Abstract

Inhibition of Angiotensin Converting Enzyme (ACE) reduces blood pressure and gives an anti-hypertensive effect. Chicken skin is an undesirable by-product of the poultry industry, disliked by consumer because of the high fat content. The aim of this research is to determine the effect of molecular weight reduction on ACE inhibition activity in chicken skin hydrolysate. Chicken skin is prepared by manually defatting, soaked in acetone and in 0.1M phosphate buffer. Sample hydrolysis is carried out using alcalase enzyme for a duration of 4 hours at 60˚C and pH 9.5. The best degree of hydrolysis (DH), at 4th hour, with value of 49.54 ± 0.79 %, is ultrafiltrated and used in ACE inhibition activity detection. The sample weight ≥ 10 kDa , 3 – 10 kDa and ≤ 3 kDa contains 5.63 ± 0.01 g/L, 2.84 ± 0.06 g/L and 1.07 ± 0.18 g/L peptide content respectively whereas soluble protein content is 0.51 mg/mL for sample weight ≥ 10 kDa, 0.27 mg/mL for sample weight 3 – 10 kDa and 0.23 mg/mL for sample weight ≤ 3 kDa. The ACE inhibition activity in sample weight ≤ 3 kDa is highest with value of 80.38 ± 2.69% followed by sample weight 3 – 10 kDa with a value of 49.40 ± 2.63% and sample weight ≥ 10 kDa with value of 42.73 ± 5.08%. Significant differences ( P ≤ 0.05) exist between sample weight ≤3 kDa and > 3 kDa. This research shows that molecular weight reduction increases ACE inhibition activity.

Highlights

  • Angiotensin Converting Enzyme (ACE) is an enzyme that effects hypertension or increases blood pressure

  • 2.0 g of chicken skin was manually defatted before soaking in acetone to remove the fat layer from the skin

  • The low fat content in the sample is desirable in hydrolysis process to reduce the formation of protein-lipid complex, which affects the formation of a stabil protein hydrolysate, and subsequently affects the angiotensin converting enzyme (ACE) inhibitory activity [15, 16]

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Summary

Introduction

Angiotensin Converting Enzyme (ACE) is an enzyme that effects hypertension or increases blood pressure. ACE is a dipeptidylcarboxypeptidase that converts the inactive decapeptide angiotensin I into the potent and active vasoconstrictor. It deactivates the bradykinin, which functions as a vasodilating agent [1]. The inhibition on the ACE activity gives antihypertensive affect to individuals. The activity of ACE inhibitor can be observed in food containing protein, through the presence of bioactive peptides. Certain peptide presence can inhibit the ACE activity. These peptides can be found in meat, the peptide presence is hidden in the core protein network and is only released in the presence of proteolysis enzymes, such as microbial and proteinase digestion [2]

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