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Mini-Review Article

Bioactive Peptides in Preventative Healthcare: An Overview of Bioactivities and Suggested Methods to Assess Potential Applications

Author(s): Maria Hayes*

Volume 27, Issue 11, 2021

Published on: 25 January, 2021

Page: [1332 - 1341] Pages: 10

DOI: 10.2174/1381612827666210125155048

Price: $65

Abstract

Food derived bioactive peptides can be generated from various protein sources and usually consist of between 2-30 amino acids with bulky, side-chain aromatic amino acids preferred in the ultimate and penultimate positions at the C-terminal end of the amino acid chain. They are reported to impart a myriad of preventative health beneficial effects to the consumer once ingested and these include heart health benefits through inhibition of enzymes including renin (EC 3.4.23.15) and angiotensin- I-converting enzyme (ACE-1; EC 3.4.15.1) within the renin angiotensin aldosterone system (RAAS) anti-inflammatory (due to inhibition of ACE-I and other enzymes) and anti-cancer benefits, prevention of type-2 diabetes through inhibition of dipeptidyl peptidase IV (DPP-IV), bone and dental strength, antimicrobial and immunomodulatory effects and several others. Peptides have also reported health benefits in the treatment of asthma, neuropathic pain, HIV and wound healing. However, the structure, amino acid composition and length of these peptides, along with the quantity of peptide that can pass through the gastrointestinal tract and often the blood-brain barrier (BBB), intact and reach the target organ, are important for the realisation of these health effects in an in vivo setting. This paper aims to collate recent important research concerning the generation and detection of peptides in the laboratory. It discusses products currently available as preventative healthcare peptide options and relevant legislation barriers to place a food peptide product on the market. The review also highlights useful in silico computer- based methods and analysis that may be used to generate specific peptide sequences from proteins whose amino acid sequences are known and also to determine if the peptides generated are unique and bioactive. The topic of food-derived bioactive peptides for health is of great interest to scientific research and industry due to evolving drivers in food product innovation, including health and wellness for the elderly, infant nutrition and optimum nutrition for sports athletes and the humanisation of pets. This paper provides an overview of what is required to generate bioactive peptide containing hydrolysates, what methods should be used in order to characterise the beneficial health effects of these hydrolysates and the active peptide sequences, potential applications of bioactive peptides and legislative requirements in Europe and the United States. It also highlights success stories and barriers to the development of peptide-containing food products that currently exist.

Keywords: Angiotensin-I-converting enzyme (ACE-I), antihypertensive activity, Dipeptidyl peptidase IV (DPP-IV), European Food Safety Authority (EFSA), in silico, peptides, renin inhibitory, acetylcholinesterase inhibition, mental health.

« Previous Next »
[1]
Schrader M, Schulz-Knappe P, Fricker LD. Historical perspective of peptidomics. EuPA Open Proteom 2014; 3: 171-82.
[http://dx.doi.org/10.1016/j.euprot.2014.02.014]
[2]
Hayes M, Stanton C, Slattery H, et al. Casein fermentate of Lactobacillus animalis DPC6134 contains a range of novel propeptide angiotensin-converting enzyme inhibitors. Appl Environ Microbiol 2007; 73(14): 4658-67.
[http://dx.doi.org/10.1128/AEM.00096-07] [PMID: 17483275]
[3]
Mellander O. The physiological importance of the casein phosphopeptide calcium salts. II. Peroral calcium dosage of infants. Acta Soc Med Ups 1950; 55(5-6): 247-55.
[PMID: 15443982]
[4]
Raikos V, Dassios T. Health-promoting properties of bioactive peptides derived from milk proteins in infant food: a review. Dairy Sci Technol 2014; 94(2): 91-101.
[http://dx.doi.org/10.1007/s13594-013-0152-3] [PMID: 24511365]
[5]
Lafarga T, O’Connor P, Hayes M. In silico methods to identify meat-derived prolyl endopeptidase inhibitors. Food Chem 2015; 175: 337-43.
