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Isolation,purification, and characterization of the globulin from wheat germ |
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| Authors: | Ling Fan Mingqian Yang Sen Ma Jihong Huang |
| Affiliation: | 1. Food and Pharmacy College, Xuchang University, Xuchang, Henan, 461000 China Contribution: Data curation (equal), Formal analysis (equal), Writing - original draft (equal), Writing - review & editing (equal);2. College of Biological Engineer, Henan University of Technology, Zhengzhou, Henan, 450001 China Contribution: Data curation (equal), Formal analysis (equal), Methodology (equal);3. College of Food Science and Engineering, Henan University of Technology, Zhengzhou, Henan, 450001 China;4. Food and Pharmacy College, Xuchang University, Xuchang, Henan, 461000 China |
| Abstract: | This research optimized the extraction and purification of globulin from wheat germ and assessed the molecular weight distribution and structure properties of the globulin obtained. The results showed that the relative extraction efficiency and purity of wheat germ globulin (WGG) reached 18.0% and 89.1% under the enzymolysis conditions of 0.32‰ α-amylase, pH 6.5, and 55 °C. The maximal precipitation rate of WGG (91.3%) was obtained with pH 4.3 (acid precipitation). Additionally, the molecular weight of WGG was mainly distributed below 70 kDa. FT-IR confirmed that random coils (30.95%), β-sheet (27.02%), α-helix (26.55%), and β-turn (15.48%) were the secondary structures of WGG. Furthermore, LTQ mass spectrometry showed that WGG was rich in variety and high in complexity, which retrieved 1274 proteins belonging to 392 proteomes by inverse peptide analysis. The findings endow a great potential of preparing WGG with superior functionality for food applications. |
| Keywords: | Enzymatic hydrolysis globulin structural properties wheat germ |