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Pesquisa : D08.811.277.450.066.100 [Categoria DeCS]
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[PMID]:28727742
[Au] Autor:Jung YS; Lee BH; Yoo SH
[Ad] Endereço:Department of Food Science and Biotechnology, and Carbohydrate Bioproduct Research Center, Sejong University, Seoul, South Korea.
[Ti] Título:Physical structure and absorption properties of tailor-made porous starch granules produced by selected amylolytic enzymes.
[So] Source:PLoS One;12(7):e0181372, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Porous starch granules (PSGs) with various pores and cavity sizes were prepared by amylolysis enzymes. The greatest hydrolysis rate on corn starch granule was observed with α-amylase, followed by gluco- and ß-amylases. Temperature increase enhanced glucoamylase reaction rate more drastically than other enzyme treatments. Final hydrolysis level with glucoamylase reached to 66.9%, close to 67.5% of α-amylolysis. The α-amylase-treated PSGs displayed the greatest pore size and ratio of cavity-to-granule diameters. Gelatinization onset temperatures of PSGs increased to 72.1 (α-), 68.7 (ß-), and 68.1°C (gluco-amylolysis) after 8 h; enthalpy changes of ß- and gluco-amylase-treated PSGs increased to 13.4, and 13.1 J/g but α-amylase-treated one showed slightly reduced value of 8.5 J/g. Water holding capacities of PSGs were 209.7 (α-), 94.6 (ß-), and 133.8% (gluco-amylolysis), and the untreated control had 89.1%; oil holding capacities of them showed 304.5, 182.7, and 211.5%, respectively, while the untreated control had 161.8%. Thus, enzyme types and their reaction conditions can be applied to generate desirable cavity and pore sizes in starch granules. This biocatalytic approach could contribute to develop tailor-made PSGs with distinct internal structure for specific uses in wide range of food, pharmaceutical and other industrial applications.
[Mh] Termos MeSH primário: Glucana 1,4-alfa-Glucosidase/metabolismo
Amido/química
alfa-Amilases/metabolismo
beta-Amilase/metabolismo
[Mh] Termos MeSH secundário: Absorção Fisico-Química
Aspergillus niger/enzimologia
Bacillus licheniformis/enzimologia
Biocatálise
Varredura Diferencial de Calorimetria
Hordeum/enzimologia
Hidrólise
Microscopia Confocal
Microscopia Eletrônica de Varredura
Porosidade
Óleo de Soja/química
Amido/metabolismo
Temperatura Ambiente
Água/química
Zea mays/química
alfa-Amilases/química
beta-Amilase/química
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
059QF0KO0R (Water); 8001-22-7 (Soybean Oil); 9005-25-8 (Starch); EC 3.2.1.1 (alpha-Amylases); EC 3.2.1.2 (beta-Amylase); EC 3.2.1.3 (Glucan 1,4-alpha-Glucosidase)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170925
[Lr] Data última revisão:
170925
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170721
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0181372


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[PMID]:28238000
[Au] Autor:Lee JE; Lee AR; Kim H; Lee E; Kim TW; Shin WC; Kim JH
[Ad] Endereço:Traditional Alcoholic Beverage Research Team, Fermentation Research Center, Korea Food Research Institute, Seongnam 13539, Republic of Korea.
[Ti] Título:Restoration of Traditional Korean Nuruk and Analysis of the Brewing Characteristics.
[So] Source:J Microbiol Biotechnol;27(5):896-908, 2017 May 28.
[Is] ISSN:1738-8872
[Cp] País de publicação:Korea (South)
[La] Idioma:eng
[Ab] Resumo:In this study, a total of 58 different kinds of nuruk (a traditional Korean fermentation starter) were prepared, including 46 kinds of restored nuruk from ancient documents. Each nuruk was evaluated by analysis of its saccharification power, and the enzyme activities of glucoamylase, α-amylase, ß-amylase, protease, and ß-glucanase. The range of saccharification power (sp) of the restored nuruk ranged between 85 and 565 sp. The diastatic enzymes, α-amylase, ß-amylase, and glucoamylase, were significantly correlated to the saccharification power value; conversely, ß-glucanase and protease did not have a correlative relationship with saccarification power. In addition, their brewing properties on chemical and organoleptic aspects of traditional alcoholic beverage production were compared. Each raw and supplementary material contained in nuruk showed its own unique characteristics on Korean alcoholic beverage brewing. For the first time, in this study, the traditional Korean nuruk types mentioned in ancient documents were restored using modernized production methods, and also characterized based on their brewing properties. Our results could be utilized as a basis for further study of traditional alcoholic beverages and their valuable microorganisms.
[Mh] Termos MeSH primário: Fermentação
Microbiologia de Alimentos
Fungos/enzimologia
Saccharomyces cerevisiae/química
Saccharomyces cerevisiae/enzimologia
[Mh] Termos MeSH secundário: Bebidas Alcoólicas/microbiologia
Ativação Enzimática
Ensaios Enzimáticos
Glucana 1,4-alfa-Glucosidase/metabolismo
Glicosídeo Hidrolases
Concentração de Íons de Hidrogênio
Peptídeo Hidrolases/metabolismo
República da Coreia
Saccharomyces cerevisiae/classificação
Temperatura Ambiente
alfa-Amilases/metabolismo
beta-Amilase/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
EC 3.2.1.- (Glycoside Hydrolases); EC 3.2.1.1 (alpha-Amylases); EC 3.2.1.2 (beta-Amylase); EC 3.2.1.3 (Glucan 1,4-alpha-Glucosidase); EC 3.4.- (Peptide Hydrolases)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171031
[Lr] Data última revisão:
171031
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170227
[St] Status:MEDLINE
[do] DOI:10.4014/jmb.1610.10039