[http://dx.doi.org/10.1016/j.foodchem.2014.11.150] [PMID: 25577089]
[6]
Udenigwe CC, Gong M, Wu S. In silico analysis of the large and small subunits of cereal RuBisCO as precursors of cryptic bioactive peptides. Process Biochem 2013; 48: 1794-9.
[http://dx.doi.org/10.1016/j.procbio.2013.08.013]
[7]
Moughan PJ, Rutherfurd SM, Montoya CA, Dave LA. Food-derived bioactive peptides--a new paradigm. Nutr Res Rev 2014; 27(1): 16-20.
[http://dx.doi.org/10.1017/S0954422413000206] [PMID: 24231033]
[8]
Korhonen H, Pihlanto A. Bioactive peptides: Production and Functionality. Int Dairy J 2006; 16(9): 945-60.
[http://dx.doi.org/10.1016/j.idairyj.2005.10.012]
[9]
Kęska P, Wójciak KM, Stadnik J. Bioactive peptides from beef products fermented by acid whey – in vitro and in silico study. Sci Agric 2019; 76(4): 311-20.
[http://dx.doi.org/10.1590/1678-992x-2018-0114]
[10]
Di Bernardini R, Mullen AM, Bolton D, Kerry J, O’Neill E, Hayes M. Assessment of the angiotensin-I-converting enzyme (ACE-I) inhibitory and antioxidant activities of hydrolysates of bovine brisket sarcoplasmic proteins produced by papain and characterisation of associated bioactive peptidic fractions. Meat Sci 2012; 90(1): 226-35.
[http://dx.doi.org/10.1016/j.meatsci.2011.07.008] [PMID: 21880436]
[11]
Hayes M, Ross RP, Fitzgerald GF, Hill C, Stanton C. Casein-derived antimicrobial peptides generated by Lactobacillus acidophilus DPC6026. Appl Environ Microbiol 2006; 72(3): 2260-4.
[http://dx.doi.org/10.1128/AEM.72.3.2260-2264.2006] [PMID: 16517684]
[12]
Fitzgerald C, Mora-Soler L, Gallagher E, et al. Isolation and characterization of bioactive pro-peptides with in vitro renin inhibitory activities from the macroalga Palmaria palmata. J Agric Food Chem 2012; 60(30): 7421-7.
[http://dx.doi.org/10.1021/jf301361c] [PMID: 22747312]
[13]
Pangestuti R, Kim S-K. Chapter 6 - Seaweed proteins, peptides, and amino acids. Seaweed Sustainability Academic Press. 2015; pp. pp 125-40.
[14]
Wang X, Yu H, Xing R, Chen X, Liu S, Li P. Optimization of antioxidative peptides from mackerel (Pneumatophorus japonicus) viscera. Peer J 2018; 6.
[http://dx.doi.org/10.7717/peerj.4373] [PMID: 29473003]
[15]
Gómez LJ, Gómez NA, Zapata JE, López-García G, Cilla A, Alegría A. Optimization of the red tilapia (Oreochromis spp.) viscera hydrolysis for obtaining iron-binding peptides and evaluation of in vitro iron bioavailability. Foods 2020; 9(7): 883.
[http://dx.doi.org/10.3390/foods9070883] [PMID: 32640574]
[16]
González-García E, Marina ML, García C. Plum (Prunus Domestica L.) by-product as a new and cheap source of bioactive peptides: Extraction method and peptide characterization. J Funct Foods 2014; 11: 428-37.
[http://dx.doi.org/10.1016/j.jff.2014.10.020]
[17]
Mussatto SI, Fernandes M, Mancilha IM, Roberto IC. Effects of medium supplementation and pH control on lactic acid production from brewer’s spent grain. Biochem Eng J 2008; 40: 437-44.
