Kinetics of angiotensin -1 converting enzyme inhibition and antioxidative properties of Azadirachta indica seed protein hydrolysates

Arise, Rotimi Olusanya and Acho, Marvellous A. and Yekeen, Abeeb A. and Omokanye, Ibrahim A. and Sunday-Nwaso, Elizabeth O. and Akiode, Olatunbosun S. and Malomo, S.O. (2019) Kinetics of angiotensin -1 converting enzyme inhibition and antioxidative properties of Azadirachta indica seed protein hydrolysates. Heliyon, 5. ISSN 2405-8440

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Abstract

Neem (Azadirachta indica) seed protein hydrolysates were investigated forin vitroantioxidant and angiotensin 1-converting enzyme (ACE)-inhibitory activities. Neem seed proteins were hydrolysed using pepsin, trypsin andAlcalase. The degree of pepsin hydrolysis of neem seed protein was significantly higher (p<0.05) than those oftrypsin and Alcalase hydrolysis. Proteolytic hydrolysis of the isolate resulted in hydrolysates with improved Arg/Lys ratio, with pepsin hydrolysates still being able to maintain an acceptable level of essential amino acidscomparable to that of the isolate. At 2.5 mg/mL, pepsin neem seed protein hydrolysate (NSPH) demonstrated thestrongest antioxidant activity with 67.15 % and 50.07 % DPPH- and superoxide anion radical-scavenging ac-tivities, respectively, while trypsin NSPH had the highest ferric-reducing power. Using N-[3-(2-furyl)acryloyl]-L-phenylalanyl-glycyl-glycine (FAPGG) as substrate, NSPHs strongly inhibited ACE (69.20–80.39 %) in aconcentration-dependent manner. Pepsin NSPH had higher ACE-inhibitory activity than trypsin and AlcalaseNSPHs. Kinetic studies showed the mechanism of ACE inhibition to be mixed-type withKivalues of 0.62, 0.84, 1.5for pepsin, trypsin and alcalase NSPH, respectively. These results suggest that NSPH can be used as a potentialnutraceutical with antioxidant capacity and inhibitory activity against ACE

Item Type: Article
Subjects: Q Science > QD Chemistry
Q Science > QH Natural history > QH301 Biology
Depositing User: Mr DIGITAL CONTENT CREATOR LMU
Date Deposited: 23 Sep 2019 08:30
Last Modified: 23 Sep 2019 08:30
URI: https://eprints.lmu.edu.ng/id/eprint/2341

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