Hydrolyzates from Pyropia columbina seaweed have antiplatelet aggregation, antioxidant and ACE I inhibitory peptides which maintain bioactivity after simulated gastrointestinal digestion

Cian, Raúl E.; Garzón, Antonela Guadalupe; Ancona, David Betancur; Chel‐Guerrero, Luis; Drago, Silvina Rosa

doi:10.1016/j.lwt.2015.06.043

Cited by 100 publications

(60 citation statements)

References 46 publications

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“…Finally, it is important to note that several studies have reported that short algae-derived peptides are capable of resisting gastrointestinal digestion from enzymes such as trypsin, pepsin, and chymotrypsin [203,207,235]. This is an essential trait for bioactive peptides in order to achieve their physiological effect at their site of action [236].…”

Section: Applicationsmentioning

confidence: 99%

Algal Proteins: Extraction, Application, and Challenges Concerning Production

Bleakley

Hayes

2017

Foods

733

418

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Population growth combined with increasingly limited resources of arable land and fresh water has resulted in a need for alternative protein sources. Macroalgae (seaweed) and microalgae are examples of under-exploited “crops”. Algae do not compete with traditional food crops for space and resources. This review details the characteristics of commonly consumed algae, as well as their potential for use as a protein source based on their protein quality, amino acid composition, and digestibility. Protein extraction methods applied to algae to date, including enzymatic hydrolysis, physical processes, and chemical extraction and novel methods such as ultrasound-assisted extraction, pulsed electric field, and microwave-assisted extraction are discussed. Moreover, existing protein enrichment methods used in the dairy industry and the potential of these methods to generate high value ingredients from algae, such as bioactive peptides and functional ingredients are discussed. Applications of algae in human nutrition, animal feed, and aquaculture are examined.

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Section: Applicationsmentioning

confidence: 99%

Algal Proteins: Extraction, Application, and Challenges Concerning Production

Bleakley

Hayes

2017

Foods

733

418

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“…It has been recorded that presence of proline and hydroxyl proline results in peptide resistance to digestive enzymes, especially tripeptides with Pro‐Pro at the C‐terminal that are resistant to proline‐specific peptides (FitzGerald and Meisel ). Generally, most of the reported seaweed protein–derived peptides with antioxidant activity were those with low molecular weights (Wang and others , ; Cian and others , , , ).…”

Section: Bioactivities Of Seaweed Protein‐derived Peptidesmentioning

confidence: 99%

Bioactive Peptides Derived from Seaweed Protein and Their Health Benefits: Antihypertensive, Antioxidant, and Antidiabetic Properties

Admassu

Gasmalla

Yang

et al. 2017

Journal of Food Science

229

130

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Cardiovascular diseases and diabetes are the biggest causes of death globally. Therefore, prevention of these diseases is a focus of pharmaceuticals and functional food manufacturers. This review summarizes recent research trends and scientific knowledge in seaweed protein-derived peptides with particular emphasis on production, isolation and potential health impacts in prevention of hypertension, diabetes and oxidative stress. The current status and future prospects of bioactive peptides are also discussed. Bioactive peptides have strong potential for use in therapeutic drug and functional food formulation in health management strategy, especially cardiovascular disease and diabetes. Seaweeds can be used as sustainable protein sources in the production of these peptide-based drugs and functional foods for preventing such diseases. Many studies have reported that peptides showing angiotensin converting enzyme inhibition, antihypertensive, antioxidative and antidiabetics activities, have been successfully isolated from seaweed. However, further research is needed in large-scale production of these peptides, efficient isolation methods, interactions with functional foods and other pharmaceuticals, and their ease to digestion in in vivo studies and safety to validate the health benefits of these peptides.

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“…It is known that intact dipeptides and tripeptides can be actively transported through the small intestine. However, data describing the enteral absorption of intact oligopeptides larger than two or three amino acids are rather conflicting as most of the peptides can be susceptible to proteolytic degradation during gastrointestinal digestion by cell enzymes (Cian et al, 2015;Gallego et al, 2016). However, peptides showing a proline residue at the C-terminus have been described to be more resistant to enzymatic hydrolysis, so this fact suggests that small bioactive peptides identified in the muscle hydrolysate of thornback ray showing Pro residue at different positions of the Cterminal site such as FQPSF, TLKYP or LKYPI might be active not only in vitro but also in vivo, although further analysis would be necessary for confirmation.…”

Section: Identification Of Ace Inhibitory Peptides By Tandem Mass Spementioning

confidence: 99%

Angiotensin I‐converting enzyme inhibitory peptides FQPSF and LKYPI identified in Bacillus subtilis A26 hydrolysate of thornback ray muscle

Lassoued

Mora

Barkia

et al. 2016

Int J of Food Sci Tech

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Summary Angiotensin I‐converting enzyme (ACE) inhibitory peptides have been searched in thornback ray (Raja clavata) muscle hydrolysed with Bacillus subtilis A26 proteases until a hydrolysis degree of 18.35%. The hydrolysate showed an IC50 of 0.83 mg mL−1. To identify peptides responsible for this activity, the extract was eluted through size‐exclusion chromatography and fractions collected. The highest ACE inhibitory activity was found for fractions F2 and F3 which had IC50 of 0.42 and 0.51 mg mL−1, respectively. These fractions were analysed by nano‐liquid chromatography coupled to tandem mass spectrometry (nLC‐MS/MS). A total of 131 and 108 peptide sequences mainly derived from actin, myosin heavy chain and procollagen alpha 1 chain proteins were identified in fractions F2 and F3, respectively. FQPSF and LKYPI showed the best results with an IC50 of 12.56 and 27.07 μM, respectively. These results prove the potential of thornback ray muscle hydrolysate as a source of ACE inhibitory peptides.

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Hydrolyzates from Pyropia columbina seaweed have antiplatelet aggregation, antioxidant and ACE I inhibitory peptides which maintain bioactivity after simulated gastrointestinal digestion

Cited by 100 publications

References 46 publications

Algal Proteins: Extraction, Application, and Challenges Concerning Production

Algal Proteins: Extraction, Application, and Challenges Concerning Production

Bioactive Peptides Derived from Seaweed Protein and Their Health Benefits: Antihypertensive, Antioxidant, and Antidiabetic Properties

Angiotensin I‐converting enzyme inhibitory peptides FQPSF and LKYPI identified in Bacillus subtilis A26 hydrolysate of thornback ray muscle

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