Molecular insight on the binding of monascin to bovine serum albumin (BSA) and its effect on antioxidant characteristics of monascin

Wu, Shu-Fen; Wang, Xiaochan; Bao, Yuxin; Zhang, Chuanying; Liu, Huanhuan; Li, Zhenjing; Chen, Mianhua; Wang, Changlu; Guo, Qingbin; Peng, Xin

doi:10.1016/j.foodchem.2020.126228

Cited by 41 publications

(24 citation statements)

References 35 publications

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“…From Table S3, it could be found that an obvious reduction in the fluorescence intensity of peak 1 (for α-amylase, decreased by 28.65%; for α-glucosidase, decreased by 32.43%) was observed, and a red shift in the peak position was recorded (for the α-amylase–silibinin system, 3 nm; for the α-glucosidase–silibinin system, 4 nm) when silibinin was added into the enzyme solution. These results indicated that some conformational and microenvironmental alterations of α-amylase/α-glucosidase appeared upon binding with silibinin, which was in line with the analysis of synchronous fluorescence spectra …”

Section: Resultssupporting

confidence: 83%

“…These results indicated that some conformational and microenvironmental alterations of α-amylase/αglucosidase appeared upon binding with silibinin, which was in line with the analysis of synchronous fluorescence spectra. 57 UV−Vis Absorption Spectra. Figure 6A,B exhibits the UV−vis absorption spectra of α-amylase/α-glucosidase without and with silibinin.…”

Section: ■ Results and Discussionmentioning

confidence: 99%

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Inhibition Mechanism of α-Amylase/α-Glucosidase by Silibinin, Its Synergism with Acarbose, and the Effect of Milk Proteins

Yang

Wang

et al. 2021

J. Agric. Food Chem.

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As a natural flavonolignan, silibinin is reported to possess multiple biological activities, while the inhibitory potential of silibinin on carbohydrate-hydrolyzing enzymes is still unclear. Therefore, in this study, the inhibitory effect and underlying mechanism of silibinin against α-amylase/α-glucosidase were investigated. The results indicated that silibinin showed a strong inhibitory efficiency against α-amylase/α-glucosidase in noncompetitive manners and exhibited synergistic inhibition against αglucosidase with acarbose. However, interestingly, the inhibitory effect of silibinin was significantly hindered in various milk proteinrich environments, but this phenomenon disappeared after simulated gastrointestinal digestion of milk proteins in vitro. Furthermore, silibinin could combine with the inactive site of α-amylase/α-glucosidase and change the microenvironment and secondary structure of the enzymes, thereby influencing the catalytic efficiency of enzymes. This research suggested that silibinin could be used as a novel carbohydrate-hydrolyzing enzyme inhibitor, and milk beverages rich in silibinin had the potential for further application in antidiabetic dietary or medicine.

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Section: Resultssupporting

confidence: 83%

Section: ■ Results and Discussionmentioning

confidence: 99%

Inhibition Mechanism of α-Amylase/α-Glucosidase by Silibinin, Its Synergism with Acarbose, and the Effect of Milk Proteins

Yang

Wang

et al. 2021

J. Agric. Food Chem.

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“…The serum concentrations of ROS and RNS were not measured although ROS and RNS levels are closely associated with oxidative stress. Albumin is a very abundant and important circulating antioxidant with ligand binding and strong DPPH (1,1-diphenyl-2-picrylhydrazyl) radical scavenging activity properties [ 68 , 69 ]. However, serum albumin was not measured in the present experiment.…”

Section: Discussionmentioning

confidence: 99%

Saikosaponin A-Induced Gut Microbiota Changes Attenuate Severe Acute Pancreatitis through the Activation of Keap1/Nrf2-ARE Antioxidant Signaling

