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| Optimization of preparation of Amygdalus pedunculata Pall peptides using response surface methodology |
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| DOI： |
| KeyWord:Amygdalus pedunculata Pall polypeptide enzymatic hydrolysation response surface optimization |
| FundProject:陕西省科技厅重点产业链项目（2018ZDXM-NY-087）；陕西省秦创原“科学家+工程师”队伍建设项目（2022KXJ-148）；陕西省创新能力支撑计划项目（2021PT-035） |
| Author Name | Affiliation | | LI Cong1, SU Chencan1, LI Haoyu1,2,WEI Bing3, ZHANG Yu3,
SHI Xuanming3,CHEN Bang 1, SHEN Yehua1 | 1.College of Chemistry and Materials Science, Northwest University, Xi′an 710127, China
2.College of
Chemistry and Chemical Engineering, Yan′an University, Yan′an 716000, Shaanxi, China
3.COFCO
ET(Xi′an) International Engineering Co. , Ltd., Xi′an 710082, China |
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| Abstract: |
| To develop Amygdalus pedunculata Pall seed protein for high-value, the water soluble protein was extracted from Amygdalus pedunculata Pall seed after defatting, then hydrolyzed by protease to prepare Amygdalus pedunculata Pall peptides. The effects of five proteases on the hydrolysis degree of the water soluble protein of Amygdalus pedunculata Pall seed and antioxidant activity of hydrolysate were studied, and the suitable hydrolytic enzyme was selected. Then the preparation process of Amygdalus pedunculata peptides was optimized by single factor experiment and response surface methodology. The results showed that the alcalase was more suitable for hydrolysis of Amygdalus pedunculata Pall protein with higher hydrolysis degree (16.03%) and DPPH free radical scavenging activity (59.49%). The optimal hydrolysis conditions of Amygdalus pedunculata Pall protein were obtained as follows: enzymatic hydrolysis temperature 57 ℃, enzymatic hydrolysis time 4 h, dosage of alcalase 1 192 U/g, pH 8.4. Under the optimal conditions, the hydrolysis degree of Amygdalus pedunculata Pall protein was 1812%. It is feasible to prepare polypeptides by enzymatic hydrolysis of Amygdalus pedunculata Pall seed protein. It can improve the added value of Amygdalus pedanculata Pall seed, and can provide high-quality raw materials for functional peptide products. |
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