Purification and characterization of angiotensin converting enzyme-inhibitory derived from crocodile blood hydrolysates

Ngo-Son, Arnon; Katekaew, Somporn

doi:10.1590/fst.08318

Cited by 3 publications

(3 citation statements)

References 26 publications

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“…Protease G6, an alkaline serine endoprotease, is reported as a commercial proteolytic enzyme [ 47 ]. The anti-hypertensive effects of protease G6-digested rice bran (G6RB) were reported in in vivo studies and its mechanism was determined in previous in vitro studies.…”

Section: Anti-hypertensive Effects Of Protease-digested Rice Branmentioning

confidence: 99%

Anti-Hypertensive Effects of Peptides Derived from Rice Bran Protein

Shobako

Ohinata

2020

Nutrients

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Hypertension is one of the major risk factors for arteriosclerosis. Anti-hypertensive peptides derived from animal proteins, such as milk, eggs and fish, are well studied. Anti-hypertensive peptides have also been identified from plant proteins such as soybeans. Rice bran, a byproduct of white rice polishing, is rich in protein and its high protein efficiency ratio is well known. This review discusses the anti-hypertensive peptides identified from rice bran protein and their mechanisms. In addition, we describe protease-digested rice bran from which functional peptides have not been isolated.

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Section: Anti-hypertensive Effects Of Protease-digested Rice Branmentioning

confidence: 99%

Anti-Hypertensive Effects of Peptides Derived from Rice Bran Protein

Shobako

Ohinata

2020

Nutrients

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“…In addition to being efficient amino acid sources, bioactive oligopeptides have been reported to possess many physiological functions and attractive physic properties in pharmacy (e.g., anticancer, antimicrobial, antihypertensive and antiinflammatory activities, anticoagulant, and immunomodulatory), foods (gelling activity and emulsifying property), cosmetic (antioxidant and water holding capacity), and other functional products (foaming ability and hydrophobicity) [2][3][4][5]. In recent years, collagen oligopeptides attract more and more attention due to their various bioactive properties, such as angiotensin I converting enzyme (ACE) inhibitory activity, antioxidant activity, immunomodulatory and antimicrobial activities [6][7][8][9], and beneficial effects on human health, including improving skin health, muscle strength, and bone density [10][11][12], and reducing obesity, joint pain, and blood pressure [13][14][15]. Collagen oligopeptides have been widely applied in food, cosmetics, healthcare, and pharmaceutical industries [16][17][18].…”

Section: Introductionmentioning

confidence: 99%

“…Enzymatic hydrolysis is now the common method to prepare collagen bioactive peptides from collagen-rich animal tissues, such as skin, bones, tendons, and ligaments. Nowadays, the common enzymes for preparing collagen bioactive peptides are proteases from plants, animals, and bacteria, such as serine proteases alcalase of the MEROPS S8 family and trypsin and α-chymotrypsin of the MEROPS S1 family, aspartic protease pepsin of the MEROPS A1 family, cysteine protease papain of the MEROPS C1 family, and metalloprotease thermolysin of the MEROPS M4 family [6,[19][20][21][22]. The S8 family is the second largest family of serine proteases after the S1 family [23].…”

Section: Introductionmentioning

confidence: 99%

A Novel Gelatinase from Marine Flocculibacter collagenilyticus SM1988: Characterization and Potential Application in Collagen Oligopeptide-Rich Hydrolysate Preparation

Cheng

Teng

et al. 2022

Marine Drugs

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Although the S8 family in the MEROPS database contains many peptidases, only a few S8 peptidases have been applied in the preparation of bioactive oligopeptides. Bovine bone collagen is a good source for preparing collagen oligopeptides, but has been so far rarely applied in collagen peptide preparation. Here, we characterized a novel S8 gelatinase, Aa2_1884, from marine bacterium Flocculibacter collagenilyticus SM1988T, and evaluated its potential application in the preparation of collagen oligopeptides from bovine bone collagen. Aa2_1884 is a multimodular S8 peptidase with a distinct domain architecture from other reported peptidases. The recombinant Aa2_1884 over-expressed in Escherichia coli showed high activity toward gelatin and denatured collagens, but no activity toward natural collagens, indicating that Aa2_1884 is a gelatinase. To evaluate the potential of Aa2_1884 in the preparation of collagen oligopeptides from bovine bone collagen, three enzymatic hydrolysis parameters, hydrolysis temperature, hydrolysis time and enzyme-substrate ratio (E/S), were optimized by single factor experiments, and the optimal hydrolysis conditions were determined to be reaction at 60 ℃ for 3 h with an E/S of 400 U/g. Under these conditions, the hydrolysis efficiency of bovine bone collagen by Aa2_1884 reached 95.3%. The resultant hydrolysate contained 97.8% peptides, in which peptides with a molecular weight lower than 1000 Da and 500 Da accounted for 55.1% and 39.5%, respectively, indicating that the hydrolysate was rich in oligopeptides. These results indicate that Aa2_1884 likely has a promising potential application in the preparation of collagen oligopeptide-rich hydrolysate from bovine bone collagen, which may provide a feasible way for the high-value utilization of bovine bone collagen.

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