[http://dx.doi.org/10.1016/j.bej.2008.01.013]
[18]
Zhao L, Wang S, Liu F, et al. Comparing the effects of high hydrostatic pressure and thermal pasteurisation combined with nisin on the quality of cucumber juice drinks. Innov Food Sci Emerg Technol 2013; 2013(17): 27-36.
[http://dx.doi.org/10.1016/j.ifset.2012.10.004]
[19]
Ebner P, Luqman A, Reichert S, et al. Non-classical protein excretion is boosted by PSMα-induced cell leakage. Cell Rep 2017; 20(6): 1278-86.
[http://dx.doi.org/10.1016/j.celrep.2017.07.045] [PMID: 28793253]
[20]
Hayes M, Mora L, Hussey K, Aluko R E. Boarfish protein recovery using the pH-shift process and generation of protein hydrolysates with ACE-I and antihypertensive bioactivities in spontaneously hypertensive rats. Innov Food Sci Emerg Technol 2016; 37(Part B): 253-60.
[http://dx.doi.org/10.1016/j.ifset.2016.03.014]
[21]
Egerton S, Culloty S, Whooley J, Stanton C, Ross RP. Characterisation of protein hydrolysates from blue whiting (Micromeisistius poutassou) and their application in beverage fortification. Food Chem 2017; 245: 698-706.
[http://dx.doi.org/10.1016/j.foodchem.2017.10.107] [PMID: 29287428]
[22]
Heo S-J, Park E-J, Lee K-W, Jeon YJ. Antioxidant activities of enzymatic extracts from brown seaweeds. Bioresour Technol 2005; 96(14): 1613-23.
[http://dx.doi.org/10.1016/j.biortech.2004.07.013] [PMID: 15978995]
[23]
Walker LM, York JL, Imam SZ, Ali SF, Muldrew KL, Mayeux PR. Oxidative stress and reactive nitrogen species generation during renal ischemia. Toxicol Sci 2001; 63(1): 143-8.
[http://dx.doi.org/10.1093/toxsci/63.1.143] [PMID: 11509754]
[24]
Liu Q, Kong B, Xiong YL, Xia X. Antioxidant activity and functional properties of porcine plasma protein hydrolysate as influenced by the degree of hydrolysis. Food Chem 2010; 118: 403-10.
[http://dx.doi.org/10.1016/j.foodchem.2009.05.013]
[25]
Prior RL, Hoang H, Gu L, et al. Assays for hydrophilic and lipophilic antioxidant capacity (oxygen radical absorbance capacity (ORAC(FL)) of plasma and other biological and food samples. J Agric Food Chem 2003; 51(11): 3273-9.
[http://dx.doi.org/10.1021/jf0262256] [PMID: 12744654]
[26]
Huang D, Ou B, Prior RL. The chemistry behind antioxidant capacity assays. J Agric Food Chem 2005; 53(6): 1841-56.
[http://dx.doi.org/10.1021/jf030723c] [PMID: 15769103]
[27]
O’ Sullivan SM, Lafarga T, Hayes M, O’ Brien NM. Bioactivity of bovine lung hydrolysates prepared using papain, pepsin and alcalase. J Food Biochem 2017; 41(6): e12406.
[http://dx.doi.org/10.1111/jfbc.12406]
[28]
García-Nebot MJ, Recio I, Hernández-Ledesma B. Antioxidant activity and protective effects of peptide lunasin against oxidative stress in intestinal Caco-2 cells. Food Chem Toxicol 2014; 65: 155-61.
[http://dx.doi.org/10.1016/j.fct.2013.12.021] [PMID: 24365261]
[29]
Kim SK, Kim YT, Byun HG, Nam KS, Joo DS, Shahidi F. Isolation and characterization of antioxidative peptides from gelatin hydrolysate of Alaska pollack skin. J Agric Food Chem 2001; 49(4): 1984-9.
[http://dx.doi.org/10.1021/jf000494j] [PMID: 11308357]
[30]
Wang J, Hu J, Cui J, et al. Purification and identification of a ACE inhibitory peptide from oyster proteins hydrolysate and the antihypertensive effect of hydrolysate in spontaneously hypertensive rats. Food Chem 2008; 111(2): 302-8.
