Effects of calcium or sodium ions on the properties of whey protein isolate-lotus root amylopectin composite gel. (February 2019)
- Record Type:
- Journal Article
- Title:
- Effects of calcium or sodium ions on the properties of whey protein isolate-lotus root amylopectin composite gel. (February 2019)
- Main Title:
- Effects of calcium or sodium ions on the properties of whey protein isolate-lotus root amylopectin composite gel
- Authors:
- Liu, Kang
Li, Qiang-Ming
Zha, Xue-Qiang
Pan, Li-Hua
Bao, Li-Juan
Zhang, Hai-Lin
Luo, Jian-Ping - Abstract:
- Abstract: The aim of this study was to investigate the effects of Ca 2+ and Na + on the properties of whey protein isolate (WPI)-lotus root amylopectin (LRA) composite gel system. Results showed that an appropriate concentration of these two salt ions can induce the formation of WPI-LRA composite gel. Compared to the gel with free of Ca 2+, the gel strength, water holding capacity and thermal transition temperature were enhanced by 2.2-fold, 3.4% and 1.9 °C, respectively, when 0.1 M CaCl2 were added to the gel system. With respect to Na +, 0.05 M was found to be an appropriate dosage for the formation of WPI-LRA composite gel. Under this concentration, the gel strength, water holding capacity and thermal transition temperature were enhanced by 2-fold, 2.2%, 2.8 °C, respectively. The storage modulus of WPI-LRA was changed by the addition of Ca 2+ or Na + . The analysis of scanning electron microscopy revealed that both Ca 2+ at 0.1 M and Na + at 0.05 M induced a compact and stable network of WPI-LRA composite gels. In addition, the measurement of reactive sulfhydryl group (SH) content and Fourier transform infrared spectroscopy were performed to investigate the gel formation mechanism induced by the two salt ions. Results indicated that the increase in the contents of SH, the changes in the protein as indicated by the relative peak areas of amide II band might be the main reason for ion-induced formation of WPI-LRA composite gel. These results obtained in the present workAbstract: The aim of this study was to investigate the effects of Ca 2+ and Na + on the properties of whey protein isolate (WPI)-lotus root amylopectin (LRA) composite gel system. Results showed that an appropriate concentration of these two salt ions can induce the formation of WPI-LRA composite gel. Compared to the gel with free of Ca 2+, the gel strength, water holding capacity and thermal transition temperature were enhanced by 2.2-fold, 3.4% and 1.9 °C, respectively, when 0.1 M CaCl2 were added to the gel system. With respect to Na +, 0.05 M was found to be an appropriate dosage for the formation of WPI-LRA composite gel. Under this concentration, the gel strength, water holding capacity and thermal transition temperature were enhanced by 2-fold, 2.2%, 2.8 °C, respectively. The storage modulus of WPI-LRA was changed by the addition of Ca 2+ or Na + . The analysis of scanning electron microscopy revealed that both Ca 2+ at 0.1 M and Na + at 0.05 M induced a compact and stable network of WPI-LRA composite gels. In addition, the measurement of reactive sulfhydryl group (SH) content and Fourier transform infrared spectroscopy were performed to investigate the gel formation mechanism induced by the two salt ions. Results indicated that the increase in the contents of SH, the changes in the protein as indicated by the relative peak areas of amide II band might be the main reason for ion-induced formation of WPI-LRA composite gel. These results obtained in the present work will provide valuable evidences for the utilization of WPI-LRA composite gels in food industry. Graphical abstract: Image 1 Highlights: Textural properties of WPI-LRA gels were enhanced by 0.1 M Ca 2+ or 0.05 M Na + . Rheological properties of WPI-LRA gels were improved by 0.1 M Ca 2+ or 0.05 M Na + . Compact network of WPI-LRA gels were induced by 0.1 M Ca 2+ or 0.05 M Na + . The reactive -SH of WPI-LRA gels was increased by 0.1 M Ca 2+ or 0.05 M Na + . Peak area of amide II band of WPI-LRA gels was increased by 0.1 M Ca 2+ or 0.05 M Na + . … (more)
- Is Part Of:
- Food hydrocolloids. Volume 87(2019)
- Journal:
- Food hydrocolloids
- Issue:
- Volume 87(2019)
- Issue Display:
- Volume 87, Issue 2019 (2019)
- Year:
- 2019
- Volume:
- 87
- Issue:
- 2019
- Issue Sort Value:
- 2019-0087-2019-0000
- Page Start:
- 629
- Page End:
- 636
- Publication Date:
- 2019-02
- Subjects:
- Lotus root amylopectin -- Whey protein isolate -- Calcium chloride -- Sodium chloride -- Gelation
Hydrocolloids -- Periodicals
Food additives -- Periodicals
Colloïdes -- Périodiques
Aliments -- Additifs -- Périodiques
Colloids
Food additives
Periodicals
Electronic journals
664.06 - Journal URLs:
- http://www.sciencedirect.com/science/journal/0268005X ↗
http://www.elsevier.com/journals ↗ - DOI:
- 10.1016/j.foodhyd.2018.08.050 ↗
- Languages:
- English
- ISSNs:
- 0268-005X
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 3977.556000
British Library DSC - BLDSS-3PM
British Library STI - ELD Digital store - Ingest File:
- 23171.xml