Abstract
Bioactive peptides can be defined as isolated small fragments of proteins which provide some physiological health benefits. They act as potential modifiers reducing the risk of many chronic diseases. To the best of our knowledge, limited literature is available for the methods of isolation of these peptides from different protein sources with their in vitro and vivo physiological effects. Also, there is a need to adopt healthy lifestyle choices for prevention of diseases, to counter increase in consumption of functional foods and nutraceuticals day-by-day. Thus, these peptides play a major role in the development of various functional foods. In the present study, attempts are made to review different physiological effects from peptides. Also, effects of processing on the peptides are discussed with special emphasis on its bioavailability, safety and future application for further development.
This is a preview of subscription content, log in via an institution to check access.
Similar content being viewed by others
References
Abdel-Hamid M, Otte J, Gobba CD et al (2017) Angiotensin I-converting enzyme inhibitory activity and antioxidant capacity of bioactive peptides derived from enzymatic hydrolysis of buffalo milk proteins. Int Dairy J 66:91–98
Adje EY, Balti R, Kouach M et al (2011) Obtaining antimicrobial peptides by controlled peptic hydrolysis of bovine hemoglobin. Int J Biol Macromol 49:143–153. https://doi.org/10.1016/j.ijbiomac.2011.04.004
Anadón A, Martínez M, Ares I et al (2010) Acute and repeated dose (4 weeks) oral toxicity studies of two antihypertensive peptides, RYLGY and AYFYPEL, that correspond to fragments (90–94) and (143–149) from α s1 -casein. Food Chem Toxicol 48:1836–1845. https://doi.org/10.1016/j.fct.2010.04.016
Arihara K (2006) Functional properties of bioactive peptides derived from meat proteins. In: Nollet LML (ed) Advanced technologies for meat processing food science and technology. CRC Press, Boca Raton, pp 245–273
Bai R, Petit GR, Hamel E (1990) Dolastatin 10, a powerful cytostatic peptide derived from a marine animal. Biochem Pharmacol 39:1941–1949. https://doi.org/10.1016/0006-2952(90)90613-p
Bellamy W, Takase M, Wakabayashi H et al (1992) Antibacterial spectrum of lactoferricin B, a potent bactericidal peptide derived from the N-terminal region of bovine lactoferrin. J Appl Bacteriol 73:472–479. https://doi.org/10.1111/j.1365-2672.1992.tb05007.x
Bitocchi E, Bellucci E, Giardini A et al (2012) Molecular analysis of the parallel domestication of the common bean (Phaseolus vulgaris) in Mesoamerica and the Andes. New Phytol 197:300–313. https://doi.org/10.1111/j.1469-8137.2012.04377.x
Boelsma E, Kloek J (2010) IPP-rich milk protein hydrolysate lowers blood pressure in subjects with stage 1 hypertension, a randomized controlled trial. Nutr J. https://doi.org/10.1186/1475-2891-9-52
Broekaert WF, Marien W, Terras FRG et al (1992) Antimicrobial peptides from Amaranthus caudatus seeds with sequence homology to the cysteine/glycine-rich domain of chitin-binding proteins. Biochemistry 31:4308–4314. https://doi.org/10.1021/bi00132a023
Chabance B, Jollès P, Izquierdo C et al (1995) Characterization of an antithrombotic peptide from α-casein in newborn plasma after milk ingestion. Br J Nutr 73:583. https://doi.org/10.1079/bjn19950060
Cheung RCF, Ng TB, Wong JH (2015) Marine peptides: bioactivities and applications. Marine drugs 13(7):4006–4043
Cicero AF, Colletti A (2016) Combinations of phytomedicines with different lipid lowering activity for dyslipidemia management: the available clinical data. Phytomedicine 23:1113–1118. https://doi.org/10.1016/j.phymed.2015.10.011