[http://dx.doi.org/10.1016/j.foodchem.2008.03.059] [PMID: 26047427]
[31]
Lee S-H, Qian Z-J, Kim S-K. A novel angiotensin I converting enzyme inhibitory peptide from tuna frame protein hydrolysate and its antihypertensive effect in spontaneously hypertensive rats. Food Chem 2010; 118: 96-102.
[http://dx.doi.org/10.1016/j.foodchem.2009.04.086]
[32]
Di Bernardini R, Rai DK, Bolton D, et al. Isolation, purification and characterization of antioxidant peptidic fractions from a bovine liver sarcoplasmic protein thermolysin hydrolyzate. Peptides 2011; 32(2): 388-400.
[http://dx.doi.org/10.1016/j.peptides.2010.11.024] [PMID: 21129427]
[33]
Rustad T. Utilisation of marine by-product. Elec J Env Agric Food Chem 2003; 2(4): 458-63.
[34]
Gangopadhyay N, Wynne K, O’Connor P, et al. In silico and in vitro analyses of the angiotensin-I converting enzyme inhibitory activity of hydrolysates generated from crude barley (Hordeum vulgare) protein concentrates. Food Chem 2016; 203: 367-74.
[http://dx.doi.org/10.1016/j.foodchem.2016.02.097] [PMID: 26948626]
[35]
Moslemi F, Taheri P, Azimipoor M, et al. Effect of angiotensin II type 1 receptor blockade on kidney ischemia/reperfusion; a gender-related difference. J Renal Inj Prev 2016; 5(3): 140-3.
[http://dx.doi.org/10.15171/jrip.2016.29] [PMID: 27689110]
[36]
Hicks BM, Filion KB, Yin H, Sakr L, Udell JA, Azoulay L. Angiotensin converting enzyme inhibitors and risk of lung cancer: population based cohort study. BMJ 2018; 363: k4209.
[http://dx.doi.org/10.1136/bmj.k4209] [PMID: 30355745]
[37]
Asgharpour M, Ebrahimi Kalan M, Mirhashemi S H, Alirezaei A. Lung cancer risk and the inhibitors of angiotensin converting enzyme: A mini-review of recent evidence. Immunopathol Persa 2019; 5(2): e6.
[38]
Chakrabarti S, Jahandideh F, Wu J. Food-derived bioactive peptides on inflammation and oxidative stress. BioMed Res Int 2014; 2014
[http://dx.doi.org/10.1155/2014/608979] [PMID: 24527452]
[39]
Derwa Y, Gracie DJ, Hamlin PJ, Ford AC. Systematic review with meta-analysis: the efficacy of probiotics in inflammatory bowel disease. Aliment Pharmacol Ther 2017; 46(4): 389-400.
[http://dx.doi.org/10.1111/apt.14203] [PMID: 28653751]
[40]
He R, Aluko RE, Ju X-R. Evaluating molecular mechanism of hypotensive peptides interactions with renin and angiotensin converting enzyme. PLoS One 2014; 9(3): e91051.
[http://dx.doi.org/10.1371/journal.pone.0091051] [PMID: 24603692]
[41]
He R, Malomo SA, Alashi A, Girgih AT, Ju X. Purification and hypotensive activity of rapeseed protein-derived renin and angiotensin converting enzyme inhibitory peptides. J Funct Foods 2013; 5: 781-9.
[http://dx.doi.org/10.1016/j.jff.2013.01.024]
[42]
Moughan PJ, Souffrant WB, Hodgkinson SM. Physiological approaches to determining gut endogenous amino acid flows in the mammal. Arch Tierernahr 1998; 51(2-3): 237-52.
