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. 2021 May 18;10(5):1112.
doi: 10.3390/foods10051112.

Effect of Protease Type and Peptide Size on the In Vitro Antioxidant, Antihypertensive and Anti-Diabetic Activities of Eggplant Leaf Protein Hydrolysates

Akinsola A Famuwagun  1   2 , Adeola M Alashi  1 , Saka O Gbadamosi  1 , Kehinde A Taiwo  2 , Durodoluwa Oyedele  3 , Odunayo C Adebooye  4 , Rotimi E Aluko  1
Affiliations

Effect of Protease Type and Peptide Size on the In Vitro Antioxidant, Antihypertensive and Anti-Diabetic Activities of Eggplant Leaf Protein Hydrolysates

Akinsola A Famuwagun et al. Foods. .

Abstract

Solanum macrocarpon (eggplant) leaf protein isolate (ELI) was hydrolyzed using four different enzymes to produce hydrolysates from alcalase (AH), chymotrypsin (CH) pepsin (PH) and trypsin (TH). CH had an overall stronger antioxidant property and was separated using ultrafiltration membranes into <1, 1-3 and 3-5 kDa peptide fractions. Gel-permeation chromatography confirmed conversion of the ELI (average of 22 kDa) into protein hydrolysates that contained smaller peptides (<6 kDa). A total of 23 peptides consisting of tri and tetrapeptides were identified from the CH, which is a wider spectrum when compared to seven for AH and four each for TH and PH. CH exhibited stronger scavenging activities against DPPH and hydroxyl radicals. CH and TH exhibited the strongest inhibitions against angiotensin-converting enzyme. In contrast, AH was the strongest inhibitor of α-amylase while AH and PH had strong inhibitory activities against α-glucosidase when compared with other hydrolysates. Ultrafiltration fractionation produced peptides that were stronger (p < 0.05) scavengers of DPPH, and hydroxyl radicals, in addition to better metal-chelating and enzyme inhibition agents. The study concluded that the eggplant protein hydrolysates and the UF fractions may find applications in tackling oxidative stress-related diseases and conditions involving excessive activities of the metabolic enzymes.

Keywords: Solanum macrocarpon; antioxidant; enzyme inhibition; leaf protein; membrane ultrafiltration; peptide sequence; protein hydrolysate.

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Conflict of interest statement

The authors declare no conflict of interest.

Figures

Figure 1
Figure 1
Degree of hydrolysis of alcalase (AH), chymotrypsin (CH), pepsin (PH) and trypsin (TH) eggplant leaf protein hydrolysates.
Figure 2
Figure 2
Comparative gel-permeation chromatograms of eggplant leaf protein isolate (ELI) and enzymatic protein hydrolysates: alcalase (AH), chymotrypsin (CH), pepsin (PH) and trypsin (TH). Inserted values indicate estimated molecular weights.
Figure 3
Figure 3
(A). Ferric reducing antioxidant power of glutathione (GSH), eggplant leaf protein isolate (ELI) and hydrolysates: alcalase (AH), chymotrypsin (CH), pepsin (PH) and trypsin (TH). Hydrolysates. (B). FRAP of chymotrypsin hydrolysate (CH) and the ultrafiltration peptide fractions. Values are mean ± standard deviation of three determinations. Bars with different letters (a–e) on the same layout are significantly different (p ≤ 0.05).
Figure 4
Figure 4
Inhibition of linoleic acid peroxidation by glutathione (GSH as control), eggplant leaf protein isolate (ELI) and enzymatic protein hydrolysates alcalase (AH), chymotrypsin (CH), pepsin (PH) and trypsin (TH).
Figure 5
Figure 5
α-Amylase inhibitory activities of (A) acarbose (standard), eggplant leaf protein isolate (ELI) and protein hydrolysates alcalase (AH), chymotrypsin (CH), pepsin (PH),and trypsin (TH), and(B) acarbose (standard) and CH-ultrafiltration peptide fractions. Values are mean ± standard deviation of three determinations. Bars with different letters (a–d) on the same layout are significantly different (p ≤ 0.05).
Figure 6
Figure 6
α-glucosidase inhibitory activities of (A) acarbose (standard), eggplant leaf protein isolate (ELI) and protein hydrolysates alcalase (AH), chymotrypsin (CH), pepsin (PH) and trypsin (TH), and (B) α-amylase inhibitory activities of ultrafiltration peptide fractions of CH and acarbose (standard). Values are mean ± standard deviation of three determinations. Bars with different letters (a–d) on the same layout are significantly different (p ≤ 0.05)
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