Clare D, Swaisgood H (2000) Bioactive milk peptides: a prospectus. J Dairy Sci 83:1187–1195. https://doi.org/10.3168/jds.s0022-0302(00)74983-6
Contreras MDM, Carrón R, Montero MJ et al (2009) Novel casein-derived peptides with antihypertensive activity. Int Dairy J 19:566–573. https://doi.org/10.1016/j.idairyj.2009.05.004
Daliri EBanan-Mwine, Oh DH, Byong H. Lee (2017) Bioactive peptides. Foods 6.5: 32
Darewicz M, Dziuba B, Minkiewicz P, Dziuba J (2011) The preventive potential of milk and colostrum proteins and protein fragments. Food Rev Int 27:357–388. https://doi.org/10.1080/87559129.2011.563396
Duvick DN (1992) Genetic contributions to advances in yield of US maize. Maydica (Italy)
El-Fattah AA, Sakr S, El-Dieb S, Elkashef H (2016) Angiotensin-converting enzyme inhibition and antioxidant activity of commercial dairy starter cultures. Food Sci Biotechnol 25:1745–1751. https://doi.org/10.1007/s10068-016-0266-5
Erdmann K, Grosser N, Schipporeit K, SchroÓ¦der, Henning (2006) The ACE inhibitory dipeptide Met-Tyr diminishes free radical formation in human endothelial cells via induction of heme oxygenase-1 and ferritin. J Nutr 136:2148–2152. https://doi.org/10.1093/jn/136.8.2148
Erdmann K, Cheung BW, Schröder H (2008) The possible roles of food-derived bioactive peptides in reducing the risk of cardiovascular disease. The J Nutr Biochem 19:643–654. https://doi.org/10.1016/j.jnutbio.2007.11.010
Fitzgerald RJ, Murray BA, Walsh DJ (2004) Hypotensive peptides from milk proteins. J Nutr 134(4):980S–988S
Fitzgerald RJ, Murray BA (2006) Bioactive peptides and lactic fermentations. Int J Dairy Technol 59:118–125. https://doi.org/10.1111/j.1471-0307.2006.00250.x
Freitas VM, Rangel M, Bisson LF et al (2008) The geodiamolide H, derived from brazilian sponge Geodia corticostylifera, regulates actin cytoskeleton, migration and invasion of breast cancer cells cultured in three-dimensional environment. J Cell Physiol 216:583–594. https://doi.org/10.1002/jcp.21432
Gamble WR, Durso NA, Fuller RW et al (1999) Cytotoxic and tubulin-interactive hemiasterlins from Auletta sp. and Siphonochalina spp. sponges. Biorgan Med Chem 7:1611–1615. https://doi.org/10.1016/s0968-0896(99)00089-9
Garcia-Mora P, Penas E, Frias J et al (2015) High-pressure improves enzymatic proteolysis and the release of peptides with angiotensin I converting enzyme inhibitory and antioxidant activities from lentil proteins. Food Chem 171:224–232
García-Rocha M, Bonay P, Avila J (1996) The antitumoral compound Kahalalide F acts on cell lysosomes. Cancer Lett 99:43–50. https://doi.org/10.1016/0304-3835(95)04036-6
Girgih AT, He R, Malomo S et al (2014) Structural and functional characterization of hemp seed (Cannabis sativa L.) protein-derived antioxidant and antihypertensive peptides. J Funct Foods 6:384–394. https://doi.org/10.1016/j.jff.2013.11.005
Harnedy PA, Fitzgerald RJ (2011) Bioactive proteins, peptides, and amino acids from Macroalgae1. J Phycol 47:218–232. https://doi.org/10.1111/j.1529-8817.2011.00969.x
He R, Malomo SA, Alashi A et al (2013) Purification and hypotensive activity of rapeseed protein-derived renin and angiotensin converting enzyme inhibitory peptides. J Funct Foods 5:781–789. https://doi.org/10.1016/j.jff.2013.01.024
Hernández-Ledesma B, Hsieh CC, Ben O (2009) Antioxidant and anti-inflammatory properties of cancer preventive peptide lunasin in RAW 264.7 macrophages. Biochem Biophys Res Commun 390(3):803–808
Hori K, Sato Y, Ito K et al (2007) Strict specificity for high-mannose type N-glycans and primary structure of a red alga Eucheuma serra lectin. Glycobiol 17:479–491. https://doi.org/10.1093/glycob/cwm007
Huang D, Ou B, Prior RL (2005) The chemistry behind antioxidant capacity assays. J Agri Food Chem 53(6):1841–1856
