pH-shifting encapsulation of curcumin in egg white protein isolate for improved dispersity, antioxidant capacity and thermal stability

The effects of egg white protein and soy protein isolate addition on the nutritional and digestibility of gluten-free pasta based on banana flour were studied. The level of protein additions (soy protein or egg white protein) were 0, 5, 10 and 15% of banana flour (w/w). Pasta made from 100% durum wheat semolina was used as a control. Soy protein isolate inclusion into banana pasta increased total phenolic content (TPC) and antioxidant capacities, while egg white protein decreased the TPC and antioxidant capacities with the increasing level of addition. Starch digestibility was affected by the type of protein addition. Egg white protein lowered starch digestibility compared to soy protein isolate. Protein inclusion in banana pasta also altered protein digestibility, amino acid profiles and protein digestibility-corrected amino acid score (PDCAAS). Soy protein isolate increased protein digestibility of gluten-free pasta compared to egg white protein. Protein enrichment gave better amino acid profiles of banana pasta compared to semolina pasta with egg white protein and performed a better PDCAAS compared to soy protein isolate. These results showed that soy protein isolate and egg white protein addition enhanced nutritional qualities and digestibility properties of gluten-free banana pasta.

Download Full-text

pH Shifting Alters Solubility Characteristics and Thermal Stability of Soy Protein Isolate and Its Globulin Fractions in Different pH, Salt Concentration, and Temperature Conditions

Journal of Agricultural and Food Chemistry ◽

10.1021/jf101045b ◽

2010 ◽

Vol 58 (13) ◽

pp. 8035-8042 ◽

Cited By ~ 86

Author(s):

Jiang Jiang ◽

Youling L. Xiong ◽

Jie Chen

Keyword(s):

Thermal Stability ◽

Soy Protein ◽

Salt Concentration ◽

Soy Protein Isolate ◽

Protein Isolate ◽

Temperature Conditions ◽

Ph Shifting ◽

Thermal Stability Of

Download Full-text

Tailor made protein based aerogel particles from egg white protein, whey protein isolate and sodium caseinate: Influence of the preceding hydrogel characteristics

Food Hydrocolloids ◽

10.1016/j.foodhyd.2018.05.021 ◽

2018 ◽

Vol 83 ◽

pp. 365-374 ◽

Cited By ~ 20

Author(s):

Christian Kleemann ◽

Ilka Selmer ◽

Irina Smirnova ◽

Ulrich Kulozik

Keyword(s):

Whey Protein ◽

Sodium Caseinate ◽

Whey Protein Isolate ◽

Egg White ◽

Protein Isolate ◽

Egg White Protein

Download Full-text

Application of Glycation in Regulating the Heat-Induced Nanoparticles of Egg White Protein

Nanomaterials ◽

10.3390/nano8110943 ◽

2018 ◽

Vol 8 (11) ◽

pp. 943 ◽

Cited By ~ 7

Author(s):

Chenying Wang ◽

Xidong Ren ◽

Yujie Su ◽

Yanjun Yang

Keyword(s):

Thermal Stability ◽

Protein Concentration ◽

Thermal Denaturation ◽

Negative Charge ◽

Activity Index ◽

Stability Index ◽

Egg White ◽

Egg White Protein ◽

Neutral Conditions ◽

Thermal Stability Of

Due to the poor thermal stability of egg white protein (EWP), important challenges remain regarding preparation of nanoparticles for EWP above the denaturation temperature at neutral conditions. In this study, nanoparticles were fabricated from conjugates of EWP and isomalto-oligosaccharide (IMO) after heating at 90 °C for 30 min. Meanwhile, the effects of protein concentration, temperature, pH, ionic strength and degree of glycation (DG) on the formation of nanoparticles from IMO-EWP were investigated. To further reveal the formation mechanism of the nanoparticles, structures, thermal denaturation properties and surface properties were compared between EWP and IMO-EWP conjugates. Furthermore, the emulsifying activity index (EAI) and the emulsifying stability index (ESI) of nanoparticles were determined. The results indicated that glycation enhanced thermal stability and net surface charge of EWP due to changes in the EWP structure. The thermal aggregation of EWP was inhibited significantly by glycation, and enhanced with a higher degree of glycation. Meanwhile, the nanoparticles (<200 nm in size) were obtained at pH 3.0, 7.0 and 9.0 in the presence of NaCl. The increased thermal stability and surface net negative charge after glycation contributed to the inhibition. The EAI and ESI of nanoparticles were increased nearly 3-fold and 2-fold respectively, as compared to unheated EWP.

Download Full-text