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Information Journal Paper

Title

Investigation of functional and antioxidant properties of Faba bean protein hydrolysates using combined hydrolysis

Pages

  25-38

Abstract

 Background and objectives: Food is considered not only as a source of energy and essential ingredients for growth and health but as a source of bioactive compounds with beneficial effects. Bioactive peptides are considered as functional compounds that have been known in food recently. Enzymatic hydrolysis is used to improve the Functional properties of plant proteins. One of the features of the protein hydrolysates is their antioxidant activity, which makes it possible to use them as antioxidant agents in the diet. In this study, the effect of different enzymes and their combination in the production of protein hydrolysates with high functional and Antioxidant properties was investigated. Material and methods: Faba bean protein isolate was enzymatically hydrolyzed by trypsin and alcalase each, and in a successive way with trypsin and alcalase at the concentrations of 1. 5 and 3% for reaction time of 3 h. The optimum temperature of 37 and 50 ° C and pH of 7 and 8. 5 was used for trypsin and alcalase, respectively. The solubility parameters at pH 2-12, foaming and foam stability at the pH level of 4, 6, 8 and 10, DPPH radical scavenging activity, and iron chelating activity of protein hydrolysates were investigated. Results: The results showed that enzymatic hydrolysis increased the solubility, especially in acidic pH range. The protein hydrolysates derived from alcalase and trypsin-alcalase combinations (at the concentration of 3%) showed the highest solubility of 64. 51% and 60. 95% at pH value of 3, respectively. Foaming capacity enhanced with pH increment from 4 to 8. The maximum and minimum foaming capacity of protein hydrolysates were observed at pH values of 8 and 10, respectively, while protein isolate created no foam at pH value of 4. The highest foam stability was observed at pH level of 8 in all samples. The results also showed that hydrolysis of Faba bean protein significantly increased the foaming stability (P<0. 05). Hydrolyzed samples from trypsin and trypsin-alcalase combination (at the concentration of 3%) showed the highest foam stability at pH=8. The enzymatic hydrolysis significantly increased the DPPH radical scavenging activity (P<0. 05). Maximum DPPH radical scavenging activity was observed in the alcalase treated samples (75. 71%) which showed significant difference with other treatments (P<0. 05). There was no significant difference in the DPPH radical scavenging activity of trypsin treated samples (72. 54%), and trypsin-alcalase combinations with concentrations of 1. 5% (73. 66) and 3% (73. 62%) (P>0. 05). The enzymatic hydrolysis significantly increased the iron chelating activity compared to Faba bean protein isolate (P<0. 05). Conclusion: The results showed that different enzymes under constant hydrolysis conditions have different effects on a single substrate. Enzymatic modification of proteins creates a natural antioxidant source in food models, which may increase the shelf-life of products.

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    APA: Copy

    SAMAEI, S.P., GHORBANI, M., SADEGHI MAHOONAK, A.R., & ALAMI, M.. (2021). Investigation of functional and antioxidant properties of Faba bean protein hydrolysates using combined hydrolysis. ELECTRONIC JOURNAL OF FOOD PROCESSING AND PRESERVATION, 12(2 ), 25-38. SID. https://sid.ir/paper/407234/en

    Vancouver: Copy

    SAMAEI S.P., GHORBANI M., SADEGHI MAHOONAK A.R., ALAMI M.. Investigation of functional and antioxidant properties of Faba bean protein hydrolysates using combined hydrolysis. ELECTRONIC JOURNAL OF FOOD PROCESSING AND PRESERVATION[Internet]. 2021;12(2 ):25-38. Available from: https://sid.ir/paper/407234/en

    IEEE: Copy

    S.P. SAMAEI, M. GHORBANI, A.R. SADEGHI MAHOONAK, and M. ALAMI, “Investigation of functional and antioxidant properties of Faba bean protein hydrolysates using combined hydrolysis,” ELECTRONIC JOURNAL OF FOOD PROCESSING AND PRESERVATION, vol. 12, no. 2 , pp. 25–38, 2021, [Online]. Available: https://sid.ir/paper/407234/en

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