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Production of goat milk protein hydrolysate enriched in ACE-inhibitory peptides by ultrafiltration

Published online by Cambridge University Press:  08 July 2014

Francisco Javier Espejo-Carpio ,
Raúl Pérez-Gálvez ,
María del Carmen Almécija ,
Antonio Guadix  and
Emilia M. Guadix
Francisco Javier Espejo-Carpio*
Affiliation:
Department of Chemical Engineering, University of Granada, 18071 Granada, Spain
Raúl Pérez-Gálvez
Affiliation:
Department of Chemical Engineering, University of Granada, 18071 Granada, Spain
María del Carmen Almécija
Affiliation:
Department of Chemical Engineering, University of Granada, 18071 Granada, Spain
Antonio Guadix
Affiliation:
Department of Chemical Engineering, University of Granada, 18071 Granada, Spain
Emilia M. Guadix
Affiliation:
Department of Chemical Engineering, University of Granada, 18071 Granada, Spain
*
*For correspondence; e-mail: [email protected]
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Abstract

A global process for the production of goat milk hydrolysates enriched in angiotensin converting enzyme (ACE) inhibitory peptides was proposed. Firstly, the protein fractions (caseins and whey proteins) were separated by ultrafiltration through a 0·14 μm ceramic membrane. The casein fraction obtained in the retentate stream of the above filtration step was subsequently hydrolysed with a combination of subtilisin and trypsin. After 3 h of reaction, the hydrolysate produced presented an IC50 of 218·50 μg/ml, which represent a relatively high ACE inhibitory activity. Finally, this hydrolysate was filtered through a 50 kDa ceramic membrane until reaching a volume reduction factor of 3. The permeate produced presented an improvement of more than 30% in the ACE inhibitory activity. In contrast, the retentate was concentrated in larger and inactive peptides which led to a decrease of more than 80% in its inhibitory activity. The process suggested in this work was suitable to obtain a potent ACE inhibitory activity product able to be incorporated into food formulas intended to control or lower blood pressure. Moreover, the liquid product could be easily stabilised by spray dried if it would be necessary.

Keywords

Goat milk proteinenzymatic hydrolysisACE-inhibitory activitymembrane ultrafiltrationpeptide identification
Type
Research Article
Information
Journal of Dairy Research , Volume 81 , Issue 4 , November 2014 , pp. 385 - 393
Copyright
Copyright © Proprietors of Journal of Dairy Research 2014 

