Angiotensin I-converting enzyme inhibitory activity of protein hydrolysates prepared from three freshwater carps (Catla catla,Labeo rohitaandCirrhinus mrigala) using Flavorzyme

2013 ◽  
Vol 49 (5) ◽  
pp. 1344-1350 ◽  
Author(s):  
Krishnamoorthy Elavarasan ◽  
Bangalore Aswathnarayan Shamasundar
Keyword(s):  
Inhibitory Activity ◽  
Protein Hydrolysates ◽  
Catla Catla ◽  
Converting Enzyme ◽  
Angiotensin I ◽  
Angiotensin I Converting Enzyme

scholarly journals A novel angiotensin I-converting enzyme inhibitory peptide derived from the trypsin hydrolysates of salmon bone proteins

PLoS ONE ◽  
2021 ◽  
Vol 16 (9) ◽  
pp. e0256595
Author(s):  
Thanakrit Kaewsahnguan ◽  
Sajee Noitang ◽  
Papassara Sangtanoo ◽  
Piroonporn Srimongkol ◽  
Tanatorn Saisavoey ◽  
...  
Keyword(s):  
Response Surface ◽  
Inhibitory Activity ◽  
Fish Bone ◽  
Protein Hydrolysates ◽  
Converting Enzyme ◽  
Angiotensin I ◽  
Ace Inhibitory Activity ◽  
Inhibitory Peptide ◽  
Angiotensin I Converting Enzyme ◽  
Ace Inhibitory

When fish are processed, fish bone becomes a key component of the waste, but to date very few researchers have sought to use fish bone to prepare protein hydrolysates as a means of adding value to the final product. This study, therefore, examines the potential of salmon bone, through an analysis of the benefits of its constituent components, namely fat, moisture, protein, and ash. In particular, the study seeks to optimize the process of enzymatic hydrolysis of salmon bone with trypsin in order to produce angiotensin-I converting enzyme (ACE) inhibitory peptides making use of response surface methodology in combination with central composite design (CCD). Optimum hydrolysis conditions concerning DH (degree of hydrolysis) and ACE-inhibitory activity were initially determined using the response surface model. Having thus determined which of the salmon bone protein hydrolysates (SBPH) offered the greatest level of ACE-inhibitory activity, these SBPH were duly selected to undergo ultrafiltration for further fractionation. It was found that the greatest ACE-inhibitory activity was achieved by the SBPH fraction which had a molecular weight lower than 0.65 kDa. This fraction underwent further purification using RP-HPLC, revealing that the F7 fraction offered the best ACE-inhibitory activity. For ACE inhibition, the ideal peptide in the context of the F7 fraction comprised eight amino acids: Phe-Cys-Leu-Tyr-Glu-Leu-Ala-Arg (FCLYELAR), while analysis of the Lineweaver-Burk plot revealed that the FCLYELAR peptide can serve as an uncompetitive ACE inhibitor. An examination of the molecular docking process showed that the FCLYELAR peptide was primarily able to provide ACE-inhibitory qualities as a consequence of the hydrogen bond interactions taking place between ACE and the peptide. Furthermore, upon isolation form the SBPH, the ACE-inhibitory peptide demonstrated ACE-inhibitory capabilities in vitro, underlining its potential for applications in the food and pharmaceutical sectors.

Purification and Characterization of Angiotensin-I Converting Enzyme Inhibitory Peptides from Prickly Ash (Zanthoxylum bungeanum Maxim) Seed Protein Hydrolysates

2016 ◽  
Vol 12 (4) ◽  
pp. 333-342 ◽  
Author(s):  
Hongyang Wu ◽  
Tailing Jiang ◽  
Xiaohua Dong ◽  
Guanghui Shen ◽  
Shanshan Li ◽  
...  
Keyword(s):  
Inhibitory Activity ◽  
Seed Protein ◽  
Protein Hydrolysates ◽  
Gel Chromatography ◽  
Converting Enzyme ◽  
Angiotensin I ◽  
Inhibitory Peptides ◽  
Angiotensin I Converting Enzyme ◽  
Zanthoxylum Bungeanum ◽  
Ace Inhibitory

Abstract Prickly ash (Zanthoxylum bungeanum Maxim) seed protein was hydrolyzed with papain to obtain hydrolysates with inhibitory activity against angiotensin-I converting enzyme (ACE). ACE inhibitory peptides (ACEIPs) were successfully purified from seed protein hydrolysates through ultrafiltration and gel chromatography. In vitro ACE inhibitory assay revealed an IC50 value of 0.032± 0.008 mg·mL−1 for a component with <5 kDa molecular weight. Four fractions were isolated by Sephadex G-25 gel chromatography under the following elution conditions: flow rate, 0.6 mL·min−1; initial volume, 2.0 mL; and sample concentration, 30 mg·mL−1. The second fraction showed the highest inhibitory activity with an IC50 value of 0.021±0.007 mg·mL−1. The stability of the ACE inhibitory activity of the obtained ACEIPs was identified under storage conditions with varied temperature, pH, and gastrointestinal protease digestion. Peptides derived from prickly ash seed protein hydrolysates may be a potential resource for exploring functional food or pharmaceuticals against hypertension.

Mung-bean Protein Hydrolysates Obtained with Alcalase Exhibit Angiotensin I-converting Enzyme Inhibitory Activity

2005 ◽  
Vol 11 (4) ◽  
pp. 281-287 ◽  
Author(s):  
Guan Hong Li ◽  
Guo Wei Le ◽  
Huan Liu ◽  
Yong Hui Shi
Keyword(s):  
Inhibitory Activity ◽  
Mung Bean ◽  
Protein Hydrolysates ◽  
Antihypertensive Activity ◽  
Converting Enzyme ◽  
Angiotensin I ◽  
Ace Inhibitory Activity ◽  
Angiotensin I Converting Enzyme ◽  
Ace Inhibitory ◽  
Bean Protein

Mung-bean protein isolates were hydrolysed by two proteases alcalase and neutrase commercially available for food industry use, and the angiotensin I-converting enzyme (ACE) inhibitory activities of the enzymatic hydrolysates were measured at different hydrolysis times. The non-hydrolysed protein showed no inhibitory activity. Hydrolysates generated with neutrase displayed very low ACE inhibitory activity, while those obtained with alcalase exhibited high inhibitory activity. The highest ACE inhibitory activity with the IC50 value of 0.64 mg protein/mL was found in the hydrolysate obtained with alcalase at 2h of hydrolysis time. These results indicated that mung-bean protein is a good protein source of ACE inhibitory peptides when hydrolysed with the protease alcalase. The mung-bean protein hydrolysates prepared with alcalase might be utilised for physiologically functional foods with antihypertensive activity.

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