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[PMID]:29370193
[Au] Autor:Kalita D; Holm DG; LaBarbera DV; Petrash JM; Jayanty SS
[Ad] Endereço:San Luis Valley Research Center, Department of Horticulture and Landscape Architecture, Colorado State University, Center, United States of America.
[Ti] Título:Inhibition of α-glucosidase, α-amylase, and aldose reductase by potato polyphenolic compounds.
[So] Source:PLoS One;13(1):e0191025, 2018.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Diabetes mellitus is a chronic disease that is becoming a serious global health problem. Diabetes has been considered to be one of the major risks of cataract and retinopathy. Synthetic and natural product inhibitors of carbohydrate degrading enzymes are able to reduce type 2 diabetes and its complications. For a long time, potatoes have been portrayed as unhealthy for diabetic patients by some nutritionist due to their high starch content. However, purple and red potato cultivars have received considerable attention from consumers because they have high levels of polyphenolic compounds that have potent antioxidant activities. In this study, we screened the total phenolics (TP) and total anthocyanins (TA) and analyzed the phenolic and anthocyanin compounds in selected potato cultivars and advanced selections with distinct flesh colors (purple, red, yellow and white). Purple and red potato cultivars had higher levels of TP and TA than tubers with other flesh colors. Chlorogenic acid is the predominant phenolic acid, and major anthocyanin is composed of the derivatives of petunidin, peonidin, malvidin and pelargonidin. We tested the potential inhibitory effect of potato extracts on the activities of α-amylase and α-glucosidase, which were targeted to develop antidiabetic therapeutic agents. We also measured inhibitory effect of potato extracts on aldose reductase (AR) which is a key enzyme that has been a major drug target for the development of therapies to treat diabetic complications. Purple flesh tubers extract showed the most effective inhibition of α-amylase, α-glucosidase, and aldose reductase with IC50 values 25, 42, and 32 µg/ml, respectively. Kinetic studies showed that anthocyanins are noncompetitive inhibitors of these enzymes, whereas phenolic acids behaved as mixed inhibitors for α-amylase and α-glucosidase and noncompetitive inhibitors for AR. This study supports the development of a positive and healthful image of potatoes, which is an important issue for consumers.
[Mh] Termos MeSH primário: Aldeído Redutase/antagonistas & inibidores
Inibidores Enzimáticos/farmacologia
Polifenóis/farmacologia
Solanum tuberosum/química
alfa-Amilases/antagonistas & inibidores
alfa-Glucosidases/efeitos dos fármacos
[Mh] Termos MeSH secundário: Antocianinas/análise
Antocianinas/farmacologia
Cromatografia Líquida
Espectrometria de Massas
Polifenóis/análise
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Anthocyanins); 0 (Enzyme Inhibitors); 0 (Polyphenols); EC 1.1.1.21 (Aldehyde Reductase); EC 3.2.1.1 (alpha-Amylases); EC 3.2.1.20 (alpha-Glucosidases)
[Em] Mês de entrada:1803
[Cu] Atualização por classe:180309
[Lr] Data última revisão:
180309
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180126
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0191025


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[PMID]:29441920
[Ti] Título:Pancreatic lipase and -amylase inhibitory activities of plants used in Traditional Chinese Medicine (TCM).
[So] Source:Pharmazie;71(7):420-424, 2016 Jul 07.
[Is] ISSN:0031-7144
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:To find new, plant based drugs for the treatment of obesity and/or diabetes mellitus type 2 through the inhibition of essential digestive enzymes, in vitro tests were carried out on selected plants or fungi with weight-reducing, blood glucose-reducing or related potential, used in Traditional Chinese Medicine (TCM). Aqueous and methanolic extracts of 32 Chinese herbal medicines were assayed for their in vitro inhibitory activity against pancreatic lipase (PL) and α-amylase (PA). PL activity was measured by using an enzymatic in vitro assay based on the hydrolysis kinetics of an oleate ester of 4-methylumbelliferone. For the determination of α-amylase activity an enzyme assay based on the hydrolytic cleavage of a modified starch derivative was used. Our findings have shown that the methanolic extract of Lycopus lucidus Turcz. var. hirtus Regel (Lamiaceae) was a very effective PL inhibitor (IC50: 88.3±4.1 µg/mL). A high anti-amylase activity showed the methanolic extract of Trichosanthes kirilowii Maxim. (Curcurbitaceae, IC50: 248.8±67.3 µg/mL). This work provides a priority list of interesting plants for further study with respect to the treatment of obesity and associated metabolic diseases.