Huang Y-L, Ma M-F, Chow C-J, Tsai Y-H (2017) Angiotensin I-converting enzyme inhibitory and hypocholesterolemic activities: Effects of protein hydrolysates prepared from Achatina fulica snail foot muscle. Int J Food Prop 20:3102–3111. https://doi.org/10.1080/10942912.2016.1274904
Hung C-C, Yang Y-H, Kuo P-F, Hsu K-C (2014) Protein hydrolysates from tuna cooking juice inhibit cell growth and induce apoptosis of human breast cancer cell line MCF-7. J Funct Foods 11:563–570. https://doi.org/10.1016/j.jff.2014.08.015
Inouye K et al (2008) Effects of thermal treatment on the coagulation of soy proteins induced by subtilisin Carlsberg. J Agric Food Chem 57(2):717–723
Inouye K, Nakano K, Asaoka K, Yasukawa K (2009) Effects of thermal treatment on the coagulation of soy proteins induced by subtilisin carlsberg. J Agric Food Chem 57:717–723. https://doi.org/10.1021/jf802693f
Jeong HJ, Lee JR, Jeong JB, Park JH, Cheong YK, de Lumen BO (2009) The cancer preventive seed peptide lunasin from rye is bioavailable and bioactive. Nutr Cancer 61(5):680–686
Kamali Alamdari E, Ehsani M (2017) Antimicrobial peptides derived from milk: a review. J Food Biosci Technol 7:49–56
Kaspar AA, Reichert JM (2013) Future directions for peptide therapeutics development. Drug Discov Today 18(17–18):807–817
Kaur J, Kumar V, Sharma K, Kaur S, Gat Y, Goyal A, Tanwar B (2019) Opioid peptides: an overview of functional significance. Int J Pept Res Ther 1–9
Kobayashi M (1994) Arenastatin A, a potent cytotoxic depsipeptide from the Okinawan marine sponge Dysidea arenaria. Tetrahedron Lett 35:7969–7972. https://doi.org/10.1016/s0040-4039(00)78398-5
Kohama Y, Oka H, Kayamori Y et al (1991) Potent synthetic analogues of angiotensin-converting enzyme inhibitor derived from tuna muscle. Agric Biol Chem 55:2169–2170. https://doi.org/10.1080/00021369.1991.10870910
Korhonen H, Pihlanto A (2003) Food-derived bioactive peptides-opportunities for designing future foods. Curr Pharm Des 9(16):1297–1308
Korhonen H, Pihlanto A (2006) Bioactive peptides: production and functionality. Int Dairy J 16:945–960. https://doi.org/10.1016/j.idairyj.2005.10.012
Lahart N, O’Callaghan Y, Aherne SA et al (2011) Extent of hydrolysis effects on casein hydrolysate bioactivity: evaluation using the human Jurkat T cell line. Int Dairy J 21:777–782. https://doi.org/10.1016/j.idairyj.2011.03.014
López-Expósito I, Gómez-Ruiz J, Amigo L, Recio I (2006) Identification of antibacterial peptides from ovine αs2-casein. Int Dairy J 16:1072–1080. https://doi.org/10.1016/j.idairyj.2005.10.006
Lovati MR, Manzoni C, Gianazza E et al (2000) Soy protein peptides regulate cholesterol homeostasis in hep G2 cells. J Nutr 130:2543–2549. https://doi.org/10.1093/jn/130.10.2543
Lu R-R, Qian P, Sun Z et al (2010) Hempseed protein derived antioxidative peptides: purification, identification and protection from hydrogen peroxide-induced apoptosis in PC12 cells. Food Chem 123:1210–1218. https://doi.org/10.1016/j.foodchem.2010.05.089
Luna-Vital DA, de Mejía EG, Mendoza S, Loarca-Piña G (2015) Peptides present in the non-digestible fraction of common beans (Phaseolus vulgaris L.) inhibit the angiotensin-I converting enzyme by interacting with its catalytic cavity independent of their antioxidant capacity. Food Funct 6(5):1470–1479
Manso MA, López-Fandiño R (2003) Angiotensin I converting enzyme–inhibitory activity of bovine, ovine, and caprine κ-casein macropeptides and their tryptic hydrolysates. J Food Protect 66:1686–1692. https://doi.org/10.4315/0362-028x-66.9.1686
Maruyama S, Miyoshi S, Kaneko T, Tanaka H (1989) Angiotensin I-converting enzyme inhibitory activities of synthetic peptides related to the tandem repeated sequence of a maize endosperm protein. Agric Biol Chem 53:1077–1081. https://doi.org/10.1080/00021369.1989.10869427
