Optimization of Phosphorylated Modification Process of Ovalbumin Peptide
Journal Title: 河南科技大学学报(自然科学版) - Year 2017, Vol 38, Issue 3
Abstract
On the basis of determining the optimum process conditions for enzymatic preparation of ovalbumin peptide,the modification process of ovalbumin phosphorylation after enzymolysis was studied. Taking the phosphorylation degree as index,sodium tripolyphosphate was determined as the best phosphate. The optimum phosphorylated modification process conditions of ovalbumin peptide phosphorylation were determined by the single factor and four-factor quadric orthogonal rotatory combination experiments. The optimum process conditions is that reaction temperature is 30 ℃,p H is 8. 0,reaction time is 3 h,and additive mass fraction of sodium tripolyphosphate is 9%. The degree of phosphorylation reaches the peak( 57. 27 ± 1. 68) mg / g under the optimum conditions. The structural characterization of phosphorylation modified and unmodified ovalbumin peptides was analyzed by ultraviolet scanning. The results show that ultraviolet absorption peak of phosphorylation modified ovalbumin peptides shifts to the red,while ordered secondary structure of ovalbumin molecular is reduced. Because the insertion of phosphate group changes the structure of ovalbumin peptides,the maximum ultraviolet absorption peak of phosphorylation modified ovalbumin peptides is enhanced.
Authors and Affiliations
Lili LIU, Yu LI, Yanyu LIANG, Dan LI, Chenliu YANG
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