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Expanded Functionality of Modified Whey Protein Dispersions after Transglutaminase Catalysis
Author(s) -
Clare Debra A.,
Daubert Christopher R.
Publication year - 2011
Publication title -
journal of food science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.772
H-Index - 150
eISSN - 1750-3841
pISSN - 0022-1147
DOI - 10.1111/j.1750-3841.2011.02128.x
Subject(s) - tissue transglutaminase , emulsion , materials science , chromatography , polymerization , chemistry , polymer chemistry , enzyme , polymer , organic chemistry , composite material
The functionality of whey dispersions, prepared with a modified whey protein concentrate (mWPC) ingredient, was significantly altered after cross‐linking with microbial transglutaminase (TGase) upon pH adjustment to 8. Test TGase–mWPC solutions, pH 8, gelled faster than control mWPC dispersions, as measured in real time; whereas, the gelling temperature of pretreated TGase–mWPC samples (37 °C, 2.5 h) increased from 67.8 to 74.8 °C with a minimal change in gel strength. Prolonged prior incubation with the enzyme (37 °C, 20 h) raised the gel strength in both control mWPC and TGase–mWPC dispersions, though these values were approximately 2.7 times lower in TGase–mWPC samples. Furthermore, the gelling temperature was raised by 9 °C after extensive polymerization. The water holding capacity was not impacted by enzymatic processing while emulsions prepared with TGase–mWPC dispersions proved very stable with no evidence of phase separation during storage at room temperature for 1 mo. Moreover, the apparent viscosity of TGase–mWPC emulsions exhibited a 10‐fold increase compared to nonenzyme‐treated mWPC samples. The particle size was nearly 11 μm in covalently linked TGase–mWPC test fractions compared with 8 μm in nonpolymerized mWPC dispersions. Ultimately, the functional characteristics of TGase–mWPC ingredients may be designed to deliver superior performance, especially with regard to improving heat and emulsion stability.