Task-specific deep eutectic solvent based extraction coupled cascade chromatography quantification of α-glucosidase inhibitory peptide from Ocimum tenuriflorum seeds

Karthiraj, T.; Balaraman, Harish Babu; Rathnasamy, Senthilkumar

doi:10.1016/j.microc.2020.104883

Cited by 20 publications

(16 citation statements)

References 41 publications

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“…To date, various protease-digested plant hydrolysates from beans, Ocimum tenuriflorum seeds, hemp seed protein, walnut, soybean, rice, and dark tea have been indicated as the main contributors to inhibit α-glucosidase [27,31,[70][71][72][73][74][75]. Small peptides generally possess more potential α-glucosidase inhibitors as compared to large peptides.…”

Section: Food Protein-derived α-Glucosidase Inhibition Peptidesmentioning

confidence: 99%

Characteristics of Food Protein-Derived Antidiabetic Bioactive Peptides: A Literature Update

Nong

Hsu

2021

IJMS

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Diabetes, a glucose metabolic disorder, is considered one of the biggest challenges associated with a complex complication of health crises in the modern lifestyle. Inhibition or reduction of the dipeptidyl peptidase IV (DPP-IV), alpha-glucosidase, and protein-tyrosine phosphatase 1B (PTP-1B) enzyme activities or expressions are notably considered as the promising therapeutic strategies for the management of type 2 diabetes (T2D). Various food protein-derived antidiabetic bioactive peptides have been isolated and verified. This review provides an overview of the DPP-IV, PTP-1B, and α-glucosidase inhibitors, and updates on the methods for the discovery of DPP-IV inhibitory peptides released from food-protein hydrolysate. The finding of novel bioactive peptides involves studies about the strategy of separation fractionation, the identification of peptide sequences, and the evaluation of peptide characteristics in vitro, in silico, in situ, and in vivo. The potential of bioactive peptides suggests useful applications in the prevention and management of diabetes. Furthermore, evidence of clinical studies is necessary for the validation of these peptides’ efficiencies before commercial applications.

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Section: Food Protein-derived α-Glucosidase Inhibition Peptidesmentioning

confidence: 99%

Characteristics of Food Protein-Derived Antidiabetic Bioactive Peptides: A Literature Update

Nong

Hsu

2021

IJMS

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“…The eluted fractions exhibiting a single peak is observed to be rich in an active enzyme (protease) and was observed to occur at a retention time of 10 min. The flow rate maintained was 1.0 ml/min throughout the process to reduce discrepancy during purification 32 . The total retention volume was calculated to be 24.03 ml (Fig.…”

Section: Resultsmentioning

confidence: 99%

One-pot simultaneous production and sustainable purification of fibrinolytic protease from Bacillus cereus using natural deep eutectic solvents

Rathnasamy

Durai

Vigneshkumar

et al. 2020

Sci Rep

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“…A size exclusion column (Sephadex G-15, AKTA prime plus, GE, USA) of 5 ml volume was used for the fractionation of the enzyme. The column was equilibrated with (20 mM phosphate buffer, pH 7) before the sample injection to set the baseline at zero 26 . The flow rate throughout the process is maintained constant at 1 ml/min.…”

Section: Methodsmentioning

confidence: 99%

Simultaneous production and sustainable eutectic mixture based purification of narringinase with Bacillus amyloliquefaciens by valorization of tofu wastewater

Balaraman

Purushotaman

Chandramouliswaran

et al. 2022

Sci Rep

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The current investigation is being executed for sustainable one-pot production and purification of naringinase using natural deep eutectic solvent-based extractive fermentation. Five natural deep eutectic solvents were prepared and their physicochemical properties were determined as a function of temperature. Tofu wastewater was used as a low-cost substrate for naringinase production and simultaneous in-situ purification of the enzyme was accomplished by employing NADES. Optimal conditions of influential factors like concentrations of NADES (74.5% w/w), Na2SO4 (15% w/v) and tofu wastewater (1.5% w/w) resulted in an effective yield of naringinase (249.6 U/ml). Scale-up of naringinase production with a 3 l custom made desktop bioreactor was accomplished and effective regeneration of NADES was established. NADES exhibits selectivity during extraction even after the fifth cycle proving it to be tailor-made. The resulting active enzyme was quantified by size exclusion chromatography (736.85 U/mg). Ultrapure enzyme fraction was obtained with anion exchange chromatography yielding maximum purity of (63.2 U/ml) and specific naringinase activity of (3516 U/mg). The in-vitro debittering activity of the resulting ultrapure enzyme fraction was determined with grape juice resulting in naringin and limonin removal of [23.4% (w/w)] and [64.3% (w/w)] respectively.

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Task-specific deep eutectic solvent based extraction coupled cascade chromatography quantification of α-glucosidase inhibitory peptide from Ocimum tenuriflorum seeds

Cited by 20 publications

References 41 publications

Characteristics of Food Protein-Derived Antidiabetic Bioactive Peptides: A Literature Update

Characteristics of Food Protein-Derived Antidiabetic Bioactive Peptides: A Literature Update

One-pot simultaneous production and sustainable purification of fibrinolytic protease from Bacillus cereus using natural deep eutectic solvents

Simultaneous production and sustainable eutectic mixture based purification of narringinase with Bacillus amyloliquefaciens by valorization of tofu wastewater

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