Skip to main content

Preparation of Functional Peanut Oligopeptide and Its Biological Activity

  • Chapter
  • First Online:

Abstract

Biopeptides are peptidic compounds that are beneficial or biologically active to the life activities of living organisms (Liu and Cao 2002; Pang Guangchang et al. 2001). Since Brantl (1979) first reported that small peptide with morphine-like activity was found from the small intestine of guinea pig fed with bovine casein zymolyte, a variety of bioactive peptides have been isolated from the animals, plants, and microorganisms (Gill et al. 1996). Among them, peptides that are composed of two to more than ten amino acids with biological activity are known as functional oligopeptides. Functional oligopeptides belong to biologically active peptides. Modern nutrition studies have found that proteins are not completely absorbed in the form of free amino acids after the action of digestive tract enzymes but are absorbed mainly in the form of oligopeptides; the biological meaning of functional oligopeptides is mainly reflected in both a variety of functional activity and completely independent absorption mechanism.

This is a preview of subscription content, log in via an institution.

Buying options

Chapter
USD   29.95
Price excludes VAT (USA)
  • Available as PDF
  • Read on any device
  • Instant download
  • Own it forever
eBook
USD   169.00
Price excludes VAT (USA)
  • Available as EPUB and PDF
  • Read on any device
  • Instant download
  • Own it forever
Softcover Book
USD   219.99
Price excludes VAT (USA)
  • Compact, lightweight edition
  • Dispatched in 3 to 5 business days
  • Free shipping worldwide - see info
Hardcover Book
USD   219.99
Price excludes VAT (USA)
  • Durable hardcover edition
  • Dispatched in 3 to 5 business days
  • Free shipping worldwide - see info

Tax calculation will be finalised at checkout

Purchases are for personal use only

Learn about institutional subscriptions

References

  • Brantl V, Teschemacher H, Henschen A, et al. Novel opioid peptides derived from casein (beta-casomorphins). I. Isolation from bovine casein peptone[J]. Hoppe Seyler’s Z Physiol Chem. 1979;360(9):1211.

    Google Scholar 

  • Byun HG, Kim SK. Purification and characterization of angiotensin I converting enzyme (ACE) inhibitory peptides from Alaska Pollack (Theragra chalcogramma) skin[J]. Process Biochem. 2001;36(12):1155–1162.

    Google Scholar 

  • Chen Meizhen, Yu Jie, Guo Huimin. Study on the scavenging activity on hydroxyl radical of enzymic hydrolysates of soy protein isolates [J]. Food Sci. 2002;23(1):43–6.

    Google Scholar 

  • Chen Xiu, Chen Weizhou, Zeng Guiyun. Cardiovascular pharmacology. 3rd Edition[M] ed. People’s Health Publishing House: Beijing; 2003. p. 352–3.

    Google Scholar 

  • Chen HM, Muramoto K, Yamauchi F. Structural analysis of antioxidative peptides from soybean. β-conglycinin [J]. J Agric Food Chem. 1995;43(3):574–8.

    Google Scholar 

  • Cheung HS, Wang FL, Ondetti MA, et al. Binding of peptide substrates and inhibitors of angiotensin-converting enzyme. Importance of the COOH-terminal dipeptide sequence [J]. J Biol Chem. 1980;255:401–7.

    Google Scholar 

  • Coakley WT, James CJ. A simple linear transform for the Folin-Lowry protein calibration curve to 1.0 mg/ml. Anal Biochem. 1978;85(1):90–7.

    Article  CAS  Google Scholar 

  • Cushman DW, Cheung HS, Sabo EF, Ondetti MA. Design of potent competitive inhibitors of angiotensin-converting enzyme. Carboxyalkanoyl and mercaptoalkanoyl amino acids. Biochemistry. 2002;16(25):5484–91.

    Google Scholar 

  • Deng JC. Effect of temperatures on fish alkaline protease, protein Interaction and texture quality. J Food Sci. 1981;46(1):62–5.

    Article  CAS  Google Scholar 

  • Douglas RG, Sturrock ED. Structure-based design of domain-selective angiotensin-converting enzyme inhibitors. Drug Discovery Afr. 2012:355–77.

    Google Scholar 

  • Dun XP, Chen ZW. Enzyme hydrolysis preparation of rice small polypeptides from rice residue [J]. Food Sci. 2004;25(6):113–6.

    Google Scholar 

  • Enyonam Quist E, Dixon Phillips R, Saalia FK. Angiotensin converting enzyme inhibitory activity of proteolytic digests of peanut (Arachis hypogaea L.) flour. LWT Food Sci Technol. 2009;42(3):694–9.

