Affinity screening of potential anti-obesity and anti-diabetic component from pomegranate peel by co-immobilization of lipase and α-amylase using carbon nanotube and hydrogel. (March 2023)

• Record Type: Journal Article
• Authors: Wang, Shuai; Liu, Shuo; Liu, Chang; Tang, Shanshan; Gu, Dongyu; Tian, Jing; Yang, Yi
• Is Part Of: Process biochemistry. Volume 126(2023)
• Page Start: 51
• Page End: 60
• Publication Date: 2023-03
• Subjects: Co-immbilization -- Multi-walled carbon nanotube -- Hydrogel -- Pomegranate peel -- Ligand fishing -- Molecular docking; Biochemical engineering -- Periodicals; Biotechnology -- Periodicals; Biochemistry -- periodicals; Biotechnology -- periodicals; Chemical Engineering -- periodicals; Génie biochimique -- Périodiques; Biotechnologie -- Périodiques; Biochemical engineering; Biotechnology; Periodicals; 660.63
• DOI: 10.1016/j.procbio.2023.01.002
• Languages: English
• ISSNs: 1359-5113

Abstract

Abstract: Lipase and α-amylase play a very important role in the screening of anti-obesity and anti-diabetic drugs. Here, bienzyme microspheres containing lipase and α-amylase were synthesized for simultaneous affinity screening of anti-obesity and anti-diabetic component from pomegranate peel. Lipase was immobilized by functionalized multi-walled carbon nanotube (MWCNT) coated with polyamide dendrimers to obtain MWCNT-lipase. Subsequently, MWCNT-lipase and α-amylase was encapsulated by sodium alginate (SA) hydrogel microspheres to form MWCNT/SA-bienzymes. Under the optimized reaction conditions, the immobilization rate of lipase and α-amylase was 65.16% and 95.79%, and the activities were 85.76% and 88.11% of free enzymes, respectively. Moreover, the enzyme activity conditions of MWCNT/SA-bienzymes were also optimized. The MWCNT/SA-bienzymes were more stable than two free enzymes at room temperature and can be reused. More importantly, in application, a compound (ellagic acid) was selectively screened from pomegranate peel extract by MWCNT/SA-bienzymes. In vitro activity determination confirmed that ellagic acid with IC50 of 369.83 ± 11.75 μg/mL and 672.81 ± 18.55 μg/mL can interact with two enzymes through non-competitive inhibition. The molecular docking showed that ellagic acid bound with α-amylase and lipase through hydrogen bonds, van der Waals forces, etc, resulting in the binding energies of − 8.54 kcal/mol and − 6.87 kcal/mol, respectively. Graphical Abstract: ga1 Highlights: An effective strategy was proposed for screening of bifunctional inhibitor. Bienzyme microspheres containing lipase and α-amylase were synthesized. Multi-walled carbon nanotubes and hydrogels were used as carriers. Ellagic acid has the dual function of inhibiting lipase and α-amylase.