[Mh] Termos MeSH primário: Lipase/antagonistas & inibidores
Pâncreas/enzimologia
Plantas/química
alfa-Amilases/antagonistas & inibidores
[Mh] Termos MeSH secundário: Fungos/química
Hidrólise
Himecromona/química
Cinética
Lycopus/química
Medicina Tradicional Chinesa
Pâncreas/efeitos dos fármacos
Extratos Vegetais/farmacologia
Trichosanthes/química
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Plant Extracts); 3T5NG4Q468 (Hymecromone); EC 3.1.1.3 (Lipase); EC 3.2.1.1 (alpha-Amylases)
[Em] Mês de entrada:1803
[Cu] Atualização por classe:180308
[Lr] Data última revisão:
180308
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180215
[St] Status:MEDLINE
[do] DOI:10.1691/ph.2016.6569


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[PMID]:29250543
[Au] Autor:Li Z; Su L; Duan X; Wu D; Wu J
[Ad] Endereço:State Key Laboratory of Food Science and Technology, Jiangnan University, 1800 Lihu Avenue, Wuxi 214122, China.
[Ti] Título:Efficient Expression of Maltohexaose-Forming -Amylase from in SP3 and Its Use in Maltose Production.
[So] Source:Biomed Res Int;2017:5479762, 2017.
[Is] ISSN:2314-6141
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The maltohexaose-forming, Ca -independent -amylase gene from (AmyMH) was efficiently expressed in SP3. To improve the production of AmyMH in SP3, the temperature and initial pH of culture medium were optimized. In addition, single-factor and response surface methodologies were pursued to optimize culture medium. Addition of proline to the culture medium significantly improved the production of recombinant -amylase in SP3. This improvement may result from improved cellular integrity of recombinant SP3 in existence of proline. Culture medium optimization resulted in an 8-fold improvement in -amylase yield, which reached 1.72 × 10 U·mL . The recombinant -amylase was applied to the production of maltose on a laboratory scale. A maltose content of 90.72%, which could be classified as an extremely high maltose syrup, could be achieved using 15% (m/v) corn starch as the substrate. This study demonstrated that the SP3 expression system was able to produce substantial quantities of recombinant -amylase that has potential application in the starch industry.
[Mh] Termos MeSH primário: Brevibacillus/metabolismo
Geobacillus stearothermophilus/enzimologia
Maltose/metabolismo
Oligossacarídeos/metabolismo
alfa-Amilases/metabolismo
[Mh] Termos MeSH secundário: Proteínas de Bactérias/genética
Proteínas de Bactérias/metabolismo
Reatores Biológicos
Brevibacillus/genética
Meios de Cultura
Fermentação
Geobacillus stearothermophilus/genética
Glucose/metabolismo
Maltose/análise
Proteínas Recombinantes/genética
Proteínas Recombinantes/metabolismo
alfa-Amilases/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Culture Media); 0 (Oligosaccharides); 0 (Recombinant Proteins); 34620-77-4 (maltohexaose); 69-79-4 (Maltose); EC 3.2.1.1 (alpha-Amylases); IY9XDZ35W2 (Glucose)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180129
[Lr] Data última revisão:
180129
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171219
[St] Status:MEDLINE
[do] DOI:10.1155/2017/5479762


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[PMID]:28448467
[Au] Autor:Araújo JS; Chambó ED; Costa MAPC; Cavalcante da Silva SMP; Lopes de Carvalho CA; M Estevinho L
[Ad] Endereço:Centro de Ciências Agrárias, Ambientais e Biológicas, Universidade Federal do Recôncavo da Bahia, Cruz das Almas 44380-000, Bahia, Brazil. jucilenearaujo15@hotmail.com.
[Ti] Título:Chemical Composition and Biological Activities of Mono- and Heterofloral Bee Pollen of Different Geographical Origins.