Han

et al. 2020

Oxidative Medicine and Cellular Longevity

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Objective. Severe acute pancreatitis (SAP) is a serious and life-threatening disease associated with multiple organ failure and a high mortality rate and is accompanied by distinct oxidative stress and inflammatory responses. Saikosaponin A has strong antioxidant properties and can affect the composition of gut microbiota. We sought to determine the effects of Saikosaponin A interventions on SAP by investigating the changes of gut microbiota and related antioxidant signaling. Methods. A SAP model was established in Sprague-Dawley (SD) rats through the injection of sodium taurocholate into the biliopancreatic duct and confirmed by elevated levels of serum lipase and amylase. The model was fed a standard diet either with saline solution or with Saikosaponin A. Fecal microbiota transplantation (FMT) from Saikosaponin A-induced rats into the rat model was performed to test the effects of gut microbiota. The composition of gut microbiota was analyzed by using 16S rRNA gene sequencing. We measured apoptotic status, inflammatory biomarkers, and Keap1-Nrf2-ARE ((Kelch-like ECH-associated protein 1) nuclear factor erythroid 2-related factor 2-antioxidant response element) antioxidant signaling. Results. Saikosaponin A intervention attenuated SAP lesions and reduced the levels of serum amylase and lipase, oxidative stress, and inflammatory responses by reducing pathological scores and affecting the serum level of oxidative and inflammatory factors. Meanwhile, the expression of Keap1-Nrf2-ARE was increased. Saikosaponin A intervention improved microbiota composition by increasing the relative abundance of Lactobacillus and Prevotella species. FMT resulted in similar results as those caused by the Saikosaponin A intervention, suggesting Saikosaponin A may exert its function via the improvement of gut microbiota composition. Conclusions. Saikosaponin A-induced gut microbiota changes attenuate SAP progression in the rat model and may be a potential natural drug for adjuvant treatment of SAP. Further work is needed to clear up the points.

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“…40 , the lowest MW BBP-24 showed the lowest IC 50 indicating the highest inhibitory effect of α-glucosidase activity. Dou et al (2019) analysed the decrease in fluorescent intensity (fluorescent quenching) of α-glucosidase with increasing concentration of BBP and its degraded compounds based on fluorescence resonance energy transfer (FRET) method ( Kandagal et al, 2006 ; Wu et al, 2020 ). Dou et al (2019) found that the binding affinity and binding site number of inhibitors (BBP) to α-glucosidase were affected by the molar mass of BBP which was in line with Fig.…”

Section: Digestion – From High To Lower Molar Massmentioning

confidence: 99%

Molar mass effect in food and health

Nishinari

Fang

2021

Food Hydrocolloids

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It is demanded to supply foods with good quality for all the humans. With the advent of aging society, palatable and healthy foods are required to improve the quality of life and reduce the burden of finance for medical expenditure. Food hydrocolloids can contribute to this demand by versatile functions such as thickening, gelling, stabilising, and emulsifying, controlling texture and flavour release in food processing. Molar mass effects on viscosity and diffusion in liquid foods, and on mechanical and other physical properties of solid and semi-solid foods and films are overviewed. In these functions, the molar mass is one of the key factors, and therefore, the effects of molar mass on various health problems related to noncommunicable diseases or symptoms such as cancer, hyperlipidemia, hyperglycemia, constipation, high blood pressure, knee pain, osteoporosis, cystic fibrosis and dysphagia are described. Understanding these problems only from the viewpoint of molar mass is limited since other structural characteristics, conformation, branching, blockiness in copolymers such as pectin and alginate, degree of substitution as well as the position of the substituents are sometimes the determining factor rather than the molar mass. Nevertheless, comparison of different behaviours and functions in different polymers from the viewpoint of molar mass is expected to be useful to find a common characteristics, which may be helpful to understand the mechanism in other problems.

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Molecular insight on the binding of monascin to bovine serum albumin (BSA) and its effect on antioxidant characteristics of monascin

Cited by 41 publications

References 35 publications

Inhibition Mechanism of α-Amylase/α-Glucosidase by Silibinin, Its Synergism with Acarbose, and the Effect of Milk Proteins

Inhibition Mechanism of α-Amylase/α-Glucosidase by Silibinin, Its Synergism with Acarbose, and the Effect of Milk Proteins

Saikosaponin A-Induced Gut Microbiota Changes Attenuate Severe Acute Pancreatitis through the Activation of Keap1/Nrf2-ARE Antioxidant Signaling

Molar mass effect in food and health

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