Enhancing the thermal stability of soy proteins by preheat treatment at lower protein concentration. (15th February 2020)
- Record Type:
- Journal Article
- Title:
- Enhancing the thermal stability of soy proteins by preheat treatment at lower protein concentration. (15th February 2020)
- Main Title:
- Enhancing the thermal stability of soy proteins by preheat treatment at lower protein concentration
- Authors:
- Ma, Wuchao
Wang, Tao
Wang, Jiamei
Wu, Di
Wu, Chao
Du, Ming - Abstract:
- Highlights: Preheating at lower concentration produce heat stable soy proteins. Larger particles were induced via disulfide bonds and hydrophobic interaction. Smaller particles were obtained by heating at lower concentration and higher pH. Heat stable soy proteins possess larger unfolding extent. Abstract: The heat-induced aggregation of edible proteins has been regarded as one of the critical challenges for their application in protein-enriched beverages. Therefore, the formulation of thermal stable proteins to improve the stability of these beverages upon heating is highly desired. In this study, soy proteins (SPs) with enhanced heat stability were obtained by low-concentration-preheating (LCPH). Results from reheating of the above samples showed that pretreatment of SPs at low concentrations (≤1.0%, w/v) increased their resistance against aggregation. Additionally, when the suspensions of the particles were reheated at 10% (w/v) protein concentration, no gelation was found for samples prepared by LCPH, indicating collapsed protein–protein interactions, whereas gelled suspensions were obtained for native SPs and samples prepared by preheating at higher protein concentrations (≥2.0%, w/v). Furthermore, suspensions of particles prepared at lower protein concentration showed lower viscosities and higher flow behavior index values before and after reheat treatment. These findings highlighted that LCPH would provide fundamental information on the application of SPs in highHighlights: Preheating at lower concentration produce heat stable soy proteins. Larger particles were induced via disulfide bonds and hydrophobic interaction. Smaller particles were obtained by heating at lower concentration and higher pH. Heat stable soy proteins possess larger unfolding extent. Abstract: The heat-induced aggregation of edible proteins has been regarded as one of the critical challenges for their application in protein-enriched beverages. Therefore, the formulation of thermal stable proteins to improve the stability of these beverages upon heating is highly desired. In this study, soy proteins (SPs) with enhanced heat stability were obtained by low-concentration-preheating (LCPH). Results from reheating of the above samples showed that pretreatment of SPs at low concentrations (≤1.0%, w/v) increased their resistance against aggregation. Additionally, when the suspensions of the particles were reheated at 10% (w/v) protein concentration, no gelation was found for samples prepared by LCPH, indicating collapsed protein–protein interactions, whereas gelled suspensions were obtained for native SPs and samples prepared by preheating at higher protein concentrations (≥2.0%, w/v). Furthermore, suspensions of particles prepared at lower protein concentration showed lower viscosities and higher flow behavior index values before and after reheat treatment. These findings highlighted that LCPH would provide fundamental information on the application of SPs in high protein beverages. … (more)
- Is Part Of:
- Food chemistry. Volume 306(2020)
- Journal:
- Food chemistry
- Issue:
- Volume 306(2020)
- Issue Display:
- Volume 306, Issue 2020 (2020)
- Year:
- 2020
- Volume:
- 306
- Issue:
- 2020
- Issue Sort Value:
- 2020-0306-2020-0000
- Page Start:
- Page End:
- Publication Date:
- 2020-02-15
- Subjects:
- Aggregation -- Heat stability -- Low-concentration-preheating -- Soy protein
Food -- Analysis -- Periodicals
Food -- Composition -- Periodicals
664 - Journal URLs:
- http://www.sciencedirect.com/science/journal/03088146 ↗
http://www.elsevier.com/journals ↗ - DOI:
- 10.1016/j.foodchem.2019.125593 ↗
- Languages:
- English
- ISSNs:
- 0308-8146
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 3977.284000
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British Library HMNTS - ELD Digital store - Ingest File:
- 11893.xml