Heat-induced gelation of protein from mealworm (Tenebrio molitor): influence of pH and zinc concentration
Mealworm protein has the general potential to substitute environmentally less favourable, animal derived raw-materials as a gelling biomaterial for zinc enriched wound healing ointments. However, various factors affecting heat-induced gelation of mealworm protein have not yet been studied in detail....
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| Format: | Article |
| Language: | English |
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Elsevier
2022-12-01
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| Series: | Food Hydrocolloids for Health |
| Subjects: | |
| Online Access: | http://www.sciencedirect.com/science/article/pii/S2667025922000516 |
| _version_ | 1811207802095403008 |
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| author | Martina Klost Maria Isabel Ramirez-Huerta Stephan Drusch |
| author_facet | Martina Klost Maria Isabel Ramirez-Huerta Stephan Drusch |
| author_sort | Martina Klost |
| collection | DOAJ |
| description | Mealworm protein has the general potential to substitute environmentally less favourable, animal derived raw-materials as a gelling biomaterial for zinc enriched wound healing ointments. However, various factors affecting heat-induced gelation of mealworm protein have not yet been studied in detail. Therefore, we investigated the influence of pH (pH 5.5 and 7.5) and zinc concentration (0 M, 0.1 M and 0.3 M) on rheological properties and gel structure of heat-induced mealworm protein gels. Additionally, we used gel solubility experiments and rheological investigations to study the gels with regard to the involved types of interactions. Generally, all examined samples were able to form heat-induced gels. From gel solubility experiments and temperature sweeps, hydrophobic interactions and hydrogen bonds were found to be dominant in all samples. From higher storage moduli we derive the contribution of additional electrostatic and/or covalent interactions in samples with ZnSO4, while shorter linear viscoelastic regimes and more pronounced intracycle strain stiffening were related to less homogenous and more particulate gel structures. From our results strategies for the customisation of gel properties and gel composition may be deduced, that may advance the potential for future utilisation of mealworm protein in wound dressings. |
| first_indexed | 2024-04-12T04:11:05Z |
| format | Article |
| id | doaj.art-7b9f16abd7994b10a79c7df9b442f041 |
| institution | Directory Open Access Journal |
| issn | 2667-0259 |
| language | English |
| last_indexed | 2024-04-12T04:11:05Z |
| publishDate | 2022-12-01 |
| publisher | Elsevier |
| record_format | Article |
| series | Food Hydrocolloids for Health |
| spelling | doaj.art-7b9f16abd7994b10a79c7df9b442f0412022-12-22T03:48:31ZengElsevierFood Hydrocolloids for Health2667-02592022-12-012100105Heat-induced gelation of protein from mealworm (Tenebrio molitor): influence of pH and zinc concentrationMartina Klost0Maria Isabel Ramirez-Huerta1Stephan Drusch2Corresponding author.; Technische Universität Berlin, Faculty III Process Sciences, Institute for Food Technology and Food Chemistry, Department of Food Technology and Food Material Science, Straße des 17. Juni 135, Berlin 10623, GermanyTechnische Universität Berlin, Faculty III Process Sciences, Institute for Food Technology and Food Chemistry, Department of Food Technology and Food Material Science, Straße des 17. Juni 135, Berlin 10623, GermanyTechnische Universität Berlin, Faculty III Process Sciences, Institute for Food Technology and Food Chemistry, Department of Food Technology and Food Material Science, Straße des 17. Juni 135, Berlin 10623, GermanyMealworm protein has the general potential to substitute environmentally less favourable, animal derived raw-materials as a gelling biomaterial for zinc enriched wound healing ointments. However, various factors affecting heat-induced gelation of mealworm protein have not yet been studied in detail. Therefore, we investigated the influence of pH (pH 5.5 and 7.5) and zinc concentration (0 M, 0.1 M and 0.3 M) on rheological properties and gel structure of heat-induced mealworm protein gels. Additionally, we used gel solubility experiments and rheological investigations to study the gels with regard to the involved types of interactions. Generally, all examined samples were able to form heat-induced gels. From gel solubility experiments and temperature sweeps, hydrophobic interactions and hydrogen bonds were found to be dominant in all samples. From higher storage moduli we derive the contribution of additional electrostatic and/or covalent interactions in samples with ZnSO4, while shorter linear viscoelastic regimes and more pronounced intracycle strain stiffening were related to less homogenous and more particulate gel structures. From our results strategies for the customisation of gel properties and gel composition may be deduced, that may advance the potential for future utilisation of mealworm protein in wound dressings.http://www.sciencedirect.com/science/article/pii/S2667025922000516RheologyGel solubilityWound healingZincDivalent cationsInsects |
| spellingShingle | Martina Klost Maria Isabel Ramirez-Huerta Stephan Drusch Heat-induced gelation of protein from mealworm (Tenebrio molitor): influence of pH and zinc concentration Food Hydrocolloids for Health Rheology Gel solubility Wound healing Zinc Divalent cations Insects |
| title | Heat-induced gelation of protein from mealworm (Tenebrio molitor): influence of pH and zinc concentration |
| title_full | Heat-induced gelation of protein from mealworm (Tenebrio molitor): influence of pH and zinc concentration |
| title_fullStr | Heat-induced gelation of protein from mealworm (Tenebrio molitor): influence of pH and zinc concentration |
| title_full_unstemmed | Heat-induced gelation of protein from mealworm (Tenebrio molitor): influence of pH and zinc concentration |
| title_short | Heat-induced gelation of protein from mealworm (Tenebrio molitor): influence of pH and zinc concentration |
| title_sort | heat induced gelation of protein from mealworm tenebrio molitor influence of ph and zinc concentration |
| topic | Rheology Gel solubility Wound healing Zinc Divalent cations Insects |
| url | http://www.sciencedirect.com/science/article/pii/S2667025922000516 |
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