi.com/2304-8158/8/11/563 |
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| author | Sungwon Yoon Nathan A. K. Wong Minki Chae Joong-Hyuck Auh |
| author_facet | Sungwon Yoon Nathan A. K. Wong Minki Chae Joong-Hyuck Auh |
| author_sort | Sungwon Yoon |
| collection | DOAJ |
| description | A comparative characterization of proteins from three edible insects—<i>Tenebrio molitor</i> (mealworm) larvae, <i>Gryllus bimaculatus</i> (cricket), and <i>Bombyx mori</i> (silkworm) pupae—was performed in this study. Proteins were extracted from edible insects and their hydrolysates were prepared through enzymatic hydrolysis with commercial enzymes (Flavourzyme: 12%; Alcalase: 3%). Solubility was significantly higher following enzymatic hydrolysis, while foamability was lower compared to those of the protein control. Angiotensin-converting enzyme was significantly inhibited after enzymatic hydrolysis, especially following Alcalase treatment, with IC<sub>50</sub> values of 0.047, 0.066, and 0.065 mg/mL for <i>G. bimaculatus</i>, <i>T. molitor</i> larvae, and <i>B. mori</i> pupae, respectively. Moreover, the Alcalase-treated group of <i>B. mori</i> pupae and the <i>T. molitor</i> larvae group treated with a mixture of enzymes showed the effective inhibition of α-glucosidase activity. The anti-inflammatory activity of the insect hydrolysates was assessed via nitric oxide production from macrophages, and <i>B. mori</i> pupae samples exhibited significant activity regardless of the method of hydrolysis. These results indicate the functional properties of protein and hydrolysates from three species of edible insects, which may be useful in their future exploitation. |
| first_indexed | 2024-12-10T09:38:10Z |
| format | Article |
| id | doaj.art-38cac1e0fb8744f79956f188fcd539b2 |
| institution | Directory Open Access Journal |
| issn | 2304-8158 |
| language | English |
| last_indexed | 2024-12-10T09:38:10Z |
| publishDate | 2019-11-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Foods |
| spelling | doaj.art-38cac1e0fb8744f79956f188fcd539b22022-12-22T01:54:07ZengMDPI AGFoods2304-81582019-11-0181156310.3390/foods8110563foods8110563Comparative Characterization of Protein Hydrolysates from Three Edible Insects: Mealworm Larvae, Adult Crickets, and Silkworm PupaeSungwon Yoon0Nathan A. K. Wong1Minki Chae2Joong-Hyuck Auh3Department of Food Science and Technology, Chung-Ang University, Anseong 17546, KoreaDepartment of Food Science and Technology, Chung-Ang University, Anseong 17546, KoreaDepartment of Food Science and Technology, Chung-Ang University, Anseong 17546, KoreaDepartment of Food Science and Technology, Chung-Ang University, Anseong 17546, KoreaA comparative characterization of proteins from three edible insects—<i>Tenebrio molitor</i> (mealworm) larvae, <i>Gryllus bimaculatus</i> (cricket), and <i>Bombyx mori</i> (silkworm) pupae—was performed in this study. Proteins were extracted from edible insects and their hydrolysates were prepared through enzymatic hydrolysis with commercial enzymes (Flavourzyme: 12%; Alcalase: 3%). Solubility was significantly higher following enzymatic hydrolysis, while foamability was lower compared to those of the protein control. Angiotensin-converting enzyme was significantly inhibited after enzymatic hydrolysis, especially following Alcalase treatment, with IC<sub>50</sub> values of 0.047, 0.066, and 0.065 mg/mL for <i>G. bimaculatus</i>, <i>T. molitor</i> larvae, and <i>B. mori</i> pupae, respectively. Moreover, the Alcalase-treated group of <i>B. mori</i> pupae and the <i>T. molitor</i> larvae group treated with a mixture of enzymes showed the effective inhibition of α-glucosidase activity. The anti-inflammatory activity of the insect hydrolysates was assessed via nitric oxide production from macrophages, and <i>B. mori</i> pupae samples exhibited significant activity regardless of the method of hydrolysis. These results indicate the functional properties of protein and hydrolysates from three species of edible insects, which may be useful in their future exploitation.https://www.mdpi.com/2304-8158/8/11/563protein hydrolysatesmealwormcricketsilkworm pupae |
| spellingShingle | Sungwon Yoon Nathan A. K. Wong Minki Chae Joong-Hyuck Auh Comparative Characterization of Protein Hydrolysates from Three Edible Insects: Mealworm Larvae, Adult Crickets, and Silkworm Pupae Foods protein hydrolysates mealworm cricket silkworm pupae |
| title | Comparative Characterization of Protein Hydrolysates from Three Edible Insects: Mealworm Larvae, Adult Crickets, and Silkworm Pupae |
| title_full | Comparative Characterization of Protein Hydrolysates from Three Edible Insects: Mealworm Larvae, Adult Crickets, and Silkworm Pupae |
| title_fullStr | Comparative Characterization of Protein Hydrolysates from Three Edible Insects: Mealworm Larvae, Adult Crickets, and Silkworm Pupae |
| title_full_unstemmed | Comparative Characterization of Protein Hydrolysates from Three Edible Insects: Mealworm Larvae, Adult Crickets, and Silkworm Pupae |
| title_short | Comparative Characterization of Protein Hydrolysates from Three Edible Insects: Mealworm Larvae, Adult Crickets, and Silkworm Pupae |
| title_sort | comparative characterization of protein hydrolysates from three edible insects mealworm larvae adult crickets and silkworm pupae |
| topic | protein hydrolysates mealworm cricket silkworm pupae |
| url | https://www.mdpi.com/2304-8158/8/11/563 |
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