    Article  Google Scholar 

  • Gill I, López-Fandiño R, Jorba X, et al. Biologically active peptides and enzymatic approaches to their production[J]. Enzym Microb Technol. 1996;18(3):163.

    Google Scholar 

  • Grimble GK, Silk DBA. Intravenous protein hydrolysates-Time to turn the clock back[J]. Clin Nutr. 1990;9(1):39–45.

    Google Scholar 

  • Guang C, Phillips RD. Purification, activity and sequence of angiotensin I converting enzyme inhibitory peptide from Alcalase hydrolysate of peanut flour[J]. J Agric Food Chem. 2009;57(21):10102–6.

    Google Scholar 

  • Guanhong L. Studies on angiotensin-converting enzyme inhibitory peptides derived from food proteins [D]. Wuxi: Jiangnan University; 2005.

    Google Scholar 

  • Guangchang P et al. Theoretical basis and prospect of research progress of bioactive peptides[J]. Food Sci. 2001;22(2):80–4.

    Google Scholar 

  • Guo H. Preparation of wheat germ protein and its antioxidant function[D]. Wuxi: Jiangnan University; 2009.

    Google Scholar 

  • Guo HQ, Mao H, Zhao B, et al. Molecular mechanism study of targeting of two angiotensin-converting enzyme inhibitory peptides[J]. Food Sci. 2010;31(23):1–5.

    Google Scholar 

  • Jamdar SN, Rajalakshmi V, Pednekar MD, Juan F, Yardi V, Sharma A. Influence of degree of hydrolysis on functional properties, antioxidant activity and ACE inhibitory activity of peanut protein hydrolysate. Food Chem. 2010;121(1):178–84.

    Article  CAS  Google Scholar 

  • Jianping Wu, Xiaolin Ding. Characterization of inhibition and stability of soy-protein-derived angiotensin I-converting enzyme inhibitory peptides. Food Res Int. 2002;35(4):367–75.

    Article  Google Scholar 

  • Jung WK, Mendis E, Je JY, et al. Angiotensin I-converting enzyme inhibitory peptide from yellowfin sole (Limanda aspera) frame protein and its antihypertensive effect in spontaneously hypertensive rats [J]. Food Chem. 2006;94(1):26–32.

    Google Scholar 

  • Kannel WB. Blood pressure as a cardiovascular risk factor: prevention and treatment. JAMA: J Am Med Assoc. 1996;275(20):1571–6.

    Article  CAS  Google Scholar 

  • Liao Dan-kui, Sun Xiu-hua, Wan Shun-gang, Yang Ke-di, Tong Zhang-fa, Liu Xiong-min. Enzymatic Hydrolysis and Screening of Prodrugtype Angiotensin I-converting Enzyme Inhibitor from Chicken Egg Yolk [J]. Fine Chem. 2006;8:757–9.

    Google Scholar 

  • Liu Lisheng. Hypertension[M]. Beijing: People’s Health Publishing House; 2001. p. 30–4.

    Google Scholar 

  • Liu YD, Cao YP. Prospect review on polypeptide [J]. Food Sci. 2002;23(8):319–20.

    Google Scholar 

  • Marquez MC, Fernandez V. Enzymic hydrolysis of vegetable proteins: mechanism and kinetics [J]. Process Biochem. 1993;28:481–90.

    Article  Google Scholar 

  • Mo Qi. A Study on the Papain Hydrolysis of Peanut Meal [J]. Cereal Feed Ind. 1996;12:37–8.

    Google Scholar 

  • Matsui T, Li C, Osajima Y. Preparation and characterization of novel bioactive peptides responsible for angiotensin I – converting enzyme inhibition from wheat germ [J]. J Peptide Sci. 1999;5(7):289–97.

    Google Scholar 

  • Munilla-moran R, Saborido-rey F. Digestive enzymes in marine species. 1: Protease activities ingut from redfish (Sebastes mentella), seabream (Sparusaarata) and turbot (Scophthalmus inaximus) [J]. Comp Biochem Physiol B: Biochem Mol Biol. 1996;113(2):395–402.

    Article  Google Scholar 

  • Nakagomi K, Fujimura A, Ebisu H, et al. Acein-1, a novel angiotensin-I-converting enzyme inhibitory peptide isolated from tryptic hydrolysate of human plasma[J]. FEBS Lett. 1998;438(3):255–7.

    Google Scholar 

  • Ondetti MA, Cushman DW. Design of specific inhibitors of angiotensin-converting enzyme: new class of orally active antihypertensive agents [J]. Science. 1977;196(4288):441–4.

