Abstract
Abstract Iberian dry-cured ham is a meat product known as a source of different bioactive peptides due to its high protein content and intense hydrolysis during its processing. In this study, the potential of α-glucosidase inhibitory peptides generated in Iberian dry-cured ham was evaluated for the first time. After size-exclusion chromatography and high-performance liquid chromatography using different stationary phases, the characterization and identification of the peptide sequences contained in the most active fractions was done using MALDI-ToF mass spectrometry and Q-ToF mass spectrometry in tandem. A total of 16 and 47 sequences of peptides were identified in the two most active fractions. On the other hand, the α-glucosidase inhibitory activity of previously identified bioactive peptides in Spanish dry-cured ham such as AEEEYPDL and LGVGG was established, confirming their multifunctionality.
Highlights
The enzyme α-glucosidase (EC 3.2.1.20) is an important enzyme participating in the digestion of carbohydrates
The deproteinised Iberian dry-cured ham extract was injected in size-exclusion chromatography to separate peptides according to their molecular mass
These results are very similar to those obtained in previous studies for antioxidant activity as well as for ACE-inhibitory activity in different European dry-cured hams after a size-exclusion chromatography separation using a Sephadex G-25 column, where the maximum levels of antioxidant activity were determined to be in fractions corresponding to elution volumes from 200 mL to 250 mL in Spanish, Italian Parma, and Belgian dry-cured ham (Mora et al, 2014, 2016), and maximum levels for ACE-inhibitory activity were observed between 195 and 250 mL in all European and Iberian dry-cured hams (Mora et al, 2016; Mora, Escudero, Arihara, & Toldrá, 2015)
Summary
The enzyme α-glucosidase (EC 3.2.1.20) is an important enzyme participating in the digestion of carbohydrates. Due to its relation with the carbohydrate metabolism, this enzyme is frequently used as a target for the treatment of type 2 Diabetes mellitus (T2DM) disease, a serious global health problem (Mollica et al, 2019; Picot et al, 2017). Inhibitors of this enzyme are effective in retarding the carbohydrate digestion, reducing the impact of carbohydrates on blood glucose level and decreasing the chance for hyperglycemia (Bhandari, Jong-Anurakkun, Hong, & Kawabata, 2008; Zengin et al, 2019). The side effects and long synthetic routes necessary to obtain them has promoted researchers to look for different heterocyclic molecules such as oxindole derivatives (Asadollahi-Baboli & Dehnavi, 2018), triazole derivatives (Avula et al, 2019;), pyrrolidine derivatives (Guazzelli et al, 2019), and oxadiazole derivatives (Khan, Zafar, Patel, Shah, & Bishayee, 2019) as well as pyrazole-triazolopyrimidine hybrids (Pogaku, Gangarapu, Basavoju, Tatapudi, & Katragadda, 2019) or thiosemicarbazide-triazole hybrids (Bakherad, MohammadiKhanaposhtani, Sadeghi-Aliabadi, Rezaei, Fassihi, Bakherad, Rastegar, Biglar, Saghaie, & Larijani, 2019), using kinetic and molecular modeling studies in their design and evaluation (Dhameja & Gupta, 2019)
Sign-in/Register to view highlights & summary Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
