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231226s2023 xx |||||o 00| ||eng c |
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|a 10.1016/j.plaphy.2022.11.026
|2 doi
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|a pubmed24n1165.xml
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|a (DE-627)NLM349724180
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|a (NLM)36459867
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|a (PII)S0981-9428(22)00527-7
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|a DE-627
|b ger
|c DE-627
|e rakwb
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|a eng
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|a Alblooshi, Munira
|e verfasserin
|4 aut
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|a Multifunctional bioactive properties of hydrolysates from colocynth (Citrullus colocynthis) seeds derived proteins
|b Characterization and biological properties
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|c 2023
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|a Text
|b txt
|2 rdacontent
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|a ƒaComputermedien
|b c
|2 rdamedia
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|a ƒa Online-Ressource
|b cr
|2 rdacarrier
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|a Date Completed 16.01.2023
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|a Date Revised 16.01.2023
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|a published: Print-Electronic
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|a Citation Status MEDLINE
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|a Copyright © 2022 Elsevier Masson SAS. All rights reserved.
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|a 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
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|a Journal Article
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|a Anti-diabetic
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|a Anti-hyperlipidaemia
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|a Antioxidant
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|a Colocynth
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|a Protein hydrolysates
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|a Bromelains
|2 NLM
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|a 9001-00-7
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|a Protein Hydrolysates
|2 NLM
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|a Chymotrypsin
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|a EC 3.4.21.1
|2 NLM
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|a alpha-Glucosidases
|2 NLM
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|a EC 3.2.1.20
|2 NLM
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|a Antioxidants
|2 NLM
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|a alpha-Amylases
|2 NLM
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|a EC 3.2.1.1
|2 NLM
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|a Lipase
|2 NLM
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|a EC 3.1.1.3
|2 NLM
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|a Subtilisins
|2 NLM
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|a EC 3.4.21.-
|2 NLM
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|a Devarajan, Aarthi Rekha
|e verfasserin
|4 aut
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|a Singh, Brij Pal
|e verfasserin
|4 aut
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|a Ramakrishnan, Preethi
|e verfasserin
|4 aut
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|a Mostafa, Hussein
|e verfasserin
|4 aut
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|a Kamal, Hina
|e verfasserin
|4 aut
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|a Mudgil, Priti
|e verfasserin
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|a Maqsood, Sajid
|e verfasserin
|4 aut
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| 773 |
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|i Enthalten in
|t Plant physiology and biochemistry : PPB
|d 1991
|g 194(2023) vom: 01. Jan., Seite 326-334
|w (DE-627)NLM098178261
|x 1873-2690
|7 nnns
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| 773 |
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|g volume:194
|g year:2023
|g day:01
|g month:01
|g pages:326-334
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|u http://dx.doi.org/10.1016/j.plaphy.2022.11.026
|3 Volltext
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