Pectin methylesterase modified pectin interaction with whey protein isolate and stability of double emulsions.

Citation:

Nissim Garti and Louise. Wicker. 2005. “Pectin methylesterase modified pectin interaction with whey protein isolate and stability of double emulsions.” In Abstracts of Papers, 229th ACS National Meeting, San Diego, CA, United States, March 13-17, 2005, Pp. CELL–119. American Chemical Society.

Abstract:

Valencia orange pectin methylesterase (PME) isoenzymes were used to de-esterify com. pectin. Unmodified and PME modified pectin were mixed with whey protein isolate (WPI), 90% $\beta$-lactoglobulin, and the interaction was studied using fluorescence, mol. wt., and charge. Double emulsions stabilized by hybrids of WPI and modified pectins were tested for rheol. properties, droplet size and stability. The zeta potential of the hybrids at pH values below the pI of protein was neg. charged at a ratio of 4:0.5 (wt/wt) WPI/pectin. Decreasing stability of double emulsions was obsd. with WPI/pectin complex if neg. charged (pH 6), pos. charged, and highly neg. charged. Rheol. confirmed that double emulsions are most stable at pH 6.0, with highest elasticity (G'/G''= 66°). Droplets of W/O/W double emulsions made from WPI and modified pectin ranged from ca. 15 to ca. 5 $μ$m, depending on pectin. At pH 6.0, stability to coalescence was excellent after 40 days. [on SciFinder(R)]
Last updated on 05/27/2020