Optimization Study in Extracting Anti-Oxidative and Α-Amylase Inhibitor Peptides from Cumin Seeds (Cuminum Cyminum)
Journal of Food Biochemistry, ISSN: 1745-4514, Vol: 41, Issue: 1
2017
- 19Citations
- 17Captures
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Article Description
Bioactive peptide with DPPH radical scavenging activity, ferric ion reducing power and α-amylase inhibition properties were successfully extracted from cumin seed using protamex. Response surface methodology was used to optimize the extraction condition. The effects of temperature (X: 30–50C), time (X: 1–2 h) and S/E ratio (X: 20–40 (w/w)) were investigated using the Box-behnken design. Data were analyzed using ANOVA and quadratic models were found to be significant for all responses. Three-dimensional response surfaces plotted and the optimum condition was determined as follows: X = 42.6C, X = 1.83 h and X = 20 (w/w). Low molecular mass of peptides (2.0–28.5 kDa) were produced in this condition and the pre-diluted extract to a dilution factor of 20 gave %DPPH of 34.67% and reducing power of 3.67 mM while the non-diluted extract exhibited α-amylase inhibition activity of 22.67%. A close agreement was found between the predicted and experimental values. Practical Applications: This study highlights that bioactive peptides derived from cumin seed have demonstrated antioxidative and antidiabetic activities, offering health promoting effect beyond its basic nutritional functions. Extraction of these bioactive peptides with the best yield and the highest bioactivity offer a great potential in functional food or nutraceutical applications. The application of response surface methodology is useful to optimize the extraction parameters for increase extraction efficiency. This would make it possible to improve the technological processes for producing high content of bioactive peptides with less cost and shorter time. Knowledge generated in this study will be beneficial in developing strategies to explore bioactive peptides from natural sources with food and pharmaceutical applications.
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