Changes in the structure and hydration properties of high-temperature peanut protein induced by cold plasma oxidation.
Int J Biol Macromol
; 253(Pt 7): 127500, 2023 Dec 31.
Article
em En
| MEDLINE
| ID: mdl-37858644
ABSTRACT
To improve the hydration properties of high-temperature pressed peanut protein isolate (HPPI), we investigated the effect of cold plasma (CP) oxidation on functional and structural properties. Compared to HPPI, the hydrated molecules number and the surface contact angle were significantly decreased at 70 W, from 77.2 × 109 to 17.7 × 109 and from 85.74° to 57.81°, respectively. The reduction of the sulfhydryl content and the increase of the disulfide bond and di-tyrosine content indicated that the structural transformation was affected by the oxidation effect. In terms of structural changes, a stretched tertiary structure, ordered secondary structure, and rough apparent structure were observed after CP treatment. Additionally, the enhancement of surface free energy and group content such as -COOH, -CO and -OH on the surface of HPPI contributed to the formation of hydrated crystal structures. In general, the oxidation effect of CP effectively improved the hydration properties of HPPI and broaden its application field.
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Texto completo:
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Base de dados:
MEDLINE
Assunto principal:
Arachis
/
Gases em Plasma
Idioma:
En
Ano de publicação:
2023
Tipo de documento:
Article