[So] Source:Int J Mol Sci;18(5), 2017 Apr 27.
[Is] ISSN:1422-0067
[Cp] País de publicação:Switzerland
[La] Idioma:eng
[Ab] Resumo:Recent research shows variations in pollen chemical constituents and, consequently, in their therapeutic properties. Mono and multifloral bee pollen extracts were investigated for antioxidant and enzyme inhibitory activity properties, phenolic compounds and fatty acid composition. Generally, spp. and multifloral extracts exhibited potent inhibitory activity against α-amylase, acetylcholinesterase, tyrosinase, lipoxygenase, lipase and hyaluronidase. On the other hand, spp. demonstrated higher antihemolytic activity. and spp. extracts exhibited important antioxidant properties in the different assays (ABTS, DPPH, ß-carotene/linoleic acid and reducing power). Moreover, these extracts had greater amounts of total phenols and flavonoids in comparison to others. The increase in antioxidant activity (decrease in EC values) was accompanied by an increase in the amount of total phenols in the extracts. The pollen extracts contained linoleic acid and α-linolenic acid as major fatty acids, followed by palmitic acid, and oleic acid. In this study, differences were observed in both chemical constituents and biological activities of the samples related to the geographical and botanical origin of bee pollen.
[Mh] Termos MeSH primário: Extratos Vegetais/química
Pólen/química
[Mh] Termos MeSH secundário: Acetilcolinesterase/química
Acetilcolinesterase/metabolismo
Animais
Antioxidantes/química
Antioxidantes/metabolismo
Abelhas
Cromatografia Gasosa
Cocos/química
Cocos/metabolismo
Eucalyptus/química
Eucalyptus/metabolismo
Ácidos Graxos/análise
Ácidos Graxos/química
Flavonoides/análise
Flavonoides/química
Melastomataceae/química
Melastomataceae/metabolismo
Monofenol Mono-Oxigenase/antagonistas & inibidores
Monofenol Mono-Oxigenase/metabolismo
Fenóis/análise
Fenóis/química
Extratos Vegetais/metabolismo
Análise de Componente Principal
alfa-Amilases/antagonistas & inibidores
alfa-Amilases/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antioxidants); 0 (Fatty Acids); 0 (Flavonoids); 0 (Phenols); 0 (Plant Extracts); EC 1.14.18.1 (Monophenol Monooxygenase); EC 3.1.1.7 (Acetylcholinesterase); EC 3.2.1.1 (alpha-Amylases)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180122
[Lr] Data última revisão:
180122
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170428
[St] Status:MEDLINE


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[PMID]:29267335
[Au] Autor:Milczarski P; Masojc P; Krajewski P; Stochmal A; Kowalczyk M; Angelov M; Ivanova V; Schollenberger M; Wakulinski W; Banaszak Z; Banaszak K; Rakoczy-Trojanowska M
[Ad] Endereço:West Pomeranian University of Technology, Szczecin, Poland.
[Ti] Título:QTL mapping for benzoxazinoid content, preharvest sprouting, α-amylase activity, and leaf rust resistance in rye (Secale cereale L.).
[So] Source:PLoS One;12(12):e0189912, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Mapping population of recombinant inbred lines (RILs) representing 541 × Ot1-3 cross exhibited wide variations of benzoxazinoid (BX) content in leaves and roots, brown rust resistance, α-amylase activity in the grain, and resistance to preharvest sprouting. QTL mapping of major BX species using a DArT-based map revealed a complex genetic architecture underlying the production of these main secondary metabolites engaged in stress and allelopathy responses. The synthesis of BX in leaves and roots was found to be regulated by different QTL. The QTL for the BX content, rust resistance, α-amylase activity, and preharvest sprouting partially overlapped; this points to their common genetic regulation by a definite subset of genes. Only one QTL for BX located on chromosome 7R coincided with the loci of the ScBx genes, which were mapped as two clusters on chromosomes 5RS (Bx3-Bx5) and 7R (Bx1-Bx2). The QTL common for several BX species, rust resistance, preharvest sprouting, and α-amylase activity are interesting objects for further exploration aimed at developing common markers for these important agronomic traits.
