AI Article Synopsis
- Ovalbumin (OVA) is a widely studied protein, but its low gelation properties limit its use in food processing.
- Researchers developed a method combining succinylation and pH-shifting to create highly transparent and elastic hydrogels from pre-treated OVA, leading to a significant increase in elasticity (507.14%) and water holding capacity (60.74%).
- The treatment improved protein structure, enabling better intermolecular interactions, resulting in superior gelation properties compared to untreated OVA hydrogels.
Article Abstract
Ovalbumin (OVA) is a model protein with extensive research on structure and function, however, the application of OVA in food processing is limited due to its low gelation properties. In this study, thermally-induced highly transparent and elastic hydrogels from OVA pretreated by succinylation combined with pH-shifting method were reported. Transmission electron microscope (TEM) and free sulfhydryl groups determination revealed that the pretreatment induced the stretching of the protein structure and promoted the formation of preliminary aggregates. Further heating the pretreated OVA suspension resulted in a homogeneous and macroporous gel network with thin connecting walls. Such homogeneous gel network structures may be related to the effective modulation of the thermal aggregation efficiency of proteins by succinylation and the high level of protein unfolding by pH-shifting treatments, which synergistically allowed for more active sites to be created during heating to facilitate intermolecular interactions, including hydrogen bonding and hydrophobic interactions. Notably, the method resulted in a 507.14% increase in elasticity, a 60.74% increase in water holding capacity of the OVA hydrogels compared to the native OVA hydrogels without pretreatment. Also, the hydrogels were transparent with 73.11% light transmittance. In conclusion, succinylation and pH-shifting combined treatment could be an effective method for the preparation of OVA hydrogels with superior gelation properties.
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| http://dx.doi.org/10.1016/j.foodres.2022.112174 | DOI Listing |
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