Effect Of Pretreatment On The Release Of Collagen Ace Inhibitory Peptide During Enzymatic Hydrolysis
Keywords
Collagen Pretreatment Polypeptides Degree Of Hydrolysis Angiotensin-Converting-Enzyme Inhibition Rate
Abstract
This article explores the effects of five pretreatment methods of acid, alkali, heat, ultrasound, and ultrahigh pressure on the preparation of ACE inhibitory peptides from collagen. After pretreatment of collagen, alkaline protease was used to enzymatically hydrolyze the hydrolyzate to prepare a hydrolyzate. The degree of hydrolysis, ACE inhibition rate and molecular weight distribution of the hydrolyzate were measured. The results showed that the degree of hydrolysis and ACE inhibition rate of the hydrolyzate in the alkali and ultrasonic treatment groups were the same. Higher than the untreated group, indicating that these two pretreatment methods may be beneficial to the exposure of collagen triple helix region sites; DSC and infrared analysis of the collagen structure after pretreatment showed that alkali treatment changed the conformational characteristics of collagen and affected non-covalent bonds. The balance of the collagen triple helix region is fully exposed, but the integrity of the subunits is maintained. Ultrasonic treatment destroys the covalent cross-linking of the collagen helix region, exposing more hydrophobic sites, which is conducive to alkaline protease enzymes. However, acid, heat and ultrahigh pressure treatments mainly affect the non-helical regions of collagen and cannot promote the release of collagen ACE inhibitory active peptides during enzymatic hydrolysis. The effects of five pretreatments (acid, alkali, heat, ultrasound, and high pressure) on the production of angiotensin-converting-enzyme (ACE) inhibitory peptide from collagen were explored. After pretreatment, collagen was hydrolyzed by Alcalase, and the degree of hydrolysis (DH), ACE inhibitory activity, and the molecular weight distribution of the hydrolysate were measured. Results showed that alkali- and ultrasound-treated groups had higher DH and ACE inhibition rate than the untreated group, which indicated that these two pretreatments can favor exposure of sites in the triple-helical region of collagen. Differential scanning calorimetry (DSC) and Fourier transform infrared spectroscopy (FT-IR) were used to analyze the structure of collagen, and the results showed that alkali treatment changed the configuration of collagen, affected the balance of non-covalent bonds, and exposed the hydrophobic site completely in the triple-helical region of collagen. However, the integrity of the subunits was maintained. Ultrasound treatment damaged the covalent bonds in the helical region of collagen and exposed more hydrophobic sites, which was helpful for alcalase hydrolysis. In contrast, acid, heat, and high-pressure treatments mostly affected the non-helical region of collagen, and could not promote the release of ACE inhibitory peptide from collagen during enzymatic hydrolysis.
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Original research was done by Huang Dandan
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