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<p>The global rise in diet-related chronic diseases, such as type 2 diabetes and hypertension, has increased interest in plant-derived bioactive peptides for managing metabolic health. African baobab seed (<i>Adansonia digitata</i>) is rich in protein and other bioactive compounds and may offer therapeutic potential. However, it is underutilised and underexplored as a source of functional peptides. This study aimed to extract, hydrolyse and characterise bioactive peptides from baobab seeds, and evaluate their antioxidant and enzyme-inhibitory activities. Protein isolate (BPI), obtained from defatted baobab flour using isoelectric precipitation, was hydrolysed with Alcalase (pH 8, 50&#xa0;°C) to produce baobab protein hydrolysate (BPH). Amino acid profile, phytochemicals, and antioxidant activity (DPPH, FRAP, TAC). BPH was further fractionated by Ultrafiltration Molecular Weight Cut Off, bioactive compounds were identified by HPLC, and enzyme-inhibitory (ACE inhibitory, α-amylase, and α-glucosidase) activities were determined. Alcalase hydrolysis yielded BPH with a 32.18% degree of hydrolysis. Sixteen amino acids were identified, of which 9 were essential, with leucine being the most abundant. BPH showed higher phenolic and flavonoid contents and stronger antioxidant activities than BPI. The bioactive compounds identified in BPH included organic acids (citric, ascorbic, benzoic, gallic) and polyphenols [quercetin, (-)- Epicatechin, (+)- Catechin, chlorogenic acid, luteolin, procyanidin]. Peptide fractionation gave four molecular weight ranges (&lt; 2.5, 2.5–5.0, 5.0–7.5, and 7.5–10&#xa0;kDa), with small- to mid-sized peptides (&lt; 2.5–7.5&#xa0;kDa) exhibiting the strongest ACE inhibition (up to 39.34%). All the four fractions had lower IC₅₀ for α-amylase (18.54–18.99&#xa0;µg/mL) and α-glucosidase (18.15–18.70&#xa0;µg/mL), significantly lower than acarbose (with IC<sub>50</sub> of 19.27 and 19.42&#xa0;µg/mL, respectively). Baobab protein hydrolysate is rich in bioactive peptides, organic acids, and polyphenols, with significant antioxidant, antidiabetic, and antihypertensive potential. Baobab seed proteins can have potential applications in developing functional foods and nutraceuticals for oxidative stress, hypertension, and hyperglycemia management.</p>

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Baobab seed protein hydrolysate as a source of bioactive peptides with antioxidant, antidiabetic, and antihypertensive potential

  • 期刊论文

  • 发表日期：

    2026年1月17日

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  • Olufunke O. Ezekiel,
  • Modupeola A. Oguntoye,
  • Olusegun A. Olabode,
  • Safura O. Olawoyin

摘要

The global rise in diet-related chronic diseases, such as type 2 diabetes and hypertension, has increased interest in plant-derived bioactive peptides for managing metabolic health. African baobab seed (Adansonia digitata) is rich in protein and other bioactive compounds and may offer therapeutic potential. However, it is underutilised and underexplored as a source of functional peptides. This study aimed to extract, hydrolyse and characterise bioactive peptides from baobab seeds, and evaluate their antioxidant and enzyme-inhibitory activities. Protein isolate (BPI), obtained from defatted baobab flour using isoelectric precipitation, was hydrolysed with Alcalase (pH 8, 50 °C) to produce baobab protein hydrolysate (BPH). Amino acid profile, phytochemicals, and antioxidant activity (DPPH, FRAP, TAC). BPH was further fractionated by Ultrafiltration Molecular Weight Cut Off, bioactive compounds were identified by HPLC, and enzyme-inhibitory (ACE inhibitory, α-amylase, and α-glucosidase) activities were determined. Alcalase hydrolysis yielded BPH with a 32.18% degree of hydrolysis. Sixteen amino acids were identified, of which 9 were essential, with leucine being the most abundant. BPH showed higher phenolic and flavonoid contents and stronger antioxidant activities than BPI. The bioactive compounds identified in BPH included organic acids (citric, ascorbic, benzoic, gallic) and polyphenols [quercetin, (-)- Epicatechin, (+)- Catechin, chlorogenic acid, luteolin, procyanidin]. Peptide fractionation gave four molecular weight ranges (< 2.5, 2.5–5.0, 5.0–7.5, and 7.5–10 kDa), with small- to mid-sized peptides (< 2.5–7.5 kDa) exhibiting the strongest ACE inhibition (up to 39.34%). All the four fractions had lower IC₅₀ for α-amylase (18.54–18.99 µg/mL) and α-glucosidase (18.15–18.70 µg/mL), significantly lower than acarbose (with IC50 of 19.27 and 19.42 µg/mL, respectively). Baobab protein hydrolysate is rich in bioactive peptides, organic acids, and polyphenols, with significant antioxidant, antidiabetic, and antihypertensive potential. Baobab seed proteins can have potential applications in developing functional foods and nutraceuticals for oxidative stress, hypertension, and hyperglycemia management.