| Literature DB >> 33091981 |
Yongli Jiang1, Yifan Zhu1, Yuanrong Zheng2, Zhenmin Liu2, Yu Zhong3, Yun Deng1, Yanyun Zhao4.
Abstract
Tenebrio molitor larvae protein isolates (TPIs) were extracted using the alkaline extraction and acid precipitation methods (AEAP) assisted by NaCl (salting-in) and (NH4)2SO4 (salting-out) procedures. The structural, physicochemical, and functional properties of TPIs were investigated. It was found that the salt-assisted treatments did not affect the total amino acid content but altered specific amino acid compositions. The salting-in-AEAP extraction resulted in non-significant (P > 0.05) differences in zeta potential, hydrophobicity, thermal stability, solubility and foaming capacity compared with the AEAP extraction. Salting-out-AEAP extraction significantly (P < 0.05) increased overall protein solubility, emulsion activity, foaming capacity and stability that were associated with lower hydrophobicity, higher zeta potential, α-helix and disulfide bond contents. The salting-in-AEAP-out extraction generated the greatest protein yield (39.54%), emulsion activity index (55.5 m2/g), foaming capacity (205%) as well as foaming stability (65.59%).Entities:
Keywords: Functional properties; Protein; Salting-assisted extraction; Structure; Tenebrio molitor
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Year: 2020 PMID: 33091981 DOI: 10.1016/j.foodchem.2020.128158
Source DB: PubMed Journal: Food Chem ISSN: 0308-8146 Impact factor: 7.514