[http://dx.doi.org/10.1080/17450399809381922] [PMID: 9672720]
[43]
Fitzgerald C, Aluko RE, Hossain M, Rai DK, Hayes M. Potential of a renin inhibitory peptide from the red seaweed Palmaria palmata as a functional food ingredient following confirmation and characterization of a hypotensive effect in spontaneously hypertensive rats. J Agric Food Chem 2014; 62(33): 8352-6.
[http://dx.doi.org/10.1021/jf500983n] [PMID: 25062358]
[44]
Fitzgerald C, Gallagher E, O’Connor P, et al. Development of a seaweed derived platelet activating factor acetylhydrolase (PAF-AH) inhibitory hydrolysate, synthesis of inhibitory peptides and assessment of their toxicity using the Zebrafish larvae assay. Peptides 2013; 50: 119-24.
[http://dx.doi.org/10.1016/j.peptides.2013.10.006] [PMID: 24140404]
[45]
Pihlanto A, Mäkinen S. The function of renin and the role of food-derived peptides as direct renin inhibitors, renin-angiotensin system - past, present and future 2017 2017. Available from: https://www.intechopen.com/books/renin-angiotensin-system-past-present-and-future/the-function-of-renin-and-the-role-of-food-derived-peptides-as-direct-renin-inhibitors
[46]
Kasina S. Dipeptidyl Peptidase IV (DPP IV) inhibitors. StatPearl 2019. Available from: https://www.ncbi.nlm.nih.gov/books/NBK542331/
[47]
Lacroix IME, Li-Chan ECY. Inhibition of dipeptidyl peptidase (DPP)-IV and α-glucosidase activities by pepsin-treated whey proteins. J Agric Food Chem 2013; 61(31): 7500-6.
[http://dx.doi.org/10.1021/jf401000s] [PMID: 23837435]
[48]
Zambrowicz A, Pokora M, Setner B, et al. Multifunctional peptides derived from an egg yolk protein hydrolysate: isolation and characterization. Amino Acids 2015; 47(2): 369-80.
[http://dx.doi.org/10.1007/s00726-014-1869-x] [PMID: 25408464]
[49]
Gallego M, Aristoy MC, Toldrá F. Dipeptidyl peptidase IV inhibitory peptides generated in Spanish dry-cured ham. Meat Sci 2014; 96(2 Pt A): 757-61.
[http://dx.doi.org/10.1016/j.meatsci.2013.09.014] [PMID: 24200567]
[50]
Lacroix I M E, Chen X M, Kitts D D, Li-Chen E C Y. Investigation into the bioavailability of milk protein-derived peptides with Dipeptidyl peptidase IV inhibitory activity using Caco-2 cell monolayers. Food Funct 2017; 8(2): 701-9.
[http://dx.doi.org/10.1039/C6FO01411A]
[51]
Zhang Y, Chen R, Chen X, Zeng Z, Ma H, Chen S. Dipeptidyl peptidase IV inhibitory peptides derived from Silver Carp (Hypophthalmichthus molitrix Val.) Proteins. J Agric Food Chem 2016; 64(4): 831-9.
[http://dx.doi.org/10.1021/acs.jafc.5b05429] [PMID: 26758401]
[52]
Prasasty V, Radifar M, Istayastono E. Natural peptides in drug discovery targeting acetylcholinesterase. Molecules 2018; 23(9): 2344.
[http://dx.doi.org/10.3390/molecules23092344]
[53]
Sanchis I, Spinelli R, Aschemacher N, Humpola MV, Siano A. Acetylcholinesterase inhibitory activity of a naturally occurring peptide isolated from Boana pulchella (Anura: Hylidae) and its analogs. Amino Acids 2020; 52(3): 387-96.
[http://dx.doi.org/10.1007/s00726-019-02815-1] [PMID: 31902008]
[54]
Malomo S A, Aluko R E. Kinetics of acetylcholinesterase inhibition by hemp seed protein derived peptides. J Food Biochem 2019; 43(7): e12897.
