Functional protein from cumin seed (Cuminum cyminum): Optimization and characterization studies

Siow, Hwee-Leng; Gan, Chee‐Yuen

doi:10.1016/j.foodhyd.2014.04.017

Cited by 35 publications

(49 citation statements)

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“…. As reported in our previous study, the protein bands were identified as 7S globulin (∼110.5 and ∼44.7 kDa), acidic subunits (30.0–38.0 kDa) and basic subunits (20.0–25.0 kDa) of 11S globulins, lectin (27.6 kDa) as well as 2S albumin (8.0–16.0 kDa) under non‐hydrolysed condition (Siow and Gan ). The hydrolysed samples showed an apparent decreased of MW, which was 5.0–44.6 kDa under non‐reducing conditions while in the range of 2.0–28.5 kDa under reducing condition.…”

Section: Resultssupporting

confidence: 78%

“…At 1 µg, the peptides extracted under optimized condition exhibiting much stronger antioxidant potencies, which they had %DPPH sc of 310.0% and ferric ion reducing power of 31.2 mM. Interestingly, the cumin seed protein isolate (1 µg) has also been previously reported to give a relatively low inhibition effect against α‐amylase, which is approximately 6.7% (Siow and Gan ). The same amount of the optimized extracts showed a 3.4 times higher of inhibitory activity (22.7%) than that of the intact protein.…”

Section: Resultsmentioning

confidence: 95%

“…Based on our previous study, the protein isolate from cumin seeds inhibited DPPH radical scavenging activity by 47.7% and possessed ferric ion reducing power of 12.0 mM at 1 µg (Siow and Gan ). In this study, gallic acid was used as positive control and had antioxidant capacities with 246.8% DPPH sc and ferric ion reducing power of 12.4 mM at the same amount.…”

Section: Resultsmentioning

confidence: 99%

“…These peptides could be the functional components which contribute to the bioactivities. Our previous study showed that the intact proteins from cumin seed exhibited anti‐oxidative and anti‐amylase activities (Siow and Gan ), and thus, it may be a promising source of bioactive peptides.…”

Section: Introductionmentioning

confidence: 99%

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Optimization Study in Extracting Anti-Oxidative and Α-Amylase Inhibitor Peptides from Cumin Seeds (Cuminum Cyminum)

Siow

Gan

2016

Journal of Food Biochemistry

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Bioactive peptide with DPPH radical scavenging activity, ferric ion reducing power and a-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 1 : 30-50C), time (X 2 : 1-2 h) and S/E ratio (X 3 : 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 1 5 42.6C, X 2 5 1.83 h and X 3 5 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 sc of 34.67% and reducing power of 3.67 mM while the non-diluted extract exhibited a-amylase inhibition activity of 22.67%. A close agreement was found between the predicted and experimental values. PRACTICAL APPLICATIONSThis 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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Section: Resultssupporting

confidence: 78%

Section: Resultsmentioning

confidence: 95%

Section: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Optimization Study in Extracting Anti-Oxidative and Α-Amylase Inhibitor Peptides from Cumin Seeds (Cuminum Cyminum)

Siow

Gan

2016

Journal of Food Biochemistry

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“…Oleoresin and ethanolic extracts have extensive applications due to their bactericidal, anti-tumor, and immunoregulatory properties (Chauhan, Satti, & Suri, 2010;Hafedh, Hedi, & Emira, 2010). Siow and Gan (2014) extracted cumin seed protein isolate using phosphate buffer (pH 8) and examined its structure, amino acid composition, a-amylase inhibition activity, DPPH free radical-scavenging activity, and reducing power. Cumin contains 59% TDF, while deoiled cumin (following essential oil and oleoresin extraction) contains 62.1% total dietary fiber (TDF), 3.3 g/g WHC, 4.0 g/g WRC, and 4.47 ml/g WSC (Sowbhagya, Suma, Mahadevamma, & Tharanathan, 2007).…”

Section: Introductionmentioning

confidence: 99%

Effects of extraction methods and particle size distribution on the structural, physicochemical, and functional properties of dietary fiber from deoiled cumin

2016

Food Chemistry

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Foxtail millet: a potential crop to meet future demand scenario for alternative sustainable protein

2020

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Foxtail millet (Setaria italica), an annual grass plant, produces seeds that possess health‐promoting properties owing to its unique protein composition containing a high content of essential amino acids. The mature foxtail seeds mainly consist of proline‐rich, alcohol‐soluble proteins (prolamin) called setarins, comprising about 60% of the total protein, with less content of disulfide cross‐linked proteins than with other cereal and millets. Protein fractionation schemes are an important tool and provide preliminary information on the nature of foxtail proteins for their applications in the field of agriculture, food pharma, and bio‐based materials. Variation in the methods of preparation can influence the composition, structure, and nutritional quality of the protein concentrate. Moreover, foxtail protein or its hydrolysate has shown several bioactive effects that can be explored further for the management of chronic diseases in humans. Additionally, owing to its low cost and excellent functional properties of flour and protein concentrate, foxtail millet can be considered as good candidate for replacing animal protein foods. Furthermore, there is huge potential for successfully developing low‐cost, protein‐rich functional food products helpful in the prevention and management of lifestyle‐related chronic diseases. © 2020 Society of Chemical Industry

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Functional protein from cumin seed (Cuminum cyminum): Optimization and characterization studies

Cited by 35 publications

References 35 publications

Optimization Study in Extracting Anti-Oxidative and Α-Amylase Inhibitor Peptides from Cumin Seeds (Cuminum Cyminum)

Optimization Study in Extracting Anti-Oxidative and Α-Amylase Inhibitor Peptides from Cumin Seeds (Cuminum Cyminum)

Effects of extraction methods and particle size distribution on the structural, physicochemical, and functional properties of dietary fiber from deoiled cumin

Foxtail millet: a potential crop to meet future demand scenario for alternative sustainable protein

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