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[PMID]:28225829
[Au] Autor:Li J; Zhou W; Francisco P; Wong R; Zhang D; Smith SM
[Ad] Endereço:School of Plant Biology, The University of Western Australia, Western Australia, Australia.
[Ti] Título:Inhibition of Arabidopsis chloroplast ß-amylase BAM3 by maltotriose suggests a mechanism for the control of transitory leaf starch mobilisation.
[So] Source:PLoS One;12(2):e0172504, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Starch breakdown in leaves at night is tightly matched to the duration of the dark period, but the mechanism by which this regulation is achieved is unknown. In Arabidopsis chloroplasts, ß-amylase BAM3 hydrolyses transitory starch, producing maltose and residual maltotriose. The aim of the current research was to investigate the regulatory and kinetic properties of BAM3. The BAM3 protein was expressed in Escherichia coli and first assayed using a model substrate. Enzyme activity was stimulated by treatment with dithiothreitol and was increased 40% by 2-10 µM Ca2+ but did not require Mg2+. In order to investigate substrate specificity and possible regulatory effects of glucans, we developed a GC-MS method to assay reaction products. BAM3 readily hydrolysed maltohexaose with a Km of 1.7 mM and Kcat of 4300 s-1 but activity was 3.4-fold lower with maltopentaose and was negligible with maltotetraose. With maltohexaose or amylopectin as substrates and using [UL-13C12]maltose in an isotopic dilution method, we discovered that BAM3 activity is inhibited by maltotriose at physiological (mM) concentrations, but not by maltose. In contrast, the extracellular ß-amylase of barley is only weakly inhibited by maltotriose. Our results may explain the impaired starch breakdown in maltotriose-accumulating mutants such as dpe1 which lacks the chloroplast disproportionating enzyme (DPE1) metabolising maltotriose to glucose. We hypothesise that the rate of starch breakdown in leaves can be regulated by inhibition of BAM3 by maltotriose, the concentration of which is determined by DPE, which is in turn influenced by the stromal concentration of glucose. Since the plastid glucose transporter pGlcT catalyses facilitated diffusion between stroma and cytosol, changes in consumption of glucose in the cytosol are expected to lead to concomitant changes in plastid glucose and maltotriose, and hence compensatory changes in BAM3 activity.
[Mh] Termos MeSH primário: Proteínas de Arabidopsis/metabolismo
Cloroplastos/efeitos dos fármacos
Proteínas Serina-Treonina Quinases/metabolismo
Amido/metabolismo
Trissacarídeos/farmacologia
[Mh] Termos MeSH secundário: Arabidopsis
Cloroplastos/metabolismo
Ativação Enzimática/efeitos dos fármacos
Escherichia coli
Cromatografia Gasosa-Espectrometria de Massas
Folhas de Planta/efeitos dos fármacos
Folhas de Planta/metabolismo
beta-Amilase/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Arabidopsis Proteins); 0 (Trisaccharides); 639K0T34IK (maltotriose); 9005-25-8 (Starch); EC 2.7.11.1 (BAM3 protein, Arabidopsis); EC 2.7.11.1 (Protein-Serine-Threonine Kinases); EC 3.2.1.2 (beta-Amylase)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170817
[Lr] Data última revisão:
170817
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170223
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0172504


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[PMID]:28062835
[Au] Autor:Lv Y; Yang M; Hu D; Yang Z; Ma S; Li X; Xiong L
[Ad] Endereço:National Key Laboratory of Crop Genetic Improvement and National Center of Plant Gene Research (Wuhan), Huazhong Agricultural University, Wuhan 430070, China.
[Ti] Título:The OsMYB30 Transcription Factor Suppresses Cold Tolerance by Interacting with a JAZ Protein and Suppressing ß-Amylase Expression.
[So] Source:Plant Physiol;173(2):1475-1491, 2017 Feb.
[Is] ISSN:1532-2548
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Cold stress is one of the major limiting factors for rice (Oryza sativa) productivity. Several MYB transcriptional factors have been reported as important regulators in the cold stress response, but the molecular mechanisms are largely unknown. In this study, we characterized a cold-responsive R2R3-type MYB gene, OsMYB30, for its regulatory function in cold tolerance in rice. Functional analysis revealed that overexpression of OsMYB30 in rice resulted in increased cold sensitivity, while the osmyb30 knockout mutant showed increased cold tolerance. Microarray and quantitative real-time polymerase chain reaction analyses revealed that a few ß-amylase (BMY) genes were down-regulated by OsMYB30. The BMY activity and maltose content, which were decreased and increased in the OsMYB30 overexpression and osmyb30 knockout mutant, respectively, were correlated with the expression patterns of the BMY genes. OsMYB30 was shown to bind to the promoters of the BMY genes. These results suggested that OsMYB30 exhibited a regulatory effect on the breakdown of starch through the regulation of the BMY genes. In addition, application of maltose had a protective effect for cell membranes under cold stress conditions. Furthermore, we identified an OsMYB30-interacting protein, OsJAZ9, that had a significant effect in suppressing the transcriptional activation of OsMYB30 and in the repression of BMY genes mediated by OsMYB30. These results together suggested that OsMYB30 might be a novel regulator of cold tolerance through the negative regulation of the BMY genes by interacting with OsJAZ9 to fine-tune the starch breakdown and the content of maltose, which might contribute to the cold tolerance as a compatible solute.
[Mh] Termos MeSH primário: Oryza