Drying and denaturation kinetics of whey protein isolate (WPI) during convective air drying process
- Authors: Haque, M. Amdadul , Putranto, Aditya , Aldred, Peter , Chen, Jie , Adhikari, Benu
- Date: 2013
- Type: Text , Journal article
- Relation: Drying Technology Vol. 31, no. 13-14 (2013), p. 1532-1544
- Full Text: false
- Reviewed:
- Description: The denaturation and drying kinetics of whey protein isolate (WPI) in a convective drying (CD) environment was measured using single droplet drying experiments. The moisture content and temperature histories during drying of WPI droplets were predicted using reaction kinetics-based models. The denaturation kinetics of WPI in the CD process was predicted using first-order reaction kinetics considering the denaturation rate constant to be moisture content and temperature dependent. Single droplets of WPI (10% [w/v], 2.0 ± 0.1 mm initial diameter) were used throughout these experiments. The drying experiments were carried out at two temperatures (65 and 80°C) at a constant air velocity (0.5 m/s) for 600 s. The extent and nature of the denaturation of WPI during the CD was compared with those in isothermal heat treatments (IHT) at the same medium temperatures. The denaturation of WPI was 68.31% in convective air drying at 65°C and 600 s and it was 10.79% in the IHT at the same temperature and time. The stress due to dehydration and the exposure time were found to be responsible for the denaturation of WPI in the CD process and long exposure time was found to be responsible for its denaturation in the IHT process. At the media temperature of 80°C, the denaturation loss of WPI was 90.00 and 68.73% in IHT and CD processes, respectively. Both the thermal (moist heat) and dehydration stresses were found to be responsible for denaturation of WPI during CD process and very high thermal stress was found to be responsible for denaturation of WPI during the IHT. There was good agreement between the experimental and reaction engineering approach (REA)-predicted moisture content and temperature histories. The experimental moisture content and temperature histories were followed by the respective REA predictions within 6.5% (R 2 = 0.995) and 3% (R 2 = 0.981) errors, respectively. The denaturation kinetics of WPI during CD was predicted well (R 2 = 0.95 - 0.98; average error = 6.5 ± 0.5%) by a first-order reaction kinetics model. © 2013 Copyright Taylor and Francis Group, LLC.
- Description: C1
Drying and denaturation characteristics of whey protein isolate in the presence of lactose and trehalose
- Authors: Haque, M. Amdadul , Chen, Jie , Aldred, Peter , Adhikari, Benu
- Date: 2015
- Type: Text , Journal article
- Relation: Food Chemistry Vol. 177, no. (2015), p. 8-16
- Full Text: false
- Reviewed:
- Description: The denaturation kinetics of whey protein isolate (WPI), in the presence and absence of lactose and trehalose, was quantified in a convective air-drying environment. Single droplets of WPI, WPI-lactose and WPI-trehalose were dried in conditioned air (2.5% RH, 0.5 m/s air velocity) at two temperatures (65°C and 80°C) for 500 s. The initial solid concentration of these solutions was 10% (w/v) in all the samples. Approximately 68% of WPI was denatured when it was dried in the absence of sugars. Addition of 20% trehalose prevented the irreversible denaturation of WPI at both temperatures. Thirty percent lactose was required to prevent denaturation of WPI at 65°C and the same amount of lactose protected only 70% of WPI from denaturation at 80°C. The secondary structures of WPI were found to be altered by the drying-induced stresses, even in the presence of 20% trehalose and 30% lactose.
Comparative study of denaturation of whey protein isolate (WPI) in convective air drying and isothermal heat treatment processes
- Authors: Haque, M. Amdadul , Aldred, Peter , Chen, Jie , Barrow, Colin , Adhikari, Benu
- Date: 2013
- Type: Text , Journal article
- Relation: Food Chemistry Vol. 141, no. 2 (2013), p. 702-711
- Full Text: false
- Reviewed:
- Description: The extent and nature of denaturation of whey protein isolate (WPI) in convective air drying environments was measured and analysed using single droplet drying. A custom-built, single droplet drying instrument was used for this purpose. Single droplets having 5. ±. 0.1. μl volume (initial droplet diameter 1.5. ±. 0.1. mm) containing 10% (w/v) WPI were dried at air temperatures of 45, 65 and 80. °C for 600. s at constant air velocity of 0.5. m/s. The extent and nature of denaturation of WPI in isothermal heat treatment processes was measured at 65 and 80. °C for 600. s and compared with those obtained from convective air drying. The extent of denaturation of WPI in a high hydrostatic pressure environment (600. MPa for 600. s) was also determined. The results showed that at the end of 600. s of convective drying at 65. °C the denaturation of WPI was 68.3%, while it was only 10.8% during isothermal heat treatment at the same medium temperature. When the medium temperature was maintained at 80. °C, the denaturation loss of WPI was 90.0% and 68.7% during isothermal heat treatment and convective drying, respectively. The bovine serum albumin (BSA) fraction of WPI was found to be more stable in the convective drying conditions than
- Description: 2003011092
Drying and denaturation characteristics of α-LACTALBUMIN, β-lactoglobulin, and bovine serum albumin in a convective drying process
- Authors: Haque, M. Amdadul , Aldred, Peter , Chen, Jie , Barrow, Colin , Adhikari, Benu
- Date: 2014
- Type: Text , Journal article
- Relation: Journal of Agricultural and Food Chemistry Vol. 62, no. 20 (2014), p. 4695-4706
- Full Text: false
- Reviewed:
- Description: Drying and denaturation kinetics of aqueous droplets of α-lactalbumin (α-lac), β-lactoglobulin (β-lg), and bovine serum albumin (BSA) were measured in a convective drying environment. Single droplets having an initial droplet diameter of 2 ± 0.1 mm and containing 10% (w/v) protein concentration were dried using conditioned air (65 and 80 °C, 2-3% RH, 0.5 m/s velocity) for 600 s. The denaturation of these proteins was measured by using reversed-phase HPLC. At the end of 600 s of drying 13.3 and 19.4% α-lac was found to be lost due to denaturation at 65 and 80 °C, respectively. Up to 31.0% of β-lg was found to be denatured, whereas BSA was not found to be significantly (p > 0.05) denatured in these drying conditions. The formation and strength of skin and the associated morphological features were found to be linked with the degree of denaturation of these proteins. The secondary structure of these proteins was significantly (p < 0.05) affected and altered by the drying stresses. The β-sheet and random coil contents were increased in α-lac by 6.5 and 4.0%, respectively, whereas the α-helix and β-turn contents decreased by 5.5 and 5.0%, respectively. The β-sheet and random coil contents in β-lg were increased by 7.5 and 2.0%, respectively, whereas the α-helix and β-turn contents decreased by 3.5 and 6.0%, respectively. In the case of BSA the β-sheet, α-helix, and random coil contents were found to increase, whereas the β-turn content decreased. © 2014 American Chemical Society.
