TY - JOUR
T1 - Multifunctional bioactive properties of hydrolysates from colocynth (Citrullus colocynthis) seeds derived proteins
T2 - Characterization and biological properties
AU - Alblooshi, Munira
AU - Devarajan, Aarthi Rekha
AU - Singh, Brij Pal
AU - Ramakrishnan, Preethi
AU - Mostafa, Hussein
AU - Kamal, Hina
AU - Mudgil, Priti
AU - Maqsood, Sajid
N1 - Funding Information:
Authors would like to thank United Arab Emirates University for funding this study through a research grant 12F002 (AUA-UAEU grant).
Publisher Copyright:
© 2022 Elsevier Masson SAS
PY - 2023/1
Y1 - 2023/1
N2 - Citrullus colocynthis (Colocynth) has gained a great deal of interest in their applications as indigenous nutraceutical and as a functional food ingredient. The intact colocynth seed protein was enzymatically hydrolyzed using proteolytic enzymes (alcalase, bromelain, and chymotrypsin) at different time intervals of 3, 6, and 9 h. The highest degree of hydrolysis (87.82%) was observed in chymotrypsin derived colocynth seed protein hydrolysates (CSPH) for 9 h. The CSPHs was further investigated through in-vitro assay to explore its potential biological activity such as antioxidant, inhibition of enzymatic marker related to diabetes (DPP-IV, α-glucosidase and α-amylase) and hyperlipidaemia (cholesteryl esterase and pancreatic lipase). Chymotrypsin hydrolysate showed the strongest DPPH (65.7 mM TEAC) and ABTS (525.2 mM TEAC) radical scavenging activity after 6 h of hydrolysis. Moreover, chymotrypsin-treated CSPH for 6 h inhibited cholesteryl esterase (IC50 = 13.68 μg/mL) and pancreatic lipase (IC50 = 14.12 μg/mL) significantly when compared to native protein. Whereas, bromelain and alcalase treated hydrolysate for 6 h effectively inhibited α-glucosidase and α-amylase at an inhibitory concentration of IC50 = 13.27 μg/mL and of IC50 = 17 μg/mL. Overall, the findings indicated that protein hydrolysates exhibited superior biological activity than intact colocynth seed proteins isolate (CSPI) and could be a sustainable source of bioactive peptides.
AB - Citrullus colocynthis (Colocynth) has gained a great deal of interest in their applications as indigenous nutraceutical and as a functional food ingredient. The intact colocynth seed protein was enzymatically hydrolyzed using proteolytic enzymes (alcalase, bromelain, and chymotrypsin) at different time intervals of 3, 6, and 9 h. The highest degree of hydrolysis (87.82%) was observed in chymotrypsin derived colocynth seed protein hydrolysates (CSPH) for 9 h. The CSPHs was further investigated through in-vitro assay to explore its potential biological activity such as antioxidant, inhibition of enzymatic marker related to diabetes (DPP-IV, α-glucosidase and α-amylase) and hyperlipidaemia (cholesteryl esterase and pancreatic lipase). Chymotrypsin hydrolysate showed the strongest DPPH (65.7 mM TEAC) and ABTS (525.2 mM TEAC) radical scavenging activity after 6 h of hydrolysis. Moreover, chymotrypsin-treated CSPH for 6 h inhibited cholesteryl esterase (IC50 = 13.68 μg/mL) and pancreatic lipase (IC50 = 14.12 μg/mL) significantly when compared to native protein. Whereas, bromelain and alcalase treated hydrolysate for 6 h effectively inhibited α-glucosidase and α-amylase at an inhibitory concentration of IC50 = 13.27 μg/mL and of IC50 = 17 μg/mL. Overall, the findings indicated that protein hydrolysates exhibited superior biological activity than intact colocynth seed proteins isolate (CSPI) and could be a sustainable source of bioactive peptides.
KW - Anti-diabetic
KW - Anti-hyperlipidaemia
KW - Antioxidant
KW - Colocynth
KW - Protein hydrolysates
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U2 - 10.1016/j.plaphy.2022.11.026
DO - 10.1016/j.plaphy.2022.11.026
M3 - Article
C2 - 36459867
AN - SCOPUS:85145576097
SN - 0981-9428
VL - 194
SP - 326
EP - 334
JO - Plant Physiology and Biochemistry
JF - Plant Physiology and Biochemistry
ER -
