Dipeptidyl peptidase-IV, α-amylase, and angiotensin I converting enzyme inhibitory properties of novel camel skin gelatin hydrolysates
| Autor: | Noura Al Ahbabi, Maitha Alameri, Priti Mudgil, Hina Kamal, Sajid Maqsood, Baboucarr Jobe |
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| Rok vydání: | 2019 |
| Předmět: |
0106 biological sciences
chemistry.chemical_classification Protease food.ingredient biology medicine.medical_treatment Proteolytic enzymes Substrate (chemistry) 04 agricultural and veterinary sciences 040401 food science 01 natural sciences Gelatin Dipeptidyl peptidase Hydrolysate 0404 agricultural biotechnology Enzyme food chemistry Biochemistry 010608 biotechnology biology.protein medicine Amylase Food Science |
| Zdroj: | LWT. 101:251-258 |
| ISSN: | 0023-6438 |
| DOI: | 10.1016/j.lwt.2018.11.014 |
| Popis: | In-vitro antidiabetic and antihypertensive properties of novel camel skin gelatin hydrolysates (CSGHs) were reported for the first time. Effect of different proteolytic enzymes, time of hydrolysis and enzyme: substrate (E/S) ratio on the bioactive (antidiabetic and antihypertensive) properties was explored. Results revealed that CSGHs exhibited highly potent inhibitory activity against dipeptidyl peptidase-IV (DPP-IV), pancreatic α-amylase (PA) and angiotensin-I converting enzyme (ACE) compared to non-hydrolyzed camel skin gelatin. All three enzyme combinations used produced highly potent PA inhibitory hydrolysates while for DPP-IV inhibitory property, protease and alcalase-protease (A/P) in combination produced more potent hydrolysates than alcalase generated hydrolysates. Moreover, alcalase and protease generated hydrolysates were highly active in inhibiting ACE activity in comparison to their combination (AP) (P |
| Databáze: | OpenAIRE |
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