[http://dx.doi.org/10.1111/jfbc.12897]
[55]
Ferreira A, Proença C, Serralheiro ML, Araújo ME. The in vitro screening for acetylcholinesterase inhibition and antioxidant activity of medicinal plants from Portugal. J Ethnopharmacol 2006; 108(1): 31-7.
[http://dx.doi.org/10.1016/j.jep.2006.04.010] [PMID: 16737790]
[56]
Deptula M, Wardowska A, Dzierzynska M. Antibacterial peptides in Dermatology - Strategies for evaluation of allergic potential. Molecules 2018; 23(2): 414.
[57]
Kumar P, Kizhakkedathu JN, Straus SK. Antimicrobial peptides: diversity, mechanism of action and strategies to improve the activity and biocompatibility in vivo. Biomolecules 2018; 8(1): 4.
[http://dx.doi.org/10.3390/biom8010004] [PMID: 29351202]
[58]
Bakare OO, Fadaka AO, Klein O, Pretorius A. Dietary effects of antimicrobials in therapeutics. All Life 2020; 13(1): 78-91.
[http://dx.doi.org/10.1080/26895293.2020.1726826]
[59]
Lahov E, Regelson W. Antibacterial and immunostimulating casein-derived substances from milk: casecidin, isracidin peptides. Food Chem Toxicol 1996; 34(1): 131-45.
[http://dx.doi.org/10.1016/0278-6915(95)00097-6] [PMID: 8603791]
[60]
Wang G, Watson KM, Peterkofsky A, Buckheit RW Jr. Identification of novel human immunodeficiency virus type 1-inhibitory peptides based on the antimicrobial peptide database. Antimicrob Agents Chemother 2010; 54(3): 1343-6.
[http://dx.doi.org/10.1128/AAC.01448-09] [PMID: 20086159]
[61]
Trivedi M, Zhang Y, Lopez-Toledano M, Clarke A, Deth R. Differential neurogenic effects of casein-derived opioid peptides on neuronal stem cells: implications for redox-based epigenetic changes. J Nutr Biochem 2016; 37: 39-46.
[http://dx.doi.org/10.1016/j.jnutbio.2015.10.012] [PMID: 27611101]
[62]
Wilson J, Hayes M, Carney B. Angiotensin-I-converting enzyme and prolyl endopeptidase inhibitory peptides from natural sources with a focus on marine processing by-products. Food Chem 2011; 129(2): 235-44.
[http://dx.doi.org/10.1016/j.foodchem.2011.04.081] [PMID: 30634221]
[63]
Hayes M, Moen LF, Auty MAE, Lea TE. Transport of a prolyl endopeptidase inhibitory peptide across the blood brain barrier demonstrated using the hCMEC/D3 cell line transcytosis assay. J Agric Food Chem 2016; 64(1): 146-50.
[http://dx.doi.org/10.1021/acs.jafc.5b04696] [PMID: 26716467]
[64]
Morain P, Lestage P, De Nanteuil G, et al. S 17092: a prolyl endopeptidase inhibitor as a potential therapeutic drug for memory impairment. Preclinical and clinical studies. CNS Drug Rev 2002; 8(1): 31-52.
[http://dx.doi.org/10.1111/j.1527-3458.2002.tb00214.x] [PMID: 12070525]
[65]
Ting Y, Zhao Q, Xia C, Huang Q. Using in vitro and in vivo models to evaluate the oral bioavailability of nutraceuticals. J Agric Food Chem 2015; 63(5): 1332-8.
[http://dx.doi.org/10.1021/jf5047464] [PMID: 25615514]
[66]
Minekus M. The TNO Gastro-Intestinal Model (TIM-1). The impact of Food Bioactives on Health. 2015; pp. 37-46. Cham:Springer
[67]
Cavonius LR, Albers E, Undeland I. pH-shift processing of Nannochloropsis oculata microalgal biomass to obtain a protein-enriched food or feed ingredient. Algal Res 2015; 11: 95-102.
[http://dx.doi.org/10.1016/j.algal.2015.05.022]
[68]
Sousa R, Portmann R, Dubois S, Recio I, Egger L. Protein digestion of different protein sources using the INFOGEST static digestion model. Food Res Int 2020; 130.
