Food Frontiers
·
2024
·
IF 7.4
Ziyi Han,Leyu Wang,Panjie Sun,Mengxin Huang,Fei Yu,Junsheng Liu,Yuanyuan Wu,Puming He,Youying Tu,Bo Li
Hyperglycemia and diabetes are common metabolic disorders. It is considered a safe and effective strategy to screen active ingredients from food and herbs for controlling blood sugar levels. Quinic acid (QA) is a natural polyphenolic acid with various health-promoting properties. In this study, QA was found to exhibit a potent inhibitory effect on α-glucosidase activity, with a half maximal inhibitory concentration (IC 50 ) of 5.46 mM. This inhibitory property surpassed that of three common organic acids including gallic acid, malic acid, and citric acid. A combination of 25% acarbose (0.5 mM) and 75% QA (5 mM) (v/v) exhibited synergistic inhibition of α-glucosidase activity. Enzyme kinetics, fluorescence spectra, and molecular docking analyses indicated that QA acted as an uncompetitive inhibitor of α-glucosidase, with hydrogen bonds playing a key role in the intermolecular interactions. Moreover, QA was found to effectively inhibit three major nonenzymatic glycation products including advanced glycosylation end products (AGEs), fructosamine, and α-dicarbonyl in a dose-dependent manner, outperforming the positive control aminoguanidine (AG) within the tested concentration range. Utilizing a Caco-2 cell model, QA demonstrated the ability to inhibit the transmembrane absorption of glucose. This study highlighted QA as a promising food functional factor that had been overlooked in the past, offering potential benefits in improving hyperglycemia, diabetes, and associated complications through the inhibition of α-glucosidase, nonenzymatic glycosylation, and glucose uptake.
研究领域:
食品科学
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分子生物学
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代谢疾病研究
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产品关联
DOI
高影响因子
JOURNAL OF BIOSCIENCE AND BIOENGINEERING
·
2021
·
IF 2.894
Chen Yu,Zi-Yi Yu,Yi-Ting Wen,Wei-Ming Chai,Lin-Jun Wang,Mei-Zhen Lin
In this study, the inhibitory effect and mechanism of omeprazole on α-glucosidase and nonenzymatic glycation were investigated in vitro by using multi-spectroscopic methods and molecular docking . Enzyme kinetic results showed that omeprazole inhibited α-glucosidase in a reversible and noncompetitive manner (IC 50 = 0.595 ± 0.003 mM). The results from fluorescence quenching and thermomechanical analyses signified that omeprazole reduced the fluorescence intensity of α-glucosidase by forming an omeprazole-α-glucosidase complex primarily driven by hydrogen bonds . Molecular docking further confirmed that hydrogen bonds and hydrophobic forces were the major driving forces for omeprazole binding to α-glucosidase. The nonenzymatic glycation assays revealed that omeprazole had a moderate inhibition against the formation of fructosamine , dicarbonyl compounds, and advanced glycation end products (AGEs). This study provides a new inhibitor of both α-glucosidase and nonenzymatic glycation and provides a practicable candidate for treating diabetes and its complications.
研究领域:
药理学
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生物化学
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糖尿病研究
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产品关联
DOI
PubMed
高影响因子
Foods
·
2024
·Vol. 13
·期 8
·1183
·
IF 4.7
Qin Li,Ke Xiao,Chi Yi,Fan Yu,Wenyue Wang,Junhui Rao,Menglin Liu,Lin Zhang,Yang Mu,Chao Wang,Qian Wu,Dongsheng Li,Mengzhou Zhou
Lactobacillus fermentum(L. fermentum) was first evaluated as a potential advanced glycation end-product (AGE) formation inhibitor by establishing a bovine serum albumin (BSA) + glucose (glu) glycation model in the present study. The results showed that the highest inhibition rates of pentosidine and total fluorescent AGEs byL. fermentumwere approximately 51.67% and 77.22%, respectively, which were higher than that of aminoguanidine (AG). Mechanistic analysis showed thatL. fermentumcould capture methylglyoxal and glyoxal, inhibit carbonyl and sulfhydryl oxidation, reduce the binding of glucose and amino groups, increase total phenolic content and antioxidant activity, and release intracellular substances to scavenge free radicals; these abilities were the basis of the antiglycation mechanism ofL. fermentum. In addition,L. fermentumsignificantly prevented conformational changes in proteins during glycation, reduced protein cross-linking by 35.67%, and protected the intrinsic fluorophore. Therefore, the inhibition ofL. fermentumon glycation mainly occurs through antioxidation, the capture of dicarbonyl compounds, and the protection of the BSA structure. These findings collectively suggest thatLactobacillusis an inhibitor of protein glycation and AGE formation and has the potential for nutraceutical applications.
