Journal
JOURNAL OF CEREAL SCIENCE
Volume 43, Issue 1, Pages 85-93Publisher
ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD
DOI: 10.1016/j.jcs.2005.06.006
Keywords
Raman spectroscopy; rice globulin; protein conformation
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The conformation of rice globulin was studied by Fourier-transform Raman spectroscopy as influenced by different buffer environments and heat treatments. The Raman spectrum of the native protein showed a predominance of alpha-helical structures as indicated by major amide I and III bands at 1657 and 1270 cm(-1) respectively. Highly acidic and alkaline pH conditions induced band shifts and intensity changes in amide I, amide III, and C-H (bending and stretching) vibrations, indicating protein denaturation. Addition of dithiothreitol and beta-mercaptoethanol led to changes in S-S stretching vibration, whereas ethylene glycol and urea caused marked changes in tryptophan, tyrosine Fermi doublet and C-H band intensities. Heating at 100 degrees C resulted in progressive denaturation as indicated by band shifts and intensity changes of major spectral regions. Our results revealed that hydrophobic interactions and disulfide bonds play a major role in stabilizing the conformation and in thermal aggregation of rice globulin. (c) 2005 Elsevier Ltd. All rights reserved.
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