[Mh] Termos MeSH primário: Basidiomycota/patogenicidade
Benzoxazinas/metabolismo
Folhas de Planta/microbiologia
Locos de Características Quantitativas
Secale/microbiologia
alfa-Amilases/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Benzoxazines); EC 3.2.1.1 (alpha-Amylases)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180116
[Lr] Data última revisão:
180116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171222
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0189912


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[PMID]:28466664
[Au] Autor:Andrianome S; Hugueville L; de Seze R; Selmaoui B
[Ad] Endereço:a Department of Experimental Toxicology , Institut National de l'Environnement Industriel et des Risques (INERIS) , Verneuil-en-Halatte , France.
[Ti] Título:Increasing levels of saliva alpha amylase in electrohypersensitive (EHS) patients.
[So] Source:Int J Radiat Biol;93(8):841-848, 2017 08.
[Is] ISSN:1362-3095
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:PURPOSE: To assess the level of various salivary and urinary markers of patients with electromagnetic hypersensitivity (EHS) and to compare them with those of a healthy control group. MATERIALS AND METHODS: We analyzed samples from 30 EHS individuals and a matched control group of 25 individuals (non-EHS) aged between 22 and 66. We quantified cortisol both in saliva and urine, alpha amylase (sAA), immunoglobulin A and C Reactive Protein levels in saliva and neopterin in urine (uNeopterin). RESULTS: sAA was found to be significantly higher (p < 0.005) in the EHS group. uNeopterin and sAA analysis showed a significant difference based on the duration of EHS. CONCLUSION: Higher levels of sAA in EHS participants may suggest that the sympathetic adrenal medullar system is activated. However, most of the analyzed markers of the immune system, sympathetic activity and circadian rhythm did not vary significantly in the EHS group. There is a trend to the higher levels of some variables in subgroups according to the EHS duration.
[Mh] Termos MeSH primário: Campos Eletromagnéticos/efeitos adversos
Saliva/enzimologia
alfa-Amilases/metabolismo
[Mh] Termos MeSH secundário: Biomarcadores/urina
Estudos de Casos e Controles
Feminino
Seres Humanos
Masculino
Meia-Idade
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Biomarkers); EC 3.2.1.1 (alpha-Amylases)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:180111
[Lr] Data última revisão:
180111
[Sb] Subgrupo de revista:IM; S
[Da] Data de entrada para processamento:170504
[St] Status:MEDLINE
[do] DOI:10.1080/09553002.2017.1325971


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[PMID]:28455339
[Au] Autor:Tanaka M; Hiramoto T; Tada H; Shintani T; Gomi K
[Ad] Endereço:Laboratory of Bioindustrial Genomics, Department of Bioindustrial Informatics and Genomics, Graduate School of Agricultural Science, Tohoku University, Aramaki, Aoba-ku, Sendai, Japan.
[Ti] Título:Improved α-Amylase Production by Dephosphorylation Mutation of CreD, an Arrestin-Like Protein Required for Glucose-Induced Endocytosis of Maltose Permease and Carbon Catabolite Derepression in Aspergillus oryzae.
[So] Source:Appl Environ Microbiol;83(13), 2017 Jul 01.