Meisel H (2005) Biochemical properties of peptides encrypted in bovine milk proteins. Curr Med Chem 12:1905–1919. https://doi.org/10.2174/0929867054546618
Meisel H, FitzGerald RJ (2003) Biofunctional peptides from milk proteins: mineral binding and Cytomodulatory effects. Curr Pharm Des. 9:1289–1295. https://doi.org/10.2174/1381612033454847
Moayedi A, Mora L, Aristoy MC et al (2017) ACE-inhibitory and antioxidant activities of peptide fragments obtained from tomato processing by-products fermented using Bacillus subtilis: effect of amino acid composition and peptides molecular mass distribution. Appl Biochem Biotechnol 181(1):48–64
Mojica L, Mejía EGD (2016) Optimization of enzymatic production of anti-diabetic peptides from black bean (Phaseolus vulgaris L.) proteins, their characterization and biological potential. Food Funct 7:713–727. https://doi.org/10.1039/c5fo01204j
Möller NP, Scholz-Ahrens KE, Roos N, Schrezenmei J (2008) Bioactive peptides and proteins from foods: indication for health effects. Eur J Nutr 47(4):171–182
Montoya-Rodríguez A, Mejía EGD, Dia VP et al (2014) Extrusion improved the anti-inflammatory effect of amaranth (Amaranthus hypochondriacus) hydrolysates in LPS-induced human THP-1 macrophage-like and mouse RAW 264.7 macrophages by preventing activation of NF-κB signaling. Mol Nutr Food Res 58:1028–1041. https://doi.org/10.1002/mnfr.201300764
Mora L, Bolumar T, Heres A, Toldrá F (2017) Effect of cooking and simulated gastrointestinal digestion on the activity of generated bioactive peptides in aged beef meat. Food Funct 8:4347–4355. https://doi.org/10.1039/c7fo01148b
Morato A, Carreira R, Junqueira R, Silvestre M (2000) Optimization of casein hydrolysis for obtaining high contents of small peptides: use of subtilisin and trypsin. J Food Compos Anal 13:843–857. https://doi.org/10.1006/jfca.2000.0912
Murakami M, Tonouchi H, Takahashi R et al (2004) Structural analysis of a new anti-hypertensive peptide (β-Lactosin B) isolated from a commercial whey product. J Dairy Sci 87:1967–1974. https://doi.org/10.3168/jds.s0022-0302(04)70013-2
Nakamura Y, Yamamoto N, Sakai K, Takano T (1995) Antihypertensive effect of sour milk and peptides isolated from it that are inhibitors to angiotensin I-converting enzyme. J Dairy Sci 78:1253–1257. https://doi.org/10.3168/jds.s0022-0302(95)76745-5
Naot D, Grey A, Reid IR, Cornish J (2005) Lactoferrin—A novel bone growth factor. Clin Med Res 3:93–101. https://doi.org/10.3121/cmr.3.2.93
Niaz K, Khan F, Abdollahi M (2018) Toxicity of biologically active peptides and future safety aspects: an update. Curr Drug Discov Technol. https://doi.org/10.2174/1570163815666180219112806
Odaka C, Sanders ML, Crews P (2000) Jasplakinolide induces apoptosis in various transformed cell lines by a caspase-3-like protease-dependent pathway. Clin Vaccine Immunol 7:947–952. https://doi.org/10.1128/cdli.7.6.947-952.2000
Olivera B (2000) ω-Conotoxin MVIIA: from marine snail venom to analgesic drug. In: Fusetani N (ed) Drugs from the sea. Karger, Basel, pp 74–85
Palanisamy SK, Giacobbe S, Sundaresan U (2015) Marine ascidians potential source for new class of anti-cancer drugs. World J Pharm Sci 4.8:474–485
Pandey M, Kapila S, Kapila R et al (2018) Evaluation of the osteoprotective potential of whey derived-antioxidative (YVEEL) and angiotensin-converting enzyme inhibitory (YLLF) bioactive peptides in ovariectomised rats. Food Funct 9:4791–4801. https://doi.org/10.1039/c8fo00620b
Park CB, Lee JH, Park IY et al (1997) A novel antimicrobial peptide from the loach, Misgurnus anguillicaudatus. FEBS Lett 411:173–178. https://doi.org/10.1016/s0014-5793(97)00684-4