[http://dx.doi.org/10.1016/j.foodres.2020.108996] [PMID: 32156409]
[69]
Carbonell-Capella JM, Buniowska M, Barba FJ, Esteve MJ, Frígola A. Analytical methods for determining bioavailability and bioaccessibility of bioactive compounds from fruits and vegetables: A review. Compr Rev Food Sci Food Saf 2014; 13: 155-71.
[http://dx.doi.org/10.1111/1541-4337.12049]
[70]
Glahn RP, Wien EM, Van Campen DR, Miller DD. Caco-2 cell iron uptake from meat and casein digests parallels in vivo studies: use of a novel in vitro method for rapid estimation of iron bioavailability. J Nutr 1996; 126(1): 332-9.
[http://dx.doi.org/10.1093/jn/126.1.332] [PMID: 8558319]
[71]
Glahn RP, Lee OA, Yeung A, Goldman MI, Miller DD. Caco-2 cell ferritin formation predicts non radiolabeled food iron availability in an in vitro digestion Caco-2 cell culture model. J Nutr 1998; 128: 155-61.
[72]
Rutherfurd SM, Fanning AC, Miller BJ, Moughan PJ. Protein digestibility-corrected amino acid scores and digestible indispensable amino acid scores differentially describe protein quality in growing male rats. J Nutr 2015; 145(2): 372-9.
[http://dx.doi.org/10.3945/jn.114.195438] [PMID: 25644361]
[73]
Minkiewicz P, Dziuba J, Iwaniak A, Dziuba M, Darewicz M. BIOPEP database and other programs for processing bioactive peptide sequences. J AOAC Int 2008; 91(4): 965-80.
[http://dx.doi.org/10.1093/jaoac/91.4.965] [PMID: 18727559]
[74]
Dziuba M, Minkiewicz P, Dąbek M. Peptides, specific proteolysis products, as molecular markers of allergenic proteins - in silico studies. Acta Sci Pol Technol Aliment 2013; 12(1): 101-12.
[PMID: 24584870]
[75]
Parmar H, Hati S, Sakure A. In vitro and in silico analysis of novel ACE-inhibitory peptides derived from fermented goat milk. Int J Pept Res Ther 2017; 24 (3).
[http://dx.doi.org/10.1007/s10989-017-9630-4]
[76]
Porter Y. Antioxidant properties of green broccoli and purple sprouting broccoli under different cooking conditions. Biosci Horiz 2012.
[http://dx.doi.org/10.1093/biohorizons/hzs004]
[77]
Dave LA, Hayes M, Mora L, Montoya CA, Moughan PJ, Rutherfurd SM. Gastrointestinal endogenous protein-derived bioactive peptides: An in vitro study of their gut modulatory potential. Int J Mol Sci 2016; 17(4): 482-6.
[http://dx.doi.org/10.3390/ijms17040482] [PMID: 27043546]
[78]
Westerhout J, Krone T, Snippe A, et al. Allergenicity prediction of novel and modified proteins: Not a mission impossible! Development of a Random Forest allergenicity prediction model. Regul Toxicol Pharmacol 2019; 107.
[http://dx.doi.org/10.1016/j.yrtph.2019.104422] [PMID: 31310847]
[79]
Hayes M, Rougé P, Barre A, Herouet-Guicheney C, Roggen EL. In silico tools for exploring human allergy to proteins. Drug Discov Today Dis Models 2015; 17-18: 3-11.
[http://dx.doi.org/10.1016/j.ddmod.2016.06.001]
[80]
Lafarga T, Hayes M. Effect of pre-treatment on the generation of dipeptidyl peptidase-IV and prolyl endopeptidase inhibitory hydrolysates from bovine lung. Ir J Agric Food Res 2017; 56(1): 12-24.
[http://dx.doi.org/10.1515/ijafr-2017-0002]

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