[Is] ISSN:1098-5336
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:produces copious amount of amylolytic enzymes, and MalP, a major maltose permease, is required for the expression of amylase-encoding genes. The expression of these genes is strongly repressed by carbon catabolite repression (CCR) in the presence of glucose. MalP is transported from the plasma membrane to the vacuole by endocytosis, which requires the homolog of E6-AP carboxyl terminus ubiquitin ligase HulA, an ortholog of yeast Rsp5. In yeast, arrestin-like proteins mediate endocytosis as adaptors of Rsp5 and transporters. In the present study, we examined the involvement of CreD, an arrestin-like protein, in glucose-induced MalP endocytosis and CCR of amylase-encoding genes. Deletion of inhibited the glucose-induced endocytosis of MalP, and CreD showed physical interaction with HulA. Phosphorylation of CreD was detected by Western blotting, and two serine residues were determined as the putative phosphorylation sites. However, the phosphorylation state of the serine residues did not regulate MalP endocytosis and its interaction with HulA. Although α-amylase production was significantly repressed by deletion, both phosphorylation and dephosphorylation mimics of CreD had a negligible effect on α-amylase activity. Interestingly, dephosphorylation of CreD was required for CCR relief of amylase genes that was triggered by disruption of the deubiquitinating enzyme-encoding gene The α-amylase activity of the mutant was 1.6-fold higher than that of the wild type, and the dephosphorylation mimic of CreD further improved the α-amylase activity by 2.6-fold. These results indicate that a combination of the dephosphorylation mutation of CreD and disruption increased the production of amylolytic enzymes in In eukaryotes, glucose induces carbon catabolite repression (CCR) and proteolytic degradation of plasma membrane transporters via endocytosis. Glucose-induced endocytosis of transporters is mediated by their ubiquitination, and arrestin-like proteins act as adaptors of transporters and ubiquitin ligases. In this study, we showed that CreD, an arrestin-like protein, is involved in glucose-induced endocytosis of maltose permease and carbon catabolite derepression of amylase gene expression in Dephosphorylation of CreD was required for CCR relief triggered by the disruption of , which encodes a deubiquitinating enzyme; a combination of the phosphorylation-defective mutation of CreD and disruption dramatically improved α-amylase production. This study shows the dual function of an arrestin-like protein and provides a novel approach for improving the production of amylolytic enzymes in .
[Mh] Termos MeSH primário: Arrestina/metabolismo
Aspergillus oryzae/metabolismo
Repressão Catabólica
Endocitose
Proteínas Fúngicas/genética
Proteínas de Transporte de Monossacarídeos/genética
alfa-Amilases/genética
[Mh] Termos MeSH secundário: Arrestina/genética
Aspergillus oryzae/enzimologia
Aspergillus oryzae/genética
Carbono/metabolismo
Proteínas Fúngicas/metabolismo
Regulação Fúngica da Expressão Gênica
Glucose/metabolismo
Proteínas de Transporte de Monossacarídeos/metabolismo
Mutação
Fosforilação
Transporte Proteico
alfa-Amilases/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Arrestin); 0 (Fungal Proteins); 0 (Monosaccharide Transport Proteins); 7440-44-0 (Carbon); 9055-23-6 (maltose permease); EC 3.2.1.1 (alpha-Amylases); IY9XDZ35W2 (Glucose)
[Em] Mês de entrada:1712
[Cu] Atualização por classe:171225
[Lr] Data última revisão:
171225
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170430
[St] Status:MEDLINE


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[PMID]:28455329
[Au] Autor:Yang G; Yao H; Mozzicafreddo M; Ballarini P; Pucciarelli S; Miceli C
[Ad] Endereço:School of Biosciences and Veterinary Medicine, University of Camerino, Camerino, Macerata, Italy.
[Ti] Título:Rational Engineering of a Cold-Adapted α-Amylase from the Antarctic Ciliate Euplotes focardii for Simultaneous Improvement of Thermostability and Catalytic Activity.
[So] Source:Appl Environ Microbiol;83(13), 2017 Jul 01.
[Is] ISSN:1098-5336
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The α-amylases are endo-acting enzymes that hydrolyze starch by randomly cleaving the 1,4-α-d-glucosidic linkages between the adjacent glucose units in a linear amylose chain. They have significant advantages in a wide range of applications, particularly in the food industry. The eukaryotic α-amylase isolated from the Antarctic ciliated protozoon ( Amy) is an alkaline enzyme, different from most of the α-amylases characterized so far. Furthermore, Amy has the characteristics of a psychrophilic α-amylase, such as the highest hydrolytic activity at a low temperature and high thermolability, which is the major drawback of cold-active enzymes in industrial applications. In this work, we applied site-directed mutagenesis combined with rational design to generate a cold-active Amy with improved thermostability and catalytic efficiency at low temperatures. We engineered two Amy mutants. In one mutant, we introduced Pro residues on the A and B domains in surface loops. In the second mutant, we changed Val residues to Thr close to the catalytic site. The aim of these substitutions was to rigidify the molecular structure of the enzyme. Furthermore, we also analyzed mutants containing these combined substitutions. Biochemical enzymatic assays of engineered versions of Amy revealed that the combination of mutations at the surface loops increased the thermostability and catalytic efficiency of the enzyme. The possible mechanisms responsible for the changes in the biochemical properties are discussed by analyzing the three-dimensional structural model. Cold-adapted enzymes have high specific activity at low and moderate temperatures, a property that can be extremely useful in various applications as it implies a reduction in energy consumption during the catalyzed reaction. However, the concurrent high thermolability of cold-adapted enzymes often limits their applications in industrial processes. The α-amylase from the psychrophilic Antarctic ciliate (named Amy) is a cold-adapted enzyme with optimal catalytic activity in an alkaline environment. These unique features distinguish it from most α-amylases characterized so far. In this work, we engineered a novel Amy with improved thermostability, substrate binding affinity, and catalytic efficiency to various extents, without impacting its pH preference. These characteristics can be considered important properties for use in the food, detergent, and textile industries and in other industrial applications. The enzyme engineering strategy developed in this study may also provide useful knowledge for future optimization of molecules to be used in particular industrial applications.
