FOOD SCIENCE ›› 2012, Vol. 33 ›› Issue (1): 180-185.

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Preparation of ACE Inhibitory Peptides by Bromelain Hydrolysis of Loach (Misgurnus anguillicaudatus) Protein

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  • Received:2011-05-05 Revised:2012-01-08 Online:2012-01-15 Published:2012-01-12

Abstract: The present deals with the enzymatic preparation of angiotensin-converting enzyme (ACE) inhibitory active peptides from loach (Misgurnus anguillicaudatus) protein. An L9(34) orthogonal array design methods based on single factor experiments was used to optimize the hydrolysis conditions for achieving maximum ACE inhibitory activity of loach protein hydrolysates. HPLC was used to determine ACE inhibitory activity of loach protein hydrolysates. Bromelain was found to be more suitable to prepare ACE inhibitory active peptides than trypsin, pepsin, flavourzyme and protamex. The optimal hydrolysis conditions were temperature of 55 ℃, solid-to-liquid ratio of 1:3, pH of 6.5, bromelain dose of 1000 U/g protein and hydrolysis duration of 90 min. The IC50 of the loach protein hydrolysate obtained under these conditions was 0.0184 mg/mL and the relative molecular weight distribution of ACE inhibitory peptides in it was mainly concentrated around 924.

Key words: Misgurnus anguillicaudatus, enzymatic hydrolysis, antihypertensive activity, angiotensin I-converting enzyme (ACE), bromelain

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