The Influence of the Extent of Enzymatic Hydrolysis on Antioxidative Properties and ACE-Inhibitory Activities of Protein Hydrolysates from Goby (Zosterisessor ophiocephalus) Muscle

The effects of power ultrasound pretreatments on the degree of hydrolysis (DH), angiotensin-I-converting enzyme (ACE) inhibitory activity, amino acid composition, surface hydrophobicity, protein solubility, and thermal stability of ACE inhibition of rapeseed protein hydrolysates were evaluated. Ultrasonic pretreatments before enzymolysis in terms of power and exposure time increased the DH and ACE inhibitory activities over the control (without sonication). In this study, maximum DH 22.07% and ACE inhibitory activity 72.13% were achieved at 600 W and 12 min pretreatment. Compared to the hydrolysates obtained without sonication, the amino acid profile of ultrasound pretreated hydrolysates showed significant changes particularly in the proline content and hydrophobic amino acids with an increased rate of 2.47% and 6.31%, respectively. Ultrasound pretreatment (600 watts, 12 min) improved functional properties of protein hydrolysates over control by enhancing surface hydrophobicity and solubility index with an increased rate of 130.76% and 34.22%. Moreover, the stability test showed that the ACE inhibitory activity remains stable against heat treatments. However, extensive heat, prolonged heating time, and alkaline conditions were not in the favor of stability test, while under mild heat and acidic conditions their ACE inhibitory activities were not significantly different from unheated samples.

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Antioxidant, anticancer and ACE-inhibitory activities of bioactive peptides from wheat germ protein hydrolysates

Food Bioscience ◽

10.1016/j.fbio.2019.100450 ◽

2019 ◽

Vol 32 ◽

pp. 100450 ◽

Cited By ~ 10

Author(s):

Zohreh Karami ◽

Seyed Hadi Peighambardoust ◽

Javad Hesari ◽

Behrouz Akbari-Adergani ◽

David Andreu

Keyword(s):

Wheat Germ ◽

Bioactive Peptides ◽

Protein Hydrolysates ◽

Inhibitory Activities ◽

Ace Inhibitory

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PREPARATION AND CHARACTERIZATION OF MUSSEL (MYTILUS EDULIS) PROTEIN HYDROLYSATES WITH ANGIOTENSIN-I-CONVERTING ENZYME (ACE) INHIBITORY ACTIVITY BY ENZYMATIC HYDROLYSIS

Journal of Food Biochemistry ◽

10.1111/j.1745-4514.2010.00505.x ◽

2010 ◽

Vol 36 (1) ◽

pp. 66-74 ◽

Cited By ~ 11

Author(s):

ZHI-YUAN DAI ◽

YAN-PING ZHANG ◽

HONG ZHANG ◽

YAN-BIN LU

Keyword(s):

Enzymatic Hydrolysis ◽

Mytilus Edulis ◽

Inhibitory Activity ◽

Protein Hydrolysates ◽

Converting Enzyme ◽

Angiotensin I ◽

Ace Inhibitory Activity ◽

Angiotensin I Converting Enzyme ◽

Ace Inhibitory

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Biological activity of camel milk casein following enzymatic digestion

Journal of Dairy Research ◽

10.1017/s0022029911000628 ◽

2011 ◽

Vol 78 (4) ◽

pp. 471-478 ◽

Cited By ~ 56

Author(s):

Maryam Salami ◽

Ali Akbar Moosavi-Movahedi ◽

Faezeh Moosavi-Movahedi ◽

Mohammad Reza Ehsani ◽

Reza Yousefi ◽

...

Keyword(s):

Antioxidant Activity ◽

Enzymatic Hydrolysis ◽

Natural Antioxidants ◽

Enzymatic Digestion ◽

Camel Milk ◽

Trolox Equivalent Antioxidant Capacity ◽

Trolox Equivalent ◽

Inhibitory Activities ◽

Milk Casein ◽

Ace Inhibitory

The aim of this study was to investigate the effects of enzymatic hydrolysis with digestive enzymes of camel whole casein and beta-casein (β-CN) on their antioxidant and Angiotensin Converting Enzyme (ACE)-inhibitory properties. Peptides in each hydrolysate were fractionated with ultra-filtration membranes. The antioxidant activity was determined using a Trolox equivalent antioxidant capacity (TEAC) scale. After enzymatic hydrolysis, both antioxidant and ACE-inhibitory activities of camel whole casein and camel β-CN were enhanced. Camel whole casein and β-CN showed significant ACE-inhibitory activities after hydrolysis with pepsin alone and after pepsinolysis followed by trypsinolysis and chymotrypsinolysis. Camel β-CN showed high antioxidant activity after hydrolysis with chymotrypsin. The results of this study suggest that when camel milk is consumed and digested, the produced peptides start to act as natural antioxidants and ACE-inhibitors.

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