Phelan M, Aherne-Bruce SA, Osullivan D et al (2009) Potential bioactive effects of casein hydrolysates on human cultured cells. Int Dairy J 19:279–285. https://doi.org/10.1016/j.idairyj.2008.12.004
Pihlanto A, Virtanen T, Korhonen H (2010) Angiotensin I converting enzyme (ACE) inhibitory activity and antihypertensive effect of fermented milk. Int Dairy J 20:3–10. https://doi.org/10.1016/j.idairyj.2009.07.003
Poljsak B, Milisav I (2013) Aging, oxidative stress and antioxidants. In: Morales-González JA (ed) Oxidative stress and chronic degenerative diseases-a role for antioxidants. InTechOpen, London
Puchalska P, Marina ML, García MC (2013) Development of a high-performance liquid chromatography electrospray ionization quadrupole time of flight mass spectrometry methodology for the determination of three highly antihypertensive peptides in maize crops. J Chromatogr 1285:69–77. https://doi.org/10.1016/j.chroma.2013.02.015
Quirós A, Dávalos A, Lasunción MA et al (2008) Bioavailability of the antihypertensive peptide LHLPLP: transepithelial flux of HLPLP. Int Dairy J 18:279–286. https://doi.org/10.1016/j.idairyj.2007.09.006
Rashid MA, Gustafson KR, Boswell JL, Boyd MR (2000) Haligramides A and B, Two new cytotoxic hexapeptides from the marine sponge haliclona nigra. J Nat Prod 63:956–959. https://doi.org/10.1021/np000051
Reddi S, Mada SB, Kumar N et al (2018) Antiosteopenic effect of buffalo milk casein-derived peptide (NAVPITPTL) in ovariectomized rats. Int J Pept Res Ther doi. https://doi.org/10.1007/s10989-018-9763-0
Reynolds EC (2004) U.S. Patent No. 6,780,844. U.S. Patent and Trademark Office, Washington, DC
Ryan JT, Ross RP, Bolton D et al (2011) Bioactive peptides from muscle sources: meat and fish. Nutrients 3(9):765–791. https://doi.org/10.3390/nu3090765
Shai Y (1999) Mechanism of the binding, insertion and destabilization of phospholipid bilayer membranes by α-helical antimicrobial and cell non-selective membrane-lytic peptides. Biomembrane 1462:55–70. https://doi.org/10.1016/s0005-2736(99)00200-x
Sharma S, Singh R, Rana S (2011) Bioactive peptides: a review. Int J Bioautomotion 15(4):223–250
Siow H-L, Gan C-Y (2016) Extraction, identification, and structure–activity relationship of antioxidative and α-amylase inhibitory peptides from cumin seeds (Cuminum cyminum). J Funct Foods 22:1–12. https://doi.org/10.1016/j.jff.2016.01.011
Soares R, Mendonça S, Castro LÍD et al (2015) Major peptides from amaranth (Amaranthus cruentus) protein inhibit HMG-CoA reductase activity. Int J Mol Sci 16:4150–4160. https://doi.org/10.3390/ijms16024150
Tang W, Zhang H, Wang L et al (2015) Targeted separation of antibacterial peptide from protein hydrolysate of anchovy cooking wastewater by equilibrium dialysis. Food Chem 168:115–123. https://doi.org/10.1016/j.foodchem.2014.07.027
Toba Y, Takada Y, Yamamura J et al (2000) Milk basic protein: a novel protective function of milk against osteoporosis. Bone 27:403–408. https://doi.org/10.1016/s8756-3282(00)00332-x
Toldrá F, Reig M, Aristoy M-C, Mora L (2018) Generation of bioactive peptides during food processing. Food Chem 267:395–404. https://doi.org/10.1016/j.foodchem.2017.06.119
Udenigwe CC, Aluko RE (2011) Food protein-derived bioactive peptides: production, processing, and potential health benefits. J Food Sci. https://doi.org/10.1111/j.1750-3841.2011.02455.x
Unal G, Akalın AS (2012) Antioxidant and angiotensin-converting enzyme inhibitory activity of yoghurt fortified with sodium calcium caseinate or whey protein concentrate. Dairy Sci Technol 92:627–639. https://doi.org/10.1007/s13594-012-0082-5
