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Findings on Peptides and Proteins Reported by Investigators at Food Futures National Research Flagship (Gelling properties of protein fractions and...

September 9, 2014



Findings on Peptides and Proteins Reported by Investigators at Food Futures National Research Flagship (Gelling properties of protein fractions and protein isolate extracted from Australian canola meal)

By a News Reporter-Staff News Editor at Life Science Weekly -- Current study results on Proteins have been published. According to news reporting originating from Werribee, Australia, by NewsRx correspondents, research stated, "Gelling properties of canola albumin and globulin fractions, and canola protein isolate (CPI) were examined in this study. The effects of pH and salt concentration on canola protein gelling properties were studied primarily by means of dynamic oscillatory rheology and gel texture analysis."

Our news editors obtained a quote from the research from Food Futures National Research Flagship, "The findings were supported by confocal laser scanning microscopy (CLSM) images of the gels, isoelectric point, and solubility measurement data. All canola proteins showed typical heat-set gel protein profiles. Gels formed at higher pH had better gelling properties including higher overall resistance to deformation (G*), higher gel elasticity (low tan delta), higher fracture stress and firmness, and denser gel microstructure. Isoelectric points of canola proteins used in this study were in the range of pH 3.0-4.7 where low protein solubility was observed. The albumin fraction was able to form a very weak gel at pH 4, whereas the globulin fraction and CPI precipitated due to loss of protein surface charge. The effects of NaCl on gelling were protein sample dependent. The presence of NaCl negatively affected gelling properties of albumin and globulin fractions, with decreases in overall resistance to deformation (G*), and fracture stress and firmness, but positively affected CPI gels in the same aspects. The elasticity (tan delta) of all canola protein gels remained constant in the presence of NaCl. Frequency sweep analysis revealed that the albumin fraction and CPI formed weak gels, whereas the globulin fraction formed a strong gel. Strain sweep analysis further confirmed that the globulin fraction formed a stronger gel with a critical strain of at least 10%."

According to the news editors, the research concluded: "This study demonstrates the high potential of canola proteins, particularly the globulin fraction, as a prospective gelling agent."

For more information on this research see: Gelling properties of protein fractions and protein isolate extracted from Australian canola meal. Food Research International, 2014;62():819-828. Food Research International can be contacted at: Elsevier Science Bv, PO Box 211, 1000 Ae Amsterdam, Netherlands. (Elsevier - www.elsevier.com; Food Research International - www.elsevier.com/wps/product/cws_home/422970)

The news editors report that additional information may be obtained by contacting S.H. Tan, Food Futures Natl Res Flagship, Werribee, Vic 3030, Australia. Additional authors for this research include R.J. Mailer, C.L. Blanchard, S.O. Agboola and L. Day (see also Proteins).

Keywords for this news article include: Werribee, Australia, Australia and New Zealand, Globulins, Proteins

Our reports deliver fact-based news of research and discoveries from around the world. Copyright 2014, NewsRx LLC


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Source: Life Science Weekly


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