Binding of aroma compounds with soy protein isolate in aqueous model: Effect of preheat treatment of soy protein isolate
| Autor: | Zhiyong He, Maomao Zeng, Jie Chen, Shengfang Wu, Jun Guo |
|---|---|
| Rok vydání: | 2018 |
| Předmět: |
Hot Temperature
Linalyl acetate 01 natural sciences Analytical Chemistry chemistry.chemical_compound 0404 agricultural biotechnology Linalool Hexyl acetate Soy protein Aroma Chromatography biology 010401 analytical chemistry Water 04 agricultural and veterinary sciences General Medicine biology.organism_classification 040401 food science 0104 chemical sciences Flavoring Agents chemistry Myrcene Soybean Proteins Heptyl acetate Geraniol Food Science Protein Binding |
| Zdroj: | Food chemistry. 290 |
| ISSN: | 1873-7072 |
| Popis: | The interactions between flavors (hexyl acetate [HxAc], heptyl acetate [HpAc], linalyl formate [LiFo], linalyl acetate [LiAc], geraniol, linalool, limonene and myrcene) and soy protein isolate (SPI) were investigated, the influence of flavors structure and preheated SPI (PSPI) were determined by using headspace solid-phase microextraction gas chromatography-mass spectrometry (HS-SPME/GC-MS) technology. For HxAc and HpAc, the binding of SPI and the flavors decreased in the order nature 80 °C 90 °C 100 °C PSPI, for LiFo, LiAc, geraniol, and linalool, nature 80 °C 90 °C 100 °C PSPI. For limonene and myrcene, an increase in headspace concentration or "salting out" effect was noticed. The NSPI (nature SPI) and PSPI of 80 °C showed two class binding sites for HxAc and HpAc. These results serve as a foundation for further investigation into the effect of preheating of SPI on its ability to bind to flavor-inducing compounds. |
| Databáze: | OpenAIRE |
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