Velliyagounder K, Alsaedi W, Alabdulmohsen W et al (2014) Oral lactoferrin protects against experimental candidiasis in mice. J Appl Microbiol 118:212–221. https://doi.org/10.1111/jam.12666
Wakabayashi H, Takase M, Tomita M (2003) Lactoferricin derived from milk protein lactoferrin. Curr Pharm Des 9(16):1277–1287
Wang Z, Zhang X (2016) Isolation and identification of anti-proliferative peptides from Spirulina platensis using three-step hydrolysis. J Sci Food Agric 97:918–922. https://doi.org/10.1002/jsfa.7815
Wang J, Hu J, Cui J, Bai X, Du Y, Miyaguchi Y, Lin B (2008) Purification and identification of a ACE inhibitory peptide from oyster proteins hydrolysate and the antihypertensive effect of hydrolysate in spontaneously hypertensive rats. Food Chem 111(2):302–308
Wang X, Qiu N, Liu Y (2018) Effect of different heat treatments on in vitro digestion of egg white proteins and identification of bioactive peptides in digested products. J Food Sci 83:1140–1148. https://doi.org/10.1111/1750-3841.14107
Wattanasiritham L, Theerakulkait C, Wickramasekara S et al (2016) Isolation and identification of antioxidant peptides from enzymatically hydrolyzed rice bran protein. Food Chem 192:156–162. https://doi.org/10.1016/j.foodchem.2015.06.057
Wei Y, Gao L, Wang L, Shi L, Wei E, Zhou B, Zhou L, Ge B (2017) Polydopamine and peptide decorated doxorubicin-loaded mesoporous silica nanoparticles as a targeted drug delivery system for bladder cancer therapy. Drug Deliv 24(1):681–691
Wesson KJ, Hamann MT, Keenamide A (1996) A bioactive cyclic peptide from the marine mollusc Pleurobranchus forskalii. J Nat Prod 59:629–663
Yang L, Kumagai T, Kawamura H et al (2007) Effects of rice proteins from two cultivars, Koshihikari and Shunyo, on cholesterol and triglyceride metabolism in growing and adult rats. Biosci Biotechnol Biochem 71(3):694–703
Yano S, Suzuki K, Funatsu G (1996) Isolation from α-zein of thermolysin peptides with angiotensin i-converting enzyme inhibitory activity. Biosci Biotechnol Biochem 60:661–663. https://doi.org/10.1271/bbb.60.661
Yousr M, Howell N (2015) Antioxidant and ACE inhibitory bioactive peptides purified from egg yolk proteins. Int J Mol Sci 16:29161–29178. https://doi.org/10.3390/ijms161226155
Zampella A (2008) Homophymine A, an anti-HIV cyclodepsipeptide from the sponge Homophymia sp. J Org Chem 73:14: 5319–5327
Zhang B, Liu G, Ying D et al (2017) Effect of extrusion conditions on the physico-chemical properties and in vitro protein digestibility of canola meal. Food Res Int 100:658–664
Zhang HJ, Zhang H, Wang L, Guo XN (2012) Preparation and functional properties of rice bran proteins from heat-stabilized defatted rice bran. Food Res Int 47(2):359–363
Zhou H, Wang CZ, Ye JZ et al (2016) Effects of high hydrostatic pressure treatment on structural, allergenicity and functional properties of proteins from ginkgo seeds. Innov Food Sci Emerg Technol 34:187–195
Zhuang H, Tang N, Yuan Y (2013) Purification and identification of antioxidant peptides from corn gluten meal. J Funct Foods 5:1810–1821. https://doi.org/10.1016/j.jff.2013.08.013
Author information
Authors and Affiliations
Corresponding author
Ethics declarations
Conflict of interest
Authors declare no any conflict of interest.
Additional information
Publisher’s Note
Springer Nature remains neutral with regard to jurisdictional claims in published maps and institutional affiliations.
Rights and permissions
About this article
Cite this article
Bhandari, D., Rafiq, S., Gat, Y. et al. A Review on Bioactive Peptides: Physiological Functions, Bioavailability and Safety. Int J Pept Res Ther 26, 139–150 (2020). https://doi.org/10.1007/s10989-019-09823-5
Accepted:
Published:
Issue Date:
DOI: https://doi.org/10.1007/s10989-019-09823-5