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Optimization of Preparation of Angiotensin-I Converting Enzyme Inhibitory Peptides Derived from Terebrio molitor L. Protein by Response Surface Methodology

CUI Nan, TAO Xiao-yun, LI Juan, CHEN Jian, ZHAO Li-yi, SUN Ai-dong   

  1. Beijing Key Laboratory of Forestry Food Processing and Safety, College of Biological Sciences and Technology, Beijing Forestry
    University, Beijing 100083, China
  • Online:2014-08-15 Published:2014-08-25

Abstract:

In this study, Tenebrio molitor protein powder was hydrolyzed by papain to prepare angiotensin-I converting
enzyme (ACE) inhibitory peptides. Single factor design (involving temperature, pH, substrate concentration, enzyme dosage
and hydrolysis time) and response surface methodology were used to determine the optimal hydrolysis conditions for
preparing ACE inhibitory peptides. ACE inhibitory rates of hydrolysates were determined by enzyme-linked immunosorbent
assay (ELISA). The optimum conditions were determined as follows: substrate concentration 7 g/100 mL, enzyme dosage 1%,
pH 6.5, hydrolysis time 7 h and temperature 55 ℃. The ACE inhibitory rate obtained under these conditions was 58.86%.

Key words: Tenebrio molitor protein powder, papain, ACE inhibitory peptides, hydrolysis conditions

CLC Number: