Abstract
The effects of glutaminase on deamidation of rice glutelin were investigated. Water-insoluble rice glutelin was deamidated to the extent of deamidation degree 52.29% in 200 mmol/L sodium phosphate buffer (pH 7.0) at 37 °C for 48 h. Zeta potential analysis indicated that the glutamines of rice glutelin were deamidated into glutamic residues. Size exclusion chromatography results demonstrated that glutaminase deamidation broke the hydrophobic, hydrogen and some intermolecular disulfide bonds in rice glutelin and thereby rearranged the molecular weight distributions without serious cleavage of the peptide bonds. Fourier transform infrared analysis revealed the transformation of α-helix to random coil and β-turn by deamidation and suggested that deamidated rice glutelin maintained more flexible or extended forms. Solubility properties of rice glutelin in mildly acid (pH 5) and neutral buffers (pH 7) were remarkably improved by glutaminase deamidation. These new features of deamidated rice glutelin suggested that glutaminase could be a potential tool for enhancing the usability of rice protein in the food industry.
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
