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Utilisation of chickpea protein isolates forproduction of peptides with angiotensinI-converting enzyme (ACE)-inhibitory activityJusto Pedroche, Mara M Yust, Julio Giron-Calle, Manuel Alaiz, Francisco Millan

and Javier VioqueInstituto de la Grasa, Padre Garcia Tejero 4, E-41012 Sevilla, Spain

INTRODUCTION

(Received 27 September 2001; revised version received 10 January 2002; accepted 13 February 2002

Correspondence to: Javier Vioque, Instituto de la Grasa, Padre Garcia Tejero 4, E-41012 Sevilla, SpainE-mail: jvioque@cica.es

Contract/grant sponsor: CICYT; contract/grant number: ALG 2001-0526

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MATERIALS AND METHODS

Materials

Proteolytic enzymes

Preparation of angiotensin-converting enzyme

Assay of angiotensin-converting enzyme

Preparation of protein isolate

Figure 1.Kinetics of hydrolysis of substrate HHL (S) by ACE (E) in

presence or absence of captopril (C).

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Hydrolysis

Degree of hydrolysis

Fast protein liquid chromatography (FPLC)

Biogel P2 chromatography

HPLC C18chromatography

RESULTS AND DISCUSSION

Generation of extensive chickpea protein

hydrolysates

ACE-inhibitory activity of chickpea protein

hydrolysates

Figure 2.Enzymatic hydrolysis of chickpea protein isolate with alcalase

and flavourzyme (added at 60min) and percentage inhibition of ACE by

resulting hydrolysates.

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CONCLUSIONS

ACKNOWLEDGEMENT

REFERENCES

Table 1. ACE-inhibitory activity of fractions obtained by Biogel P2 gel

filtration chromatography of 30min alcalase chickpea protein hydrolysate

Figure 6. HPLC C18 profile of chickpea peptides obtained from Biogel P2

gel filtration chromatography.

Table 2. ACE-inhibitory activity of fractions obtained by HPLC C 18chroma-

tography of chickpea peptides

Table 3. Inhibitory characteristics of peptides obtained by

HPLC C18chromatography of chickpea peptides

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