Characterization of <i>Tenebrio molitor</i> Larvae Protein Preparations Obtained by Different Extraction Approaches
Edible insects have recently attracted research attention due to their nutritional value and low environmental footprint. <i>Tenebrio molitor</i> larva was the first insect species to be classified by European Food Safety Authority (EFSA) as safe for human consumption. However, it is tho...
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| Format: | Article |
| Language: | English |
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MDPI AG
2022-11-01
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| Series: | Foods |
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| Online Access: | https://www.mdpi.com/2304-8158/11/23/3852 |
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| author | Alkmini-Anna Gkinali Anthia Matsakidou Adamantini Paraskevopoulou |
| author_facet | Alkmini-Anna Gkinali Anthia Matsakidou Adamantini Paraskevopoulou |
| author_sort | Alkmini-Anna Gkinali |
| collection | DOAJ |
| description | Edible insects have recently attracted research attention due to their nutritional value and low environmental footprint. <i>Tenebrio molitor</i> larva was the first insect species to be classified by European Food Safety Authority (EFSA) as safe for human consumption. However, it is thought that the incorporation of edible insect as an ingredient in a food product would be more appealing to consumers than being visible. The aim of the present study was to determine the physicochemical properties of the larvae meal and protein concentrates. Different methods to extract and recover proteins from defatted (DF) <i>Tenebrio molitor</i> larvae were applied; i.e., alkaline extraction (DF-ASP); isoelectric precipitation after alkaline extraction (DF-AIP); and NaCl treatment (DF-SSP), and the obtained protein fractions were characterized. The DF-ASP exhibited the highest protein extraction/recovery efficiency (>60%), while it was the most effective in decreasing the interfacial tension at the oil/water (<i>o/w</i>) interface. The DF-AIP had the highest protein content (75.1%) and absolute values of <b><i>ζ</i></b>-potential and the best ability to retain water (10.54 g/g) and stabilize emulsions at pH 3.0. The DF-SSP protein preparation had the highest oil binding capacity (8.62%) and solubility (~88%) at acidic pHs and the highest emulsifying activity (~86 m<sup>2</sup>/g). Electrophoresis of the protein preparations revealed proteins with different molecular weights, while the protein secondary structure was dominated by <i>β</i>-structures and <i>α</i>-helix. Protein concentrates with different properties were able to be recovered from <i>Tenebrio molitor</i> larvae, that could affect their interactions with other food ingredients and their behavior during processing or storage. These findings would be valuable guidance for the technological exploitation of larvae protein preparations in the development of food formulations. |
| first_indexed | 2024-03-09T17:47:42Z |
| format | Article |
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| institution | Directory Open Access Journal |
| issn | 2304-8158 |
| language | English |
| last_indexed | 2024-03-09T17:47:42Z |
| publishDate | 2022-11-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Foods |
| spelling | doaj.art-a9d7c1b740e54fbdbd67eea3547722662023-11-24T10:59:39ZengMDPI AGFoods2304-81582022-11-011123385210.3390/foods11233852Characterization of <i>Tenebrio molitor</i> Larvae Protein Preparations Obtained by Different Extraction ApproachesAlkmini-Anna Gkinali0Anthia Matsakidou1Adamantini Paraskevopoulou2Laboratory of Food Chemistry and Technology, School of Chemistry, Aristotle University of Thessaloniki, 54124 Thessaloniki, GreeceLaboratory of Food Chemistry and Technology, School of Chemistry, Aristotle University of Thessaloniki, 54124 Thessaloniki, GreeceLaboratory of Food Chemistry and Technology, School of Chemistry, Aristotle University of Thessaloniki, 54124 Thessaloniki, GreeceEdible insects have recently attracted research attention due to their nutritional value and low environmental footprint. <i>Tenebrio molitor</i> larva was the first insect species to be classified by European Food Safety Authority (EFSA) as safe for human consumption. However, it is thought that the incorporation of edible insect as an ingredient in a food product would be more appealing to consumers than being visible. The aim of the present study was to determine the physicochemical properties of the larvae meal and protein concentrates. Different methods to extract and recover proteins from defatted (DF) <i>Tenebrio molitor</i> larvae were applied; i.e., alkaline extraction (DF-ASP); isoelectric precipitation after alkaline extraction (DF-AIP); and NaCl treatment (DF-SSP), and the obtained protein fractions were characterized. The DF-ASP exhibited the highest protein extraction/recovery efficiency (>60%), while it was the most effective in decreasing the interfacial tension at the oil/water (<i>o/w</i>) interface. The DF-AIP had the highest protein content (75.1%) and absolute values of <b><i>ζ</i></b>-potential and the best ability to retain water (10.54 g/g) and stabilize emulsions at pH 3.0. The DF-SSP protein preparation had the highest oil binding capacity (8.62%) and solubility (~88%) at acidic pHs and the highest emulsifying activity (~86 m<sup>2</sup>/g). Electrophoresis of the protein preparations revealed proteins with different molecular weights, while the protein secondary structure was dominated by <i>β</i>-structures and <i>α</i>-helix. Protein concentrates with different properties were able to be recovered from <i>Tenebrio molitor</i> larvae, that could affect their interactions with other food ingredients and their behavior during processing or storage. These findings would be valuable guidance for the technological exploitation of larvae protein preparations in the development of food formulations.https://www.mdpi.com/2304-8158/11/23/3852<i>Tenebrio molitor</i>protein extractionphysicochemical propertiesfunctional propertiessecondary structure |
| spellingShingle | Alkmini-Anna Gkinali Anthia Matsakidou Adamantini Paraskevopoulou Characterization of <i>Tenebrio molitor</i> Larvae Protein Preparations Obtained by Different Extraction Approaches Foods <i>Tenebrio molitor</i> protein extraction physicochemical properties functional properties secondary structure |
| title | Characterization of <i>Tenebrio molitor</i> Larvae Protein Preparations Obtained by Different Extraction Approaches |
| title_full | Characterization of <i>Tenebrio molitor</i> Larvae Protein Preparations Obtained by Different Extraction Approaches |
| title_fullStr | Characterization of <i>Tenebrio molitor</i> Larvae Protein Preparations Obtained by Different Extraction Approaches |
| title_full_unstemmed | Characterization of <i>Tenebrio molitor</i> Larvae Protein Preparations Obtained by Different Extraction Approaches |
| title_short | Characterization of <i>Tenebrio molitor</i> Larvae Protein Preparations Obtained by Different Extraction Approaches |
| title_sort | characterization of i tenebrio molitor i larvae protein preparations obtained by different extraction approaches |
| topic | <i>Tenebrio molitor</i> protein extraction physicochemical properties functional properties secondary structure |
| url | https://www.mdpi.com/2304-8158/11/23/3852 |
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