Faculty of Biology, University of Latvia
Hard copy: ISSN 1691–8088
On-line: ISSN 2255–9582
Environ Exp Biol (2016) 14: 163–172
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Environmental and

Environ Exp Biol (2016) 14: 163–172

Orginal Articles

In vitro antioxidant and α-amylase inhibitory properties of watermelon seed protein hydrolysates

Rotimi Olusanya Arise1*, Abeeb Abiodun Yekeen1, Oluwafemi Emmanuel Ekun1,2
1 Department of Biochemistry, Faculty of Life Sciences, University of Ilorin, Ilorin, Nigeria
2 Department of Biochemistry, Faculty of Sciences, Adekunle Ajasin University, Akungba-Akoko, Nigeria
* Corresponding author, E-mail: ariserotimi@gmail.com


Proteins from watermelon (Citrullus lanatus L.) seed were isolated using acid-induced precipitation method and then hydrolysed using pepsin, trypsin and alcalase. The hydrolysates were investigated for in vitro antioxidant and α-amylase inhibitory properties. The yield of peptic hydrolysis (68.9 ± 1.0%) was significantly higher than of tryptic (41.4 ± 1.1%) and alcalase (38.5 ± 0.5%) hydrolysis. Peptic hydrolysate showed the highest radical-scavenging ability whereas tryptic hydrolysate gave the highest reducing ability. In a concentration-dependent manner, the hydrolysates demonstrated potent α-amylase inhibitory ability with alcalase and tryptic hydrolysates exhibiting 86.0 ± 3.9 and 83.0 ± 3.5% α-amylase inhibition respectively (IC50 0.149 to 0.234 mg mL–1). Kinetic analysis revealed that the three enzyme hydrolysates inhibited α-amylase activity via a non-competitive inhibition mechanism. The results therefore indicate that these multidirectional bioactivities of watermelon seed protein hydrolysates may serve as useful tools in the formulation of antidiabetic agents.

Key words: alcalase, antioxidant, antidiabetic, Citrullus lanatus, pepsin, trypsin.

Environ Exp Biol (2016) 14: 163–172
 DOI: http://doi.org/10.22364/eeb.14.23

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