Caiye Qu
Current Organizations / Institutes
The organizations/institutes from the scholar's latest article
Caiye Qu has a total of 7 co-authors. Here are the top co-authors by number of shared publications:
- Hui Yu
Hainan Engineering Research Center of Aquatic Resources Efficient Utilization in South China Sea, Key Laboratory of Seafood Processing of Haikou, School of Food Science and Engineering, Hainan University, Haikou 570228, China
1 shared publication - Juan Xiao
Hainan Engineering Research Center of Aquatic Resources Efficient Utilization in South China Sea, Key Laboratory of Seafood Processing of Haikou School of Food Science and Engineering, Hainan University, Haikou 570228, China
1 shared publication - Meiting Xian
Hainan Engineering Research Center of Aquatic Resources Efficient Utilization in South China Sea, Key Laboratory of Seafood Processing of Haikou, School of Food Science and Engineering, Hainan University, Haikou 570228, China
1 shared publication - Pai Peng
Hainan Engineering Research Center of Aquatic Resources Efficient Utilization in South China Sea, Key Laboratory of Seafood Processing of Haikou, School of Food Science and Engineering, Hainan University, Haikou 570228, China
1 shared publication - Shuyi Li
National R&D Center for Se-Rich Agricultural Products, Processing, Hubei Engineering Research Center for Deep Processing of Green, Se-Rich Agricultural Products, School of Modern Industry for Selenium Science and Engineering, Wuhan Polytechnic University, Wuhan 430023, China
1 shared publication - Zhenzhou Zhu
National R&D Center for Se-rich Agricultural Products Processing, Hubei Engineering Research Center for Deep Processing of Green Se-rich Agricultural Products, School of Modern Industry for Selenium Science and Engineering, Wuhan Polytechnic University, Wuhan 430023, China
1 shared publication
Latest Publications
- Open Access
- 9 February 2025
- Published by MDPI AG in Marine Drugs
- Vol. 23 (2) , 75
Preparation of Acetylcholinesterase Inhibitory Peptides from Yellowfin Tuna Pancreas Using Moderate Ultrasound-Assisted Enzymatic Hydrolysis
Bioactive peptides represent a promising therapeutic approach for Alzheimer’s disease (AD) by maintaining cholinergic system homeostasis through the inhibition of acetylcholinesterase (AChE) activity. This study focused on extracting AChE inhibitory peptides from yellowfin tuna pancreas using moderate ultrasound-assisted enzymatic hydrolysis (MUE). Firstly, papain and MUE stood out from five enzymes and four enzymatic hydrolysis methods, respectively, by comparing the degree of hydrolysis and AChE inhibitory activity of different pancreatic protein hydrolysates. Subsequently, the optimal MUE conditions were obtained by single-factor, Plackett–Burman, and response surface methodologies. The pancreatic protein hydrolysate prepared under optimal MUE conditions was then purified by ultrafiltration followed by RP-HPLC, from which a novel AChE inhibitory peptide (LLDF) was identified by LC-MS/MS and virtual screening. LLDF effectively inhibited AChE activity by a competitive inhibition mechanism, with an IC50 of 18.44 ± 0.24 μM. Molecular docking and molecular dynamic simulation revealed that LLDF bound robustly to the active site of AChE via hydrogen bonds. These findings provided a theoretical basis for the valuable use of yellowfin tuna pancreas and introduced a new viewpoint on the potential therapeutic advantages of AChE inhibitory peptides for future AD treatment.
- 9 February 2025
- Published by MDPI AG in Marine Drugs
- Vol. 23 (2) , 75
Open AccessPreparation of Acetylcholinesterase Inhibitory Peptides from Yellowfin Tuna Pancreas Using Moderate Ultrasound-Assisted Enzymatic Hydrolysis
Bioactive peptides represent a promising therapeutic approach for Alzheimer’s disease (AD) by maintaining cholinergic system homeostasis through the inhibition of acetylcholinesterase (AChE) activity. This study focused on extracting AChE inhibitory peptides from yellowfin tuna pancreas using moderate ultrasound-assisted enzymatic hydrolysis (MUE). Firstly, papain and MUE stood out from five enzymes and four enzymatic hydrolysis methods, respectively, by comparing the degree of hydrolysis and AChE inhibitory activity of different pancreatic protein hydrolysates. Subsequently, the optimal MUE conditions were obtained by single-factor, Plackett–Burman, and response surface methodologies. The pancreatic protein hydrolysate prepared under optimal MUE conditions was then purified by ultrafiltration followed by RP-HPLC, from which a novel AChE inhibitory peptide (LLDF) was identified by LC-MS/MS and virtual screening. LLDF effectively inhibited AChE activity by a competitive inhibition mechanism, with an IC50 of 18.44 ± 0.24 μM. Molecular docking and molecular dynamic simulation revealed that LLDF bound robustly to the active site of AChE via hydrogen bonds. These findings provided a theoretical basis for the valuable use of yellowfin tuna pancreas and introduced a new viewpoint on the potential therapeutic advantages of AChE inhibitory peptides for future AD treatment.