[Mh] Termos MeSH primário: Euplotes/enzimologia
alfa-Amilases/química
[Mh] Termos MeSH secundário: Motivos de Aminoácidos
Regiões Antárticas
Biocatálise
Domínio Catalítico
Temperatura Baixa
Estabilidade Enzimática
Euplotes/química
Euplotes/genética
Euplotes/metabolismo
Concentração de Íons de Hidrogênio
Cinética
Mutagênese Sítio-Dirigida
Engenharia de Proteínas
alfa-Amilases/genética
alfa-Amilases/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
EC 3.2.1.1 (alpha-Amylases)
[Em] Mês de entrada:1712
[Cu] Atualização por classe:171225
[Lr] Data última revisão:
171225
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170430
[St] Status:MEDLINE


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[PMID]:28873609
[Au] Autor:Ayyash M; Al-Nuaimi AK; Al-Mahadin S; Liu SQ
[Ad] Endereço:Food Science Department, College of Food and Agriculture, United Arab Emirates University (UAEU), PO Box 1555, Al Ain, United Arab Emirates. Electronic address: mutamed.ayyash@uaeu.ac.ae.
[Ti] Título:In vitro investigation of anticancer and ACE-inhibiting activity, α-amylase and α-glucosidase inhibition, and antioxidant activity of camel milk fermented with camel milk probiotic: A comparative study with fermented bovine milk.
[So] Source:Food Chem;239:588-597, 2018 Jan 15.
[Is] ISSN:0308-8146
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:This study aimed to investigate in vitro the health-promoting benefits (anticancer activity, α-amylase and α-glucosidase inhibition, angiotensin-converting-enzyme (ACE)-inhibition, antioxidant and proteolytic activity) of camel milk fermented with indigenous probiotic strains of Lactobacillus spp., compared with fermented bovine milk. The three camel milk probiotic strains Lb. reuteri-KX881777, Lb. plantarum-KX881772, Lb. plantarum-KX881779 and a control strain Lb. plantarum DSM2468 were employed to ferment camel and bovine milks separately. The proteolytic and antioxidant activity of water soluble extracts (WSEs) from all fermented camel milks were higher than those of fermented bovine milk. α-Amylase inhibition of WSEs were >34% in both milk types fermented with all strains during storage periods, except the WSE of camel milk fermented by Lp.K772. The highest ACE-inhibition of the WSE from camel milk fermented by Lr.K777 was >80%. The proliferations of Caco-2, MCF-7 and HELA cells were more inhibited when treated with the WSE of fermented camel milk.
[Mh] Termos MeSH primário: Camelus
[Mh] Termos MeSH secundário: Animais
Antioxidantes
Células CACO-2
Fermentação
Seres Humanos
Leite
Probióticos
alfa-Amilases
alfa-Glucosidases
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antioxidants); EC 3.2.1.1 (alpha-Amylases); EC 3.2.1.20 (alpha-Glucosidases)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171128
[Lr] Data última revisão:
171128
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170907
[St] Status:MEDLINE


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[PMID]:29058615
[Au] Autor:Njanje I; Bagla VP; Beseni BK; Mbazima V; Lebogo KW; Mampuru L; Mokgotho MP
[Ad] Endereço:Department of Biochemistry, Microbiology and Biotechnology, Faculty of Science and Agriculture, University of Limpopo, Turfloop Campus, Private Bag X1106, Sovenga, Limpopo, 0727, South Africa. injanje@gmail.com.
