Abstract
Six different proteases (Flavourzyme®, Neutrase®, Protamex®, Alcalase® 2.4L, Proleather® FG-F, and papain) were employed to hydrolyze apricot kernel protein (AKP). Alcalase® is an inexpensive and non-specific protease that has been shown to be useful for the generation of bioactive peptides from AKP. Alcalase® 2.4L was selected for further study on enzymatic preparation of ACE inhibitory peptide from AKP. After 60-min hydrolysis, the highest ACE inhibition was 82 ± 0.14%. Results of molecular weight distribution revealed that most of ACE inhibition activity was probably attributed to low-molecular weight peptide fraction ranging from 200 to 900 Da. Ultrafiltration on membranes with several molecular weight cutoffs (MWCFs) demonstrated that most of the ACE inhibitory activity was due to peptides with a less than 1,000 Da molecular weight: the IC50 value of the 1-kDa ultrafiltrate was 0.15 ± 0.007 mg mL−1, while it was 0.378 ± 0.015 mg mL−1 before ultrafiltration. Additionally, further separation and purification of the ACE inhibitory peptides were carried out using gel filtration and C18 RP-HPLC. The result of research can be used to optimize AKP enzymatic hydrolysis for producing ACE inhibitory peptides which could be used for food industry and nutraceuticals.
![](http://media.springernature.com/m312/springer-static/image/art%3A10.1007%2Fs00217-010-1235-5/MediaObjects/217_2010_1235_Fig1_HTML.gif)
![](http://media.springernature.com/m312/springer-static/image/art%3A10.1007%2Fs00217-010-1235-5/MediaObjects/217_2010_1235_Fig2_HTML.gif)
![](http://media.springernature.com/m312/springer-static/image/art%3A10.1007%2Fs00217-010-1235-5/MediaObjects/217_2010_1235_Fig3_HTML.gif)
![](http://media.springernature.com/m312/springer-static/image/art%3A10.1007%2Fs00217-010-1235-5/MediaObjects/217_2010_1235_Fig4_HTML.gif)
![](http://media.springernature.com/m312/springer-static/image/art%3A10.1007%2Fs00217-010-1235-5/MediaObjects/217_2010_1235_Fig5_HTML.gif)
Similar content being viewed by others
References
Abd El-Aal MH, Khalil MKM, Rahma EH (1986) Food Chem 19:287–298
Durmaz G, Alpaslan M (2007) Food Chem 100:1177–1181
Femenia A, Rossello C, Mulet A, Canellas J (1995) J Agric Food Chem 43:356–361
El-Adawy TA, Rahma EH, El-Badawey AA, Gomaa MA, Lásztity R, Sarkadi L (1994) Nahrung 38:12–20
World Health Organization (2003) Geneva, WHO
Murray BA, FitzGerald RJ (2007) Curr Pharm Des 13:773–791
Cushman DW, Ondetti MA (1999) Nature Med 5:1110
Vercruysse L, Van Camp J, Smagghe G (2005) J Agric Food Chem 53:8106–8115
Jang A, Lee M (2005) Meat Sci 69:653–661
Je J-Y, Park J-Y, Jung W-K, Park P-J, Kim S-K (2005) Food Chem 90:809–814
Yu YK, Hu JN, Miyaguchi Y, Bai XF, Du YG, Lin BC (2006) Peptides 27:2950–2956
Quirós A, Chichón R, Recio I, López-Fandiño R (2007) Food Chem 104:1734–1739
Chen GW, Tsai JS, Sun Pan B (2007) Int Dairy J 17:641–647
Wu JP, Ding XL (2002) Food Res Int 35:367–375
Chiang WD, Tsou MJ, Tsai ZY, Tsai TC (2006) Food Chem 98:725–732
Wu JP, Aluko RE, Muir AD (2008) Food Chem 111:942–950
Sheih IC, Fang TJ, Wu TK (2009) Food Chem 115:279–284
Sato M, Hosokawa T, Yamaguchi T, Nakano T, Muramoto K, Kahara T, Funayama K, Kobayashi A, Nakano T (2002) J Agric Food Chem 50:6245–6252
Li GH, Wan JZ, Le GW, Shi YH (2006) J Pept Sci 12:509–514
Adler-Nissen J (1986) Enzymatic hydrolysis of food proteins. Elsevier Applied Science Publishers, London, pp 116–124
Wu JP, Aluko RE, Muir AD (2002) J Chromatogr A 950:125–130
Bradford MM (1976) Anal Biochem 72:248–254
He HL, Chen XL, Wu H, Sun CY, Zhang YZ, Zhou BC (2007) Bioresour Technol 98:3499–3505
Yust MM, Pedroche J, Giron-Calle J, Alaiz M, Millan F, Vioque J (2003) Food Chem 81:363–369
Pedroche J, Yust MM, Giron-Calle J, Alaiz M, Millan F, Vioque J (2002) J Sci Food Agric 82:960–965
Byun H-G, Kim S-K (2001) Process Biochem 36:1155–1162
Li GH, Le GW, Shi YH, Shrestha S (2004) Nutr Res 24:469–486
Korhonen H, Pihlanto A (2006) Int Dairy J 16:945–960
Kapel R, Chabeau A, Lesage J, Riviere G, Ravallec-Ple R, Lecouturier D, Wartelle M, Guillochon D, Dhulster P (2006) Food Chem 98:120–126
Wu JP, Aluko RE, Nakai S (2006) J Agric Food Chem 54:732–738
Megias C, Yust MM, Pedroche J, Lquari H, Giron-Calle J, Alaiz M, Millan F, Vioque J (2004) J Agric Food Chem 52:1928–1932
Acknowledgments
This work has received financial support from project 2009JM 3021 (Shaanxi Province Basic Science Research). The authors express their appreciation to Professor Dai Jun (Jiangnan University) to determine peptides molecular weight distribution.
Author information
Authors and Affiliations
Corresponding author
Rights and permissions
About this article
Cite this article
Zhu, Z., Qiu, N. & Yi, J. Production and characterization of angiotensin converting enzyme (ACE) inhibitory peptides from apricot (Prunus armeniaca L.) kernel protein hydrolysate. Eur Food Res Technol 231, 13–19 (2010). https://doi.org/10.1007/s00217-010-1235-5
Received:
Revised:
Accepted:
Published:
Issue Date:
DOI: https://doi.org/10.1007/s00217-010-1235-5