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Molecules (Basel, Switzerland) Dec 2023Diabetes mellitus (DM) is considered one of the major health diseases worldwide, one that requires immediate alternatives to allow treatments for DM to be more effective... (Review)
Review
Chia ( L.), a Pre-Hispanic Food in the Treatment of Diabetes Mellitus: Hypoglycemic, Antioxidant, Anti-Inflammatory, and Inhibitory Properties of α-Glucosidase and α-Amylase, and in the Prevention of Cardiovascular Disease.
Diabetes mellitus (DM) is considered one of the major health diseases worldwide, one that requires immediate alternatives to allow treatments for DM to be more effective and less costly for patients and also for health-care systems. Recent approaches propose treatments for DM based on that; in addition to focusing on reducing hyperglycemia, they also consider multitargets, as in the case of plants. Among these, we find the plant known as chia to be highlighted, a crop native to Mexico and one cultivated in Mesoamerica from pre-Hispanic times. The present work contributes to the review of the antidiabetic effects of chia for the treatment of DM. The antidiabetic effects of chia are effective in different mechanisms involved in the complex pathogenesis of DM, including hypoglycemic, antioxidant, and anti-inflammatory mechanisms, and the inhibition of the enzymes α-glucosidase and α-amylase, as well as in the prevention of the risk of cardiovascular disease. The tests reviewed included 16 in vivo assays on rodent models, 13 clinical trials, and 4 in vitro tests. Furthermore, chia represents advantages over other natural products due to its availability and its acceptance and, in addition, as a component of the daily diet worldwide, especially due to its omega-3 fatty acids and its high concentration of dietary fiber. Thus, chia in the present work represents a source of antidiabetic agents that would perhaps be useful in novel clinical treatments.
Topics: Humans; alpha-Amylases; alpha-Glucosidases; Antioxidants; Cardiovascular Diseases; Diabetes Mellitus; Hypoglycemic Agents; Salvia; Salvia hispanica; Seeds
PubMed: 38138560
DOI: 10.3390/molecules28248069 -
Current Opinion in Gastroenterology Sep 2023Serum levels of amylase and lipase can be elevated in nonpancreatic conditions that may or may not be associated with abdominal pain. This leads to a large proportion of... (Review)
Review
PURPOSE OF REVIEW
Serum levels of amylase and lipase can be elevated in nonpancreatic conditions that may or may not be associated with abdominal pain. This leads to a large proportion of patients being falsely labeled as having acute pancreatitis. In this review, we aim to summarize the existing evidence on pancreatic enzyme elevation in various pancreatic and nonpancreatic conditions and its practical implications in clinical practice and healthcare.
RECENT FINDINGS
Serum amylase and lipase levels are not specific for pancreatitis. Attempts have been made to validate newer biomarkers including pancreatic elastase, serum trypsin, urinary trypsinogen-activated peptide, phospholipase A2, carboxypeptidase B, activated peptide of carboxypeptidase B, the trypsin 2 alpha 1 activation complex, and circulating cell-free DNA for the diagnosis of acute pancreatitis.
SUMMARY
Serum lipase levels can be elevated in many intra-abdominal inflammatory conditions. Although more sensitive and specific than amylase, serum lipase levels are not sufficient to diagnose acute pancreatitis in patients with abdominal pain. There is a need to increase stress on radiological evidence as well increase cut-off levels of enzyme elevation for a more accurate diagnosis of acute pancreatitis.
Topics: Humans; Pancreatitis; Trypsin; Acute Disease; Carboxypeptidase B; Amylases; Lipase; Abdominal Pain; Peptides
PubMed: 37389417
DOI: 10.1097/MOG.0000000000000961 -
The Protein Journal Oct 2023Amaranthaceae α-amylase inhibitors (AAIs) are knottin-type proteins with selective inhibitory potential against coleopteran α-amylases. Their small size and remarkable...
Amaranthaceae α-amylase inhibitors (AAIs) are knottin-type proteins with selective inhibitory potential against coleopteran α-amylases. Their small size and remarkable stability make them exciting molecules for protein engineering to achieve superior selectivity and efficacy. In this report, we have designed a set of AAI pro- and mature peptides chimeras. Based on in silico analysis, stable AAI chimeras having a stronger affinity with target amylases were selected for characterization. In vitro studies validated that chimera of the propeptide from Chenopodium quinoa α-AI and mature peptide from Beta vulgaris α-AI possess 3, 7.6, and 4.26 fold higher inhibition potential than parental counterparts. Importantly, recombinant AAI chimera retained specificity towards target coleopteran α-amylases. In addition, to improve the inhibitory potential of AAI, we performed in silico site-saturation mutagenesis. Computational analysis followed by experimental data showed that substituting Asparagine at the 6th position with Methionine had a remarkable increase in the specific inhibition potential of Amaranthus hypochondriacus α-AI. These results provide structural-functional insights into the vitality of AAI propeptide and a potential hotspot for mutagenesis to enhance the AAI activity. Our investigation will be a toolkit for AAI's optimization and functional differentiation for future biotechnological applications.
Topics: Amaranthaceae; Methionine; Mutagenesis; Protein Engineering; alpha-Amylases
PubMed: 37598128
DOI: 10.1007/s10930-023-10148-y -
Future Medicinal Chemistry 2024The objective of the present investigation was to design and synthesize new heterocyclic hybrids comprising benzothiazole and indenopyrazolone pharmacophoric units in a...
The objective of the present investigation was to design and synthesize new heterocyclic hybrids comprising benzothiazole and indenopyrazolone pharmacophoric units in a single molecular framework targeting α-amylase and α-glucosidase enzymatic inhibition. 20 new benzothiazole-appended indenopyrazoles, , were synthesized in good yields under environment-friendly conditions via cycloaddition reaction, and assessed for antidiabetic activity against α-amylase and α-glucosidase, using acarbose as the standard reference. Among all the hydroxypyrazolones, and showed the best inhibition against α-amylase and α-glucosidase, which finds support from molecular docking and dynamic studies. Compounds and have been identified as promising antidiabetic agents against α-amylase and α-glucosidase and could be considered valuable leads for further optimization of antidiabetic agents.
Topics: alpha-Glucosidases; Benzothiazoles; alpha-Amylases; Molecular Docking Simulation; Glycoside Hydrolase Inhibitors; Hypoglycemic Agents; Humans; Pyrazoles; Structure-Activity Relationship; Molecular Structure; Enzyme Inhibitors
PubMed: 38910576
DOI: 10.4155/fmc-2023-0384 -
Biotechnology and Bioengineering Aug 2023Amylases are biologically active enzymes that can hydrolyze starch to produce dextrin, glucose, maltose, and oligosaccharides. The amylases contribute approximately 30%... (Review)
Review
Amylases are biologically active enzymes that can hydrolyze starch to produce dextrin, glucose, maltose, and oligosaccharides. The amylases contribute approximately 30% to the global industrial enzyme market. The globally produced amylases are widely used in textile, biofuel, starch processing, food, bioremediation of environmental pollutants, pulp, and paper, clinical, and fermentation industries. The purpose of this review article is to summarize recent trends and aspects of α-amylases, classification, microbial production sources, biosynthesis and production methods, and its broad-spectrum applications for industrial purposes, which will depict the latest trends in α-amylases production. In the present article, we have comprehensively compared the biodiversity of α-amylases in different model organisms ranging from archaea to eukaryotes using in silico structural analysis tools. The detailed comparative analysis: regarding their structure, function, cofactor, signal peptide, and catalytic domain along with their catalytic residues of α-amylases in 16 model organisms were discussed in this paper. The comparative studies on alpha (α) amylases' secondary and tertiary structures, multiple sequence alignment, transmembrane helices, physiochemical properties, and their phylogenetic analysis in model organisms were briefly studied. This review has documented the recent trends and future perspectives of industrially important novel thermophilic α-amylases. In conclusion, this review sheds light on the current understanding and prospects of α-amylase research, highlighting its importance as a versatile enzyme with numerous applications and emphasizing the need for further exploration and innovation in this field.
Topics: alpha-Amylases; Phylogeny; Amylases; Catalysis; Starch
PubMed: 37475649
DOI: 10.1002/bit.28504 -
Journal of Biomolecular Structure &... Dec 2023In this exploration, we assessed the antihyperglycaemic properties of methanol extract of flowers of (MeT) against α-glucosidase, α-amylase and aldose reductase...
In this exploration, we assessed the antihyperglycaemic properties of methanol extract of flowers of (MeT) against α-glucosidase, α-amylase and aldose reductase enzymes for the effective management of postprandial hyperglycemia. Hyperglycemia occurs when the body lacks enough insulin or is unable to correctly utilize it. MeT inhibited both the carbohydrate digestive enzymes (α-glucosidase and α-amylase) and aldose reductase, which are vital for the therapeutic control of postprandial hyperglycaemia. MeT was also found to have significant antioxidant activity. Using several spectroscopic approaches, the primary active component found in MeT was identified as gallic acid. With low Ki values, gallic acid significantly inhibited α-glucosidase (30.86 µg/mL) and α-amylase (6.50 µg/mL). Also, MeT and gallic acid both inhibited aldose reductase effectively, corresponding to an IC value of 3.31 and 3.05 µg/mL. Our findings imply that the presence of polyphenol compounds (identified via HPLC analysis) is more likely to be responsible for the antihyperglycaemic role exhibited by MeT via the inhibition of α-glucosidase and the polyol pathway. Further, gallic acid interacted with the key residues of the active sites of α-glucosidase (-6.4 kcal/mol), α-amylase (-5.8 kcal/mol) and aldose reductase (-5.8 kcal/mol) as observed in the protein-ligand docking. It was also predicted that gallic acid was stable inside the binding pockets of the target enzymes during molecular dynamics simulation. Overall, gallic acid derived from MeT via bioassay-guided isolation emerges as a natural antidiabetic drug and can be taken into and clinical studies shortly.Communicated by Ramaswamy H. Sarma.
Topics: Gallic Acid; alpha-Glucosidases; alpha-Amylases; Aldehyde Reductase; Hypoglycemic Agents; Acanthaceae; Molecular Docking Simulation
PubMed: 36533383
DOI: 10.1080/07391102.2022.2156923 -
Applied Biochemistry and Biotechnology Dec 2023Enzymes from haloalkaliphilic microorganisms have recently focused attention on their potential and suitability in various applications. In this study, the growth and...
Enzymes from haloalkaliphilic microorganisms have recently focused attention on their potential and suitability in various applications. In this study, the growth and production of extracellular amylases in the marine actinomycetes, using kitchen waste as the raw starch source, have been investigated. Actinobacteria were isolated from the seawater of the Kachhighadi Coast near Dwarika, Gujarat. Seven Actinobacterial isolates of pre-monsoon, monsoon, and post-monsoon seasons belonging to different strains of Nocardiopsis genera were screened and selected for amylase production. The amylase production was initially assessed on the solid media supplemented with the extracts of different fruits and vegetable peels as a substrate by agar plate assay. The strains Kh-2(13), Kh-2(1), and Kh-3(12) produced maximum amylase with potato peel as a substrate, while no significant differences were found with the media containing other peels. Nevertheless, all strains produced amylases at a significant level with other raw substrates as well. For the optimization of the growth and enzyme production, the selected two isolates Kh-2(13) and Kh-3(12) of the monsoon and winter seasons were cultivated in a liquid medium under the submerged fermentation conditions, with potato peel as a substrate. In both organisms, the optimum amylase production was observed in the stationary phase of growth. For amylase production, the effect of different physical and chemical parameters was evaluated. The optimum growth and amylase production was achieved in 2% inoculum size, at pH 8.0, 28℃, and 5% salt concentration. On the basis of the amylase production index (API) (a ratio of the amylase units and cell growth), both isolates produced significant amylase with the only extract of potato peels, without any other supplements. The trends further indicated that while additional complex sources, such as yeast extract and peptone can enhance the cell growth of the actinobacteria, the amylase production remained unaltered. The study projects the significance of waste raw materials for the production of enzymes in extremophilic microorganisms.
Topics: alpha-Amylases; Vegetables; Fruit; Actinobacteria; Amylases; Starch; Fermentation; Bacteria; Hydrogen-Ion Concentration; Temperature
PubMed: 37067678
DOI: 10.1007/s12010-023-04422-z -
Marine Drugs Aug 2023Marine-derived fungi are renowned as a source of astonishingly significant and synthetically appealing metabolites that are proven as new lead chemicals for chemical,... (Review)
Review
Marine-derived fungi are renowned as a source of astonishingly significant and synthetically appealing metabolites that are proven as new lead chemicals for chemical, pharmaceutical, and agricultural fields. is a saprotrophic, ubiquitous, and halophilic fungus that is commonly found in different marine ecosystems. This fungus can cause aspergillosis in sea fan corals leading to sea fan mortality with subsequent changes in coral community structure. Interestingly, is a prolific source of distinct and structurally varied metabolites such as alkaloids, xanthones, terpenes, anthraquinones, sterols, diphenyl ethers, pyrones, cyclopentenones, and polyketides with a range of bioactivities. has capacity to produce various enzymes with marked industrial and biotechnological potential, including α-amylases, lipases, xylanases, cellulases, keratinases, and tannases. Also, this fungus has the capacity for bioremediation as well as the biocatalysis of various chemical reactions. The current work aimed at focusing on the bright side of this fungus. In this review, published studies on isolated metabolites from , including their structures, biological functions, and biosynthesis, as well as the biotechnological and industrial significance of this fungus, were highlighted. More than 245 compounds were described in the current review with 134 references published within the period from 1975 to June 2023.
Topics: Animals; Ecosystem; Aspergillus; Anthozoa; Anthraquinones
PubMed: 37623723
DOI: 10.3390/md21080441 -
Journal of the Science of Food and... Jan 2024Our previous studies have shown that ultrasound-treated γ-aminobutyric acid (GABA)-rich coffee leaves have higher angiotensin-I-converting enzyme inhibitory activity...
BACKGROUND
Our previous studies have shown that ultrasound-treated γ-aminobutyric acid (GABA)-rich coffee leaves have higher angiotensin-I-converting enzyme inhibitory activity than their untreated counterpart. However, whether they have antidiabetic activity remains unknown. In this study, we aimed to investigate the inhibitory activities of coffee leaf extracts (CLEs) prepared with ultrasound (CLE-U) or without ultrasound (CLE-NU) pretreatment on α-amylase and α-glucosidase. Subsequently, we evaluated the binding interaction between CLE-U and both enzymes using multi-spectroscopic and in silico analyses.
RESULTS
Ultrasound pretreatment increased the inhibitory activities of CLE-U against α-amylase and α-glucosidase by 21.78% and 25.13%, respectively. CLE-U reversibly inhibits both enzymes, with competitive inhibition observed for α-amylase and non-competitive inhibition for α-glucosidase. The static quenching of CLE-U against both enzymes was primarily driven by hydrogen bond and van der Waals interactions. The α-helices of α-amylase and α-glucosidase were increased by 1.8% and 21.3%, respectively. Molecular docking results showed that the key differential compounds, including mangiferin, 5-caffeoylquinic acid, rutin, trigonelline, GABA, caffeine, glutamate, and others, present in coffee leaves interacted with specific amino acid residues located at the active site of α-amylase (ASP197, GLU233, and ASP300). The binding of α-glucosidase and these bioactive components involved amino acid residues, such as PHE1289, PRO1329, and GLU1397, located outside the active site.
CONCLUSION
Ultrasound-treated coffee leaves are potential anti-diabetic substances, capable of preventing diabetes by inhibiting the activities of α-amylase and α-glucosidase, thus delaying starch digestion. Our study provides valuable information to elucidate the possible antidiabetic capacity of coffee leaves through the inhibition of α-amylase and α-glucosidase activities. © 2023 Society of Chemical Industry.
Topics: alpha-Amylases; Coffea; Molecular Docking Simulation; alpha-Glucosidases; Hypoglycemic Agents; Diabetes Mellitus; Plant Extracts; Amino Acids; gamma-Aminobutyric Acid; Glycoside Hydrolase Inhibitors
PubMed: 37515816
DOI: 10.1002/jsfa.12890 -
The Science of the Total Environment Mar 2024Plastic fragments are widely distributed in different environmental media and has recently drawn special attention due to its difficulty in degradation and serious...
Plastic fragments are widely distributed in different environmental media and has recently drawn special attention due to its difficulty in degradation and serious health and environmental problems. Among, nanoplastics (NPs) are smaller in size, larger in surface/volume ratio, and more likely to easily adsorb ambient pollutants than macro plastic particles. Moreover, NPs can be easily absorbed by wide variety of organisms and accumulate in multiple tissues/organs and cells, thus posing a more serious threat to living organisms. Alpha-amylase (α-amylase) is a hydrolase, which can be derived from various sources such as animals, plants, and microorganisms. Currently, no studies have concentrated on the binding of NPs with α-amylase and their interaction mechanisms by employing a multidimensional strategy. Hence, we explored the interaction mechanisms of polystyrene nanoplastics (PS-NPs) with α-amylase by means of multispectral analysis, in vitro enzymatic activity analysis, and molecular simulation techniques under in vitro conditions. The findings showed that PS-NPs had the capability to bind with the intrinsic fluorescence chromophores, leading to fluorescence changes of these specific amino acids. This interaction also caused the alterations in the micro-environment of the fluorophore residues mainly tryptophan (TRP) and tyrosine (TYR) residues of α-amylase. PS-NPs interaction promoted the unfolding and partial expansion of polypeptide chains and the loosening of protein skeletons, and destroyed the secondary structure (increased random coil contents and decreased α-helical contents) of this protein, forming a larger particle size of the PS-NPs-α-amylase complex. Moreover, the enzymatic activity of α-amylase in vitro was found to be inhibited in a concentration dependent manner, thereby impairing its physiological functions. Further molecular simulation found that PS-NPs had a higher tendency to bind to the active site of α-amylase, which is the cause for its structural and functional changes. Additionally, the hydrophobic force played a major role in mediating the binding interactions between PS-NPs and α-amylase. Taken together, our study indicated that PS-NPs interaction can initiate the abnormal physiological functions of α-amylase through PS-NPs-induced structural and conformational alternations.
Topics: Animals; Polystyrenes; Microplastics; alpha-Amylases; Nanoparticles; Water Pollutants, Chemical
PubMed: 38242479
DOI: 10.1016/j.scitotenv.2024.170036