Denaturation and physical characteristics of spray-dried whey protein isolate powders produced in the presence and absence of Lactose, Trehalose, and Polysorbate-80
- Authors: Haque, M. Amdadul , Chen, Jie , Aldred, Peter , Adhikari, Benu
- Date: 2015
- Type: Text , Journal article
- Relation: Drying Technology Vol. 33, no. 10 (2015), p. 1243-1254
- Full Text: false
- Reviewed:
- Description: The denaturation (loss of protein through aggregation and/or change in secondary structure) and physical characteristics such as powder morphology, particle size and size distribution, amorphous/crystalline behavior, and solubility of whey protein isolate (WPI) were investigated in a spray-drying process. The protective efficacy of sugars (lactose and trehalose) and low-molecular-weight surfactant polysorbate-80 (Tween-80) on the secondary structure (-turn, -sheet and -helix) and physical characteristics of spray-dried WPI was quantified. The WPI, WPI+sugar, and WPI+Tween-80 formulations were spray dried maintaining the total solids at 10% (w/w). The inlet and outlet temperatures were maintained at 180 and 80 degrees C, respectively. The results showed that the loss of protein through denaturation and aggregation was not significant (p>0.05). However, a significant (p<0.05) alteration of the secondary structural elements was observed. Due to spray drying of WPI without protectants, the -sheet and -turn were decreased by 4.4 and 14.5%, respectively, and the random coil increased by 20.7%. The -helix of WPI remained unaltered during the spray-drying process. The presence of Tween-80 effectively protected the -helix and -sheet but the -turn remained vulnerable and was decreased. No significant (p>0.05) change in the solubility of WPI was observed due to spray drying. Spray drying of WPI+sugar produced essentially amorphous particles. The dried powder particles were spherical with wrinkled or folded surface.
Improving the foaming properties of soy protein isolate through partial enzymatic hydrolysis
- Authors: Zeng, Maomao , Adhikari, Benu , He, Zhiyong , Qin, Fan. , Huang, Xuang , Chen, Jie
- Date: 2013
- Type: Text , Journal article
- Relation: Drying Technology Vol. 31, no. 13-14 (2013), p. 1545-1552
- Full Text: false
- Reviewed:
- Description: The effect of partial enzymatic hydrolysis of soy protein isolate (SPI) on its foaming properties is investigated in this study. Enzymes of different origin, including papain, alcalase, and pancreatin, were used. Foaming properties (foaming capacity and foam stability) were measured and their relationships with physicochemical characteristics such as degree of hydrolysis, molecular weight of hydrolysates, and surface tension were investigated. Papain hydrolyzed SPI hydrolysates were found to be the best in terms of improved foaming capacity and foam stability. Molecular weights of SPI hydrolysates obtained by papain and alcalase hydrolysis were mainly in the range of 5 kDa to 30 kDa, while those hydrolyzed by pancreatin had molecular weight above 50 kDa. Foaming capacity was found to correlate well with the relative abundance of hydrolysate in the molecular weight range of 5 kDa to 10 kDa (r = 0.84, p < 0.05). Surface hydrophobicity was found to correlate negatively (r = - 0.89, p < 0.05) with foaming capacity of SPI hydrolysates. Surface tension values of SPI hydrolysates produced by all enzymes were significantly lower than (p < 0.05) compared to that of SPI. The surface tension of pancreatin hydrolyzed SPI hydrolysates was lower than the surface tension of those hydrolyzed by papain and alcalase. The surface tension of pancreatin hydrolyzed SPI hydrolysates decreased more rapidly with time compared to the rest. These findings will provide better understanding of how best to carry out the partial hydrolysis of SPI using various enzymes in order to improve its foaming properties. © 2013 Copyright Taylor and Francis Group, LLC.
- Description: C1