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References

Adler-Nissen, J 1986 Enzymic Hydrolysis of Food Proteins (1st ed.). London: Elsevier Applied Science Publishers Google Scholar
Aluko, RE 2007 Technology for the production and utilization of food protein-derived anti-hypertensive peptides: a review. Recent Patents on Biotechnology 1 260–267 Google Scholar
Barlett, M, Bird, MR & Howell, JA 1995 An experimental study for the development of a qualitative membrane cleaning model. Journal of Membrane Science 105 147–157 Google Scholar
Cheryan, M 1998 Ultrafiltration and Microfiltration Handbook, pp. 65–69. Lancaster: Technomic Publishing Company Google Scholar
Espejo-Carpio, FJ, De Gobba, C, Guadix, A, Guadix, EM & Otte, J 2013a Angiotensin I-converting enzyme inhibitory activity of enzymatic hydrolysates of goat milk protein fractions. International Dairy Journal 32 175–183 CrossRefGoogle Scholar
Espejo-Carpio, FJ, Pérez-Gálvez, R, Guadix, EM & Guadix, A 2013b Optimisation of the hydrolysis of goat milk protein for the production of ACE-inhibitory peptides. Journal of Dairy Research 80 214–222 CrossRefGoogle ScholarPubMed
Field, RW, Wu, D, Howell, JA & Gupta, BB 1995 Critical flux concept for microfiltration fouling. Journal of Membrane Science 100 259–272 CrossRefGoogle Scholar
FitzGerald, RJ, Murray, BA & Walsh, DJ 2004 Hypotensive peptides from milk proteins. Journal of Nutrition 134 980S–988S CrossRefGoogle ScholarPubMed
Foltz, M, Cerstiaens, A, van Meensel, A, Mols, R, van der Pijl, PC, Duchateau, GS & Augustijns, P 2008. The angiotensin converting enzyme inhibitory tripeptides Ile-Pro-Pro and Val-Pro-Pro show increasing permeabilities with increasing physiological relevance of absorption models. Peptides 29 1312–1320 Google Scholar
García-Moreno, PJ, Pérez-Gálvez, R, Espejo-Carpio, FJ, Muñío, MM, Guadix, A & Guadix, EM 2013 Lipid characterization and properties of protein hydrolysates obtained from discarded Mediterranean fish species. Journal of the Science of Food and Agriculture 93 3777–3784 CrossRefGoogle ScholarPubMed
Geerlings, A, Villar, IC, Hidalgo-Zarco, F, Sánchez, M, Vera, R, Zafra-Gómez, A, Boza, J & Duarte, J 2006 Identification and characterization of novel angiotensin-converting enzyme inhibitors obtained from goat milk. Journal of Dairy Science 89 3326–3335 Google Scholar
Holder, A, Weik, J & Hinrichs, J 2013 A study of fouling during long-term fractionation of functional peptides by means of cross-flow ultrafiltration and cross-flow electro membrane filtration. Journal of Membrane Science 446 440–448 CrossRefGoogle Scholar
Ishida, Y, Shibata, Y, Fukuhara, I, Yano, Y, Takehara, I & Kaneko, K 2011 Effect of an excess intake of casein hydrolysate containing Val-Pro-Pro and Ile-Pro-Pro in subjects with normal blood pressure, high-normal blood pressure, or mild hypertension. Bioscience, Biotechnology, and Biochemistry 75 427–433 Google Scholar
Jiang, J, Chen, S, Ren, F, Luo, Z & Zeng, SS 2007 Yak milk casein as a functional ingredient: preparation and identification of angiotensin-I-converting enzyme inhibitory peptides. Journal of Dairy Research 74 18–25 CrossRefGoogle ScholarPubMed
Jiang, Z, Tian, B, Brodcrob, A & Huo, G 2010 Production, analysis and in vivo evaluation of novel angiotensin-I-converting enzyme inhibitory peptides from bovine casein. Food Chemistry 123 779–786 Google Scholar
Kumar, S, Tandon, HKL & Kapila, S 2011 Antihypertensive and immunomodulatory property of enzyme hydrolysates derived from goat casein. Milchwissenschaft 66 40–42 Google Scholar
Laemmli, UK 1970 Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227 680–685 Google Scholar
Li, GH, Le, GW, Shi, YH & Shresthaa, S 2004 Angiotensin I– converting enzyme inhibitory peptides derived from food proteins and their physiological and pharmacological effects. Nutrition Research 24 469–486 Google Scholar
Lin, F, Chen, L, Liang, R, Zhang, Z, Wang, J, Cai, M & Li, Y 2011 Pilot-scale production of low molecular weight peptides from corn wet milling byproducts and the antihypertensive effects in vivo and in vitro. Food Chemistry 124 801–807 CrossRefGoogle Scholar
López-Fandiño, R, Otte, J & van Camp, J 2006 Physiological, chemical and technological aspects of milk-protein-derived peptides with antihypertensive and ACE-inhibitory activity. International Dairy Journal 16 1277–1293 CrossRefGoogle Scholar
Mota, MVT, Ferreira, IMPLVO, Oliveira, MBP, Rocha, C, Teixeira, JA, Torres, D & Gonçalves, MP 2006 Trypsin hydrolysis of whey protein concentrates: characterization using multivariate data analysis. Food Chemistry 94 278–286 Google Scholar
Otte, J, Shalaby, SM, Zakora, M, Pripp, AH & El-Shabrawy, SA 2007 Angiotensin-converting enzyme inhibitory activity of milk protein hydrolysates: effect of substrate, enzyme and time of hydrolysis. International Dairy Journal 17 488–503 CrossRefGoogle Scholar
Pan, D, Cao, J, Guo, H & Zhao, B 2012 Studies on purification and the molecular mechanism of a novel ACE inhibitory peptide from whey protein hydrolysate. Food Chemistry 130 121–126 Google Scholar
Pihlanto-Leppälä, A, Koskinen, P, Piilola, K, Tupasela, T & Korhonen, H 2000 Angiotensin I-converting enzyme inhibitory properties of whey protein digests: concentration and characterization of active peptides. Journal of Dairy Research 67 53–64 Google Scholar
Pintado, ME & Malcata, FX 2000 Hydrolysis of ovine, caprine and bovine whey proteins by trypsin and pepsin. Bioprocess Engineering 23 275–282 CrossRefGoogle Scholar
Riordan, J 2003 Angiotensin-I-converting enzyme and its relatives. Genome Biology 4 225 Google Scholar
Roberts, PR, Burney, JD, Black, KW & Zaloga, GP 1999 Effect of chain length on absorption of biologically active peptides from the gastrointestinal tract. Digestion 60 332–337 Google Scholar
Rui, X, Boye, JI, Simpson, BK & Prasher, SO 2013 Purification and characterization of angiotensin I-converting enzyme inhibitory peptides of small red bean (Phaseolus vulgaris) hydrolysates. Journal of Functional Foods 5 1116–1124 CrossRefGoogle Scholar
Ryan, JT, Ross, RP, Bolton, D, Fitzgerald, GF & Stanton, C 2011 Bioactive peptides from muscle sources: meat and fish. Nutrients 3 765–791 CrossRefGoogle ScholarPubMed
Shalaby, SM, Zakora, M & Otte, J 2006 Performance of two commonly used angiotensin-converting enzyme inhibition assays using FA-PGG and HHL as substrates. Journal of Dairy Research 73 178–186 Google Scholar
Wang, L, Mao, X, Cheng, X, Xiong, X & Ren, F 2010 Effect of enzyme type and hydrolysis conditions on the in vitro angiotensin I-converting enzyme inhibitory activity and ash content of hydrolysed whey protein isolate. International Journal of Food Science and Technology 45 807–812 Google Scholar