研究领域:
食品科学
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生物化学
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产品关联
DOI
PubMed
高影响因子
RSC Advances
·
2018
·Vol. 8
·期 54
·30957-30965
·
IF 2.936
Yi-Xin Sun,Bing-Bing Shen,Hui-Ying Han,Yuan Lu,Bi-Xian Zhang,Yun-Fei Gao,Bao-Zhong Hu,Xiao-Mei Hu
Lignocellulosic biomass as one of the most abundant and renewable resources has great potential for biofuel production. The complete conversion of biomass to biofuel is achieved through the effective pretreatment process and the following enzyme saccharification. Ionic liquids (ILs) are considered as a green solvent for lignocellulose pretreatment. However, ILs exhibit an inhibitory effect on cellulase activity, leading to a subsequent decrease in the efficiency of saccharification. The screening of new potential IL-tolerant cellulases is important. In the current study, a fungal strain with a relatively high cellulase production was isolated and identified as Penicillium oxalicum HC6. The culture conditions were optimized using corn stover and peptone as the carbon source and nitrogen source at pH 4.0 and 30 °C with an inoculation size of 2% (v/v) for 8 days. It was found that P. oxalicum HC6 exhibited potential salt tolerance with the increase of the enzyme production at a salt concentration of 5.0% (w/v). In addition, high enzyme activities were obtained at pH 4.0–6.0 and 50–65 °C. The crude enzyme from P. oxalicum HC6 with good thermal stability was also stable in the presence of salt and ILs. Good yields of reducing sugar were obtained by the crude enzyme from P. oxalicum HC6 after the saccharification of corn stover that was pretreated by ILs. P. oxalicum HC6 with potentially salt-tolerant and IL-tolerant enzymes has great potential application in the enzymatic saccharification of lignocellulose.
研究领域:
生物技术
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生物化学
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环境科学
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可再生能源
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DOI
PubMed
高影响因子
PROCESS BIOCHEMISTRY
·
2022
·
IF 4.885
Yanzhang Liu,Yongxiao Dong,Xiaoli Pu,Xiaoyan Yin
Diabetic cataract (DC) is a major cause of visual impairment for diabetic patients. There are limited range of drug delivery approaches and pharmacologic interventions available to control the diabetic cataract progressions, specifically the eye drops related non-invasive strategies. The reported studies in diabetic cataract designate that non-enzymatic glycosylation and oxidative damages of the crystalline lens played a vital role in the formation cataract pathogenesis. In the present investigation, we developed a novel combination of anti-oxidant curcumin (CUR) and cerium oxide nanoparticles (CeO 2 NPs) entrapped poly lactic-co-glycolic acid (PLGA) copolymeric nanoformulations (CCNPs) to improve auto-regenerative redox and anti-glycation potential to treat diabetic cataract complications. The analytical methods exhibited successful entrapments of curcumin and CeO 2 NPs into the PLGA formulations under X-ray diffraction pattern (XRD), Fourier-transform infrared (FTIR) spectrum and scanning electron microscope (SEM) observations. We investigated and found that prepared CCNPs nanoformulation could have effective anti-oxidant and anti-glycation potential to protect lens epithelial (HLE-B3) cells by prominent prevention of repetitive reactive oxygen species (ROS) generations. In vivo toxicity analysis results indicated that CCNPs have no any inflammation abnormalities and less Ce ions caring on major organs of rat by subcutaneous (SC) injection procedure. We expecting that this developed approach would provide capable therapeutic potential for the treatment of diabetic cataract.
研究领域:
药学
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纳米技术
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眼科学
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糖尿病研究
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产品关联
DOI
高影响因子
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