    Article  CAS  Google Scholar 

  • Patchett AA, Harris E, Tristram EW, et al. A new class of angiotensin-converting enzyme inhibitors [J]. Nature. 1980;298:280–3.

    Google Scholar 

  • Shen Beiying. Study on Antioxidant Peptides of Soybean Protein [J]. Chinese fats oils. 1996; 21(6):21–4.

    Google Scholar 

  • Stevens RL, Micalizzi ER, Fessler DC, Pals DT. Angiotensin I converting enzyme of calf lung. Method of assay and partial purification. Biochemistry. 2002;11(16):2999–3007.

    Article  Google Scholar 

  • Rohrbach MS, Williams JEB, Rolstad RA, et al. Purification and substrate specificity of bovine angiotensin-converting enzyme [J]. J Biol Chem. 1981;256:225–30.

    CAS  Google Scholar 

  • Ruiz JÁG, Ramos M, Recio I. Angiotensin converting enzyme-inhibitory activity of peptides isolated from Manchego cheese. Stability under simulated gastrointestinal digestion[J]. Int Dairy J. 2004;14(12):1075–80.

    Google Scholar 

  • Saito Y, Wanezaki K, Kawato A, et al. Structure and activity of angiotensin I converting enzyme inhibitory peptides from sake and sake lees [J]. Biosci Biotechnol Biochem. 1994;58(10):1767–71.

    Google Scholar 

  • Sheng GH. Function and application of soybean peptide [J]. Food Sci Technol. 1993;6:21–6.

    Google Scholar 

  • Tello PG. Enzymatic hydrolysis of whey protein: I kinetic models [J]. Biotechnol Bioeng. 1994;44:523–8.

    Article  Google Scholar 

  • Vermeirssen V, Deplancke B, Tappenden KA, Van Camp J, Gaskins HR, Verstraete W. Intestinal transport of the lactokinin Ala-Leu-Pro-Met-His-Ile-Arg through a Caco-2 Bbe monolayer. J Pept Sci. 2002;8(3):95–100.

    Article  CAS  Google Scholar 

  • Wang Jiazheng. Protein technical handbook[M]. Beijing: Science Press; 2002.

    Google Scholar 

  • Wang M, Gu WY. On preparation of enzyme-modified peptides from maize gluten meal [J]. Sci Technol Cereal Oils Foods. 1999;1–3.

    Google Scholar 

  • Wang H, Ng TB. Pleureryn, a novel protease from fresh fruiting bodies of the edible mushroom Pleurotus eryngii. Biochem Biophys Res Commun. 2001;289(3):750–5.

    Article  CAS  Google Scholar 

  • Wang Q, Wang CY, Hu H, et al. Structural characterization and structure-activity relationship of ACE inhibitory peptides from peanut [J]. Food Sci. 2013.

    Google Scholar 

  • Wu JP, Ding XL. Characterization of inhibition and stability of soy-protein-derived angiotensin I-converting enzyme inhibitory peptides[J]. Food Res Int. 2002;35:367–75.

    Google Scholar 

  • Yamamoto D, Takai S, Miyazaki M. Prediction of interaction mode between a typical ACE inhibitor and MMP-9 active site. Biochem Biophys Res Commun. 2007;354(4):981–4.

    Article  CAS  Google Scholar 

  • Yude L, Yanping C. Development of biological protein peptide[J]. Food Sci. 2002;23(8):319–20.

    Google Scholar 

  • Zhang XH. Preparation of soy peptide and study on the separation of purified grade [D]. Guangzhou: South China University of Technology; 2002.

    Google Scholar 

  • Zhang YH. Study on preparation of peanut oligopeptides and its functional activities [D]. Beijing: Chinese Academy of Agricultural Sciences; 2007.

    Google Scholar 

  • Zhang XS, Feng JC. Study on protease production of functional protein short peptides [J]. Anim Sci Vet Med. 2004;21(3):48–51.

    Google Scholar 

  • Zhang YH, Wang Q. Peanut protein hydrolyzing by Alcalase to prepare peanut oligopeptides [J]. Trans CSAE. 2007;23(4):258–63.

    Google Scholar 

Download references

Author information

Authors and Affiliations

Authors

Rights and permissions

Reprints and permissions

Copyright information

© 2018 Springer Nature Singapore Pte Ltd.

About this chapter

Check for updates. Verify currency and authenticity via CrossMark

Cite this chapter

Wang, Q. (2018). Preparation of Functional Peanut Oligopeptide and Its Biological Activity. In: Peanut Processing Characteristics and Quality Evaluation. Springer, Singapore. https://doi.org/10.1007/978-981-10-6175-2_9

Download citation

Publish with us

Policies and ethics