News Column

New Findings on Milk Proteins from Indian Institute of Technology Summarized

February 25, 2014



By a News Reporter-Staff News Editor at Life Science Weekly -- Investigators publish new report on Proteins. According to news reporting from Gauhati, India, by NewsRx journalists, research stated, "The work we have undertaken is to investigate the adsorption of two different proteins (BSA and BLG) having near same IEP and differing in their conformational flexibility, onto the surface of ZnS nanopartides (ZnS NPs). BSA and BLG both have an IEP value around pH similar to 5. BSA is more prone to conformational deformation and considered 'soft' while BLG holds the conformational rigidity and considered as 'hard' protein."

The news correspondents obtained a quote from the research from the Indian Institute of Technology, "To ascertain the differences in surface coverage and conformation of the protein onto ZnS surface (PZC similar to 3.7), we have evaluated the adsorption profile at pH 7, where the entire surface behaves negatively. An integrated approach was taken by incorporating zeta (zeta) potential, fluorescence and CD for analyzing the adsorption process. In both systems, an increase in protein surface coverage was observed with the increase in free protein concentration in the solution and zeta values approaching that of native protein at high surface coverage. An alteration in the tertiary structure was observed for both BSA and BLG. The CD spectra analysis reveals that the secondary structure of the BSA was more deviated from the native protein structure, accommodating the increased adsorption value. For BLG no such prominent structural alteration was observed."

According to the news reporters, the research concluded: "These findings help us to understand better, how adjustment of the protein adsorption amount can be achieved onto the surface of nanoparticles having like charges."

For more information on this research see: Interpreting the adsorption of serum albumin and lactoglobulin onto ZnS nanopaticles: Effect of conformational rigidity of the proteins. Journal of Colloid and Interface Science, 2014;416():235-242. Journal of Colloid and Interface Science can be contacted at: Academic Press Inc Elsevier Science, 525 B St, Ste 1900, San Diego, CA 92101-4495, USA. (Elsevier - www.elsevier.com; Journal of Colloid and Interface Science - www.elsevier.com/wps/product/cws_home/622861)

Our news journalists report that additional information may be obtained by contacting J. Saikia, Indian Inst Technol Guwahati, Center Environm, Gauhati 781039, Assam, India. Additional authors for this research include B. Saha and G. Das (see also Proteins).

Keywords for this news article include: Asia, India, Gauhati, Peptides, Amino Acids, Milk Proteins, Serum Albumin, Blood Proteins, Lactoglobulins, Acute-Phase 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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