Production of bioactive peptide hydrolysates from deer, sheep and pig plasma using plant and fungal protease preparations

Bah, Clara Shui Fern; Bekhit, Alaa El‐Din A.; Carne, Alan; McConnell, Michelle

doi:10.1016/j.foodchem.2014.12.025

Cited by 52 publications

(29 citation statements)

References 26 publications

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“…Triplicate pooled blood samples were collected from the abattoir's blood waste stream. As described in Bah et al (2015), sodium citrate (10 g/L) was added to the blood to prevent coagulation. To separate the plasma fraction from the blood cell fraction, whole blood was centrifuged at 2060 ×g, 4°C for 15 minutes.…”

Section: Blood Collection and Separationmentioning

confidence: 99%

“…The following hydrolysis conditions were used as described by Bah et al (2015): (i) papain: at pH 6.5 and 55°C; (ii) bromelain: at pH 6.5 and 50°C; (iii) FP400: at pH 6.5 and 50°C; and (iv) FPII: at pH 6.5 and 50°C. The ratio of protease preparation-to-substrate was 1:10 on a weight basis, for all hydrolysis treatments.…”

Section: Proteolytic Hydrolysis Of Cattle Plasmamentioning

confidence: 99%

“…4 categories of protease preparations (plant and fungal) and the antioxidant activities of the resulting hydrolysates (Bah, Bekhit, Carne, & McConnell, 2015). Furthermore, while some researchers have reported the antioxidant activities of blood hydrolysates, not many studies have purified the hydrolysates to identify the peptides responsible for antioxidant activity.…”

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Generation of bioactive peptide hydrolysates from cattle plasma using plant and fungal proteases

et al. 2016

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Section: Blood Collection and Separationmentioning

confidence: 99%

Section: Proteolytic Hydrolysis Of Cattle Plasmamentioning

confidence: 99%

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Generation of bioactive peptide hydrolysates from cattle plasma using plant and fungal proteases

et al. 2016

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“…Peptide contents of hydrolysates and membrane ultrafiltration fractions were determined by using o-phthaldialdehyde (OPA) reagent [1]. Casein peptone was used to generate a standard curve for the assay.…”

Section: Determination Of Peptide Contentsmentioning

confidence: 99%

“…In recent years, the antioxidant potential of protein hydrolysates derived from edible fishes and other animal sources has generated great interests among researchers [1][2][3]. Proteases of plant, animal and microbial origins, such as papain, trypsin, chymotrypsin, neutrase, and alcalase, have been used in the production of antioxidative fish protein hydrolysates (FPH) [2,3].…”

Section: Introductionmentioning

confidence: 99%

Anti-oxidative, metal chelating and radical scavenging effects of protein hydrolysates from blue-spotted stingray

Chai¹,

Tong²,

Law³

et al. 2015

Trop. J. Pharm Res

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Enzymatic hydrolysis as a valorization strategy of bovine lungs: Optimization of process variables and study of antioxidant capacity

et al. 2023

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Background The increase in meat production would also imply an increase in the generation of by‐products or edible offal. These by‐products can be used, due to their high protein content, as a substrate to obtain hydrolysates with functional activities. This study aimed to valorize bovine lungs by producing hydrolysates with antioxidant capacity. Results A response surface methodology study was carried out using a central composite design in which factors were temperature (43.2–76.8°C), enzyme/substrate ratio [ES: 0.65–4.85% (w/w)] using Alcalase 2.4 L/Flavourzyme (1:1) and pH (5.8–9.2). The antioxidant capacity of the obtained BLH (bovine lung hydrolysates) was evaluated by the ABTS, DPPH, and FRAP methods. The maximum antioxidant capacity was achieved at 53.°C, ES ratio of 2.3% (w/w), and pH of 8.2. Under optimal hydrolysis conditions, the antioxidant capacity increased rapidly from the beginning of the reaction to 30 min, reaching a maximum at 120 min; then, it decreased until the end (180 min). The degree of hydrolysis increased as hydrolysis occurred up to a maximum of 45%. Molecular weight distribution of BLH evaluated by Tricine‐SDS‐PAGE and SEC‐FPLC showed that bovine lung proteins hydrolyzed for 120 min presented low molecular weight peptides (<5 kDa), which are absent in the non‐hydrolyzed sample. Conclusion In this work, we optimized the variables for producing BLH with antioxidant capacity using commercial proteases in a short reaction time, making it a worthwhile strategy for the recovery of by‐products from the meat industry.

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Production of bioactive peptide hydrolysates from deer, sheep and pig plasma using plant and fungal protease preparations

Cited by 52 publications

References 26 publications

Generation of bioactive peptide hydrolysates from cattle plasma using plant and fungal proteases

Generation of bioactive peptide hydrolysates from cattle plasma using plant and fungal proteases

Anti-oxidative, metal chelating and radical scavenging effects of protein hydrolysates from blue-spotted stingray

Enzymatic hydrolysis as a valorization strategy of bovine lungs: Optimization of process variables and study of antioxidant capacity

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