Functional properties of oil peony seed meal protein and its enzymatic hydrolysate
  
DOI:10.12166/j.zgyz.1003-7969/2020.05.014
KeyWord:peony seed meal  protein  enzymatic hydrolysate  functional property
FundProject:陕西省科技厅重点产业链项目(2018ZDXM-NY-087, 2019TSLNY03-02);国家重点研发计划(2019YFD1002400);陕西省林业厅2018年重大专项
Author NameAffiliation
WANG Min LI Cong SHU Yu LI Haoyu CHEN Bang SHEN Yehua 1.Key Laboratory of Synthetic and Natural Functional Molecule Chemistry of Ministry of Education,College of Chemistry and Materials Science, Northwest University, Xi’an 710127, China
2.College of Food Science and Engineering, Northwest University, Xi’an 710127, China
3.College of Chemistry and Chemical Engineering, Yan’an University, Yan’an 716000, Shaanxi, China 
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Abstract:
      The experimental study on the functional properties of relative molecular weight distribution, solubility, denaturation temperature and antioxidative properties affected by temperature and pH was carried out with oil peony seed meal protein (PoSMP) and its alcalase enzymatic hydrolysates (AHs). The results showed that the subunits of PoSMP were mainly distributed at 62, 45, 34 kDa and 23 kDa, and the 45, 23 kDa bands were well tolerated to alcalase. At pH 4.5 and 3.7, the solubilities of PoSMP and AHs were the lowest, which were(0.92±0.25)% and (8.90±0.32)% respectively. Both of them showed good solubility under neutral conditions. The denaturation temperatures of the two were 67.82 ℃ and 84.70 ℃, respectively. In addition, PoSMP exhibited good antioxidant activity at high temperature and pH 3.0-90, and AHs also had excellent antioxidant activity at high temperature and a strong alkali pH 11.0. The results demonstrated that PoSMP and AHs had good solubility and antioxidant stability, which were expected to be used as a supplement or functional component in the fields of food and health products.
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