[Ti] Título:Defatting of acetone leaf extract of Acacia karroo (Hayne) enhances its hypoglycaemic potential.
[So] Source:BMC Complement Altern Med;17(1):482, 2017 Oct 23.
[Is] ISSN:1472-6882
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Conventional drugs used to treat diabetes are too expensive, toxic and rarely available to rural communities. This study was aimed at investigating the phytochemical differences and hypoglycaemic effects (α-amylase enzyme inhibition, glucose uptake, GLUT4 translocation and phosphorylation of MAPKs) of non-defatted and defatted acetone leaf extract of Acacia karroo. METHODS: Qualitative phytochemical analyses of extracts were determined using standard chemical tests and total phenolic contents using the Folin-Ciocalteu reagent method. Presence of antioxidant constituents was determined using DPPH scavenging and ferric reducing power assays. Alpha amylase enzyme inhibitory potential was determined chromogenically and cytotoxicity of the extracts on C2C12 muscle and 3T3-L1 cells using the MTT assay. Glucose uptake by the cells was determined colorimetrically and the most active extract was evaluated for its ability to translocate GLUT4 and MAPKs phosphorylation potential using immunofluorescence microscopy and dot blot analysis, respectively. RESULTS: Phenols, flavonoids, tannins, saponins and cardiac glycosides were detected in both extracts. Defatting of the plant material resulted in low amounts of phenols (0.432 ± 0.014 TAE/mg), DPPH scavenging activity (EC 0.40 ± 0.012 mg/ml), low toxicity and high ferric reducing power (EC 1.13 ± 0.017 mg/ml), α-amylase enzyme inhibition (IC 30.2 ± 3.037 µg/ml) and glucose uptake by both cells. The defatted extract showed an increase in GLUT4 translocation (at 25 µg/ml) with decrease in Akt expression while in combination with insulin showed a decrease in GLUT4 translocation. A finding, that is implicative that the effect of the extract on GLUT4 translocation in C2C12 cells was not Akt dependent. The defatted extract in the absence and presence of insulin show varying phosphorylation levels of CREB, p38, GSK-3 and ERK2 which are important in cell survival and metabolism. CONCLUSION: This study represents the first report on the hypoglycemic potential of A. karroo and presence of compounds that can be exploited in the search for therapeutics with antidiabetic effect.
[Mh] Termos MeSH primário: Acacia/química
Antioxidantes/farmacologia
Glucose/metabolismo
Hipoglicemiantes/farmacologia
Extratos Vegetais/farmacologia
Folhas de Planta/química
[Mh] Termos MeSH secundário: Animais
Antioxidantes/química
Antioxidantes/farmacocinética
Antioxidantes/toxicidade
Linhagem Celular
Sobrevivência Celular/efeitos dos fármacos
Glucose/análise
Transportador de Glucose Tipo 4/metabolismo
Hipoglicemiantes/química
Hipoglicemiantes/farmacocinética
Hipoglicemiantes/toxicidade
Camundongos
Proteínas Quinases Ativadas por Mitógeno/metabolismo
Fenóis/química
Fenóis/farmacocinética
Fenóis/farmacologia
Fenóis/toxicidade
Fosforilação/efeitos dos fármacos
Extratos Vegetais/química
Extratos Vegetais/farmacocinética
Extratos Vegetais/toxicidade
alfa-Amilases/antagonistas & inibidores
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antioxidants); 0 (Glucose Transporter Type 4); 0 (Hypoglycemic Agents); 0 (Phenols); 0 (Plant Extracts); EC 2.7.11.24 (Mitogen-Activated Protein Kinases); EC 3.2.1.1 (alpha-Amylases); IY9XDZ35W2 (Glucose)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171030
[Lr] Data última revisão:
171030
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171024
[St] Status:MEDLINE
[do] DOI:10.1186/s12906-017-1987-6



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