Starch-digesting product analysis based on the hydrophilic interaction liquid chromatography coupled mass spectrometry method to evaluate the inhibition of flavonoids on pancreatic α-amylase

Xiao, Zhengcao; Hou, Xuexin; Zhang, Ting; Yuan, Yahong; Xiao, Jianbo; Song, Wei; Yue, Tianli

doi:10.1016/j.foodchem.2021.131175

Cited by 8 publications

(21 citation statements)

References 31 publications

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“…This difference in binding may be because the structural end groups of α-ZAL and β-ZOL are hydroxyl groups, but the structural end groups of ZEN and ZAN are carbonyl groups. Previous studies have shown that the presence of hydroxyl radicals may affect the biological activity of enzymes [ 28 , 29 , 30 ]. The hydroxyl structure may affect the ability of FSZ to bind and degrade α-ZAL and β-ZOL.…”

Section: Resultsmentioning

confidence: 99%

Isolation and Mechanistic Characterization of a Novel Zearalenone-Degrading Enzyme

et al. 2022

Foods

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Zearalenone (ZEN) and its derivatives pose a serious threat to global food quality and animal health. The use of enzymes to degrade mycotoxins has become a popular method to counter this threat. In this study, Aspergillus niger ZEN-S-FS10 extracellular enzyme solution with ZEN-degrading effect was separated and purified to prepare the biological enzyme, FSZ, that can degrade ZEN. The degradation rate of FSZ to ZEN was 75–80% (pH = 7.0, 28 °C). FSZ can function in a temperature range of 28–38 °C and pH range of 2.0–7.0 and can also degrade ZEN derivatives (α-ZAL, β-ZOL, and ZAN). According to the enzyme kinetics fitting, ZEN has a high degradation rate. FSZ can degrade ZEN in real samples of corn flour. FSZ can be obtained stably and repeatedly from the original strain. One ZEN degradation product was isolated: FSZ−P(C18H26O4), with a relative molecular weight of 306.18 g/mol. Amino-acid-sequencing analysis revealed that FSZ is a novel enzyme (homology < 10%). According to the results of molecular docking, ZEN and ZAN can utilize their end-terminal carbonyl groups to bind FSZ residues PHE307, THR55, and GLU129 for a high-degradation rate. However, α-ZAL and β-ZOL instead contain hydroxyl groups that would prevent binding to GLU129; thus, the degradation rate is low for these derivatives.

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Section: Resultsmentioning

confidence: 99%

Isolation and Mechanistic Characterization of a Novel Zearalenone-Degrading Enzyme

et al. 2022

Foods

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“…15 out of 25 recorded findings 69,111,112,114,117,118,120,123,124,[127][128][129][130][131][132] showed stronger activity on α-glucosidase than acarbose, in contrast with the remaining 10 studies, 39,57,58,79,116,[133][134][135][136] making a 6:4 conflict. There was greater unity in the results of α-amylase inhibition, 39,137,138 confirming a moderate but generally weaker activity than acarbose on α-amylase (IC50 ranging from 14.57 µM to 1 mM). On a side note, 5-deoxyluteolin ( 29) is structurally related to luteolin (30) but is more limited in experimental data.…”

Section: Flavonesmentioning

confidence: 83%

“…Pelargonidin (122) was involved in at least two reports for its anti-α-glucosidase and α-amylase capabilities. 138,156 The current evidence shows that pelargonidin could be a potential α-glucosidase and αamylase inhibitor with the IC50 being 0.18 µM and 2.07 µM, respectively. 156 However, in a study reported by Xiao et al, 138 a different inhibitory pattern was observed, with the IC50 of this compound against amylase being 459.15 µM.…”

Section: Anthocyanidins and Anthocyaninsmentioning

confidence: 86%

“…138,156 The current evidence shows that pelargonidin could be a potential α-glucosidase and αamylase inhibitor with the IC50 being 0.18 µM and 2.07 µM, respectively. 156 However, in a study reported by Xiao et al, 138 a different inhibitory pattern was observed, with the IC50 of this compound against amylase being 459.15 µM. Such conflict could stem from the difference in the method used in the in vitro experiments.…”

Section: Anthocyanidins and Anthocyaninsmentioning

confidence: 86%

“…Quercetin (68), which has been the subject of 75 articles, has garnered the most attention of all the flavonol aglycones, followed by kaempferol (69) and myricetin (70). , competitive 118,135,194 18 studies 15,33,39,46,53,137,138,147,170,182,184,191,193 Otherwise, compared to the control drug in the same condition, this flavonol exhibited a weak α-amylase inhibitory effect, 15,33,39,53,137,138,147,150,170,182,191,193,206,208 with the pIC50 being 4.07 (3.26-4.83). The mechanism underlying the inhibition of both enzymes remained controversial, which was documented to be in a mixed, 147,171,177,182,187,188,200 or competitive manner.…”

Section: Flavonolsmentioning

confidence: 92%

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Flavonoids as dual-target inhibitors against α-glucosidase and α-amylase: a systematic review of in vitro studies

Lam,

Tran,

Pham

et al. 2023

Preprint

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Diabetes mellitus remains a major global health burden and great attention is directed at natural therapeutics. This systematic review aimed to evaluate the potential of flavonoids as antidiabetic agents through their ability to inhibit α-amylase and α-glucosidase, two key starch digestive enzymes. Six scientific databases were queried up until August 21, 2022, for in vitro studies reporting the IC50 results of purified flavonoids on α-amylase or α-glucosidase, along with the respective data of acarbose control. A total of 339 articles were assessed as eligible and subjected to the data extraction process, resulting in 1643 retrieved structures, 177 compounds of which showed both inhibitions against α-amylase and α-glucosidase. Quality assessment was conducted following a modified CONSORT checklist. The structureactivity relationships revealed that a double bond C2=C3 and a keto group C4=O is essential for simultaneous inhibition. The hydroxyl group at C3 is favourable for α-glucosidase inhibition but detrimental to the effect against α-amylase. Further notable features which affect α-glucosidase and α-amylase inhibition were also discussed. Several limitations were considered, including the inconsistency among included studies, language restriction, and the contemporaneity of the review. In conclusion, the systematic review has summarized some crucial findings in the investigation of flavonoids as dual-target inhibitors against α-glucosidase and α-amylase and proposed several orientations for future research.

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Flavonoids as dual-target inhibitors against α-glucosidase and α-amylase: a systematic review of in vitro studies

Lam,

Tran,

Pham

et al. 2024

Nat. Prod. Bioprospect.

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Diabetes mellitus remains a major global health issue, and great attention is directed at natural therapeutics. This systematic review aimed to assess the potential of flavonoids as antidiabetic agents by investigating their inhibitory effects on α-glucosidase and α-amylase, two key enzymes involved in starch digestion. Six scientific databases (PubMed, Virtual Health Library, EMBASE, SCOPUS, Web of Science, and WHO Global Index Medicus) were searched until August 21, 2022, for in vitro studies reporting IC50 values of purified flavonoids on α-amylase and α-glucosidase, along with corresponding data for acarbose as a positive control. A total of 339 eligible articles were analyzed, resulting in the retrieval of 1643 flavonoid structures. These structures were rigorously standardized and curated, yielding 974 unique compounds, among which 177 flavonoids exhibited inhibition of both α-glucosidase and α-amylase are presented. Quality assessment utilizing a modified CONSORT checklist and structure–activity relationship (SAR) analysis were performed, revealing crucial features for the simultaneous inhibition of flavonoids against both enzymes. Moreover, the review also addressed several limitations in the current research landscape and proposed potential solutions. The curated datasets are available online at https://github.com/MedChemUMP/FDIGA. Graphical Abstract

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Starch-digesting product analysis based on the hydrophilic interaction liquid chromatography coupled mass spectrometry method to evaluate the inhibition of flavonoids on pancreatic α-amylase

Cited by 8 publications

References 31 publications

Isolation and Mechanistic Characterization of a Novel Zearalenone-Degrading Enzyme

Isolation and Mechanistic Characterization of a Novel Zearalenone-Degrading Enzyme

Flavonoids as dual-target inhibitors against α-glucosidase and α-amylase: a systematic review of in vitro studies

Flavonoids as dual-target inhibitors against α-glucosidase and α-amylase: a systematic review of in vitro studies

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