ArticleFoods (Basel, Switzerland)2022
Optimization of Extraction Process of Polysaccharides MAP-2 from Opuntia Milpa Alta by Response Surface Methodology and Evaluation of Its Potential as α-Glucosidase Inhibitor.
Article in Foods (Basel, Switzerland), 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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4 citing papers in PubMed, 10 citations in OpenAlex.
- Cactus-Based Biopolymers: A Review on Sustainable Innovations in Edible Packaging, UV Protection, Antioxidant Films, and Industrial Applications.Food science & nutrition · 2025Review
- A Hypoglycemic Peptide fromNutrients · 2025Article
- Optimization of Enzyme-Assisted Aqueous Extraction of Polysaccharide fromMolecules (Basel, Switzerland) · 2023Article
- Cutaneous Manifestations Associated with Diabetes Mellitus-A Retrospective Study.Diseases (Basel, Switzerland) · 2023Article
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4 authors at 1 institution in 1 country.
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Abstract
The α-glucosidase inhibitors play an important role in blood glucose control in patients with type 2 diabetes. At present, the development of new α-glucosidase inhibitors is an urgent clinical need. Our previous studies have found that the polysaccharide MAP-2 in the cactus Opuntia Milpa Alta has significantly better activity than acarbose (one of the most widely used first-line α-glucosidase inhibitors in clinical practice), but its optimal extraction process parameters and inhibition kinetic characteristics are not clear, and whether it has the potential to become a new α-glucosidase inhibitors is also unclear. In this study, based on previous research, we used the combination of single factor experiments and the response surface method (RSM) to identify the optimal extraction conditions for MAP-2 as follows: solid-liquid ratio 1:4, extraction temperature 90 °C, extraction time 1 h. Under these conditions, the extraction yield of MAP-2 was 3.47 ± 0.062%. When the concentration of MAP-2 was 16 mg/mL, the inhibition rate of α-glucosidase was 91.13 ± 0.62%. In addition, the results of inhibition kinetics showed that the inhibition rate of MAP-2 on α-glucosidase was the highest at pH 7.4 for 30 min, and showed a good dose-effect relationship, which was a reversible competitive inhibition. Meanwhile, we also compared the activities of MAP-2 and acarbose on the side effects of acarbose related enzymes. Compared with acarbose, MAP-2 not only had a better activation effect on lactase, but also inhibited the activity of hyaluronidase, and the activation and inhibition rate were positively correlated with the concentration. However, under the same conditions, the effect of acarbose on hyaluronidase was opposite to that of MAP-2. At low concentration, acarbose had a certain activation effect on lactase, but gradually attained an inhibitory effect with the increase in concentration. In contrast, MAP-2 not only activates lactase activity, improves diarrhea, abdominal distension, and abdominal pain, but also inhibits hyaluronidase activity, to solve the side effects of allergic reactions, suggesting that MAP-2 has the potential to become a novel and effective inhibitor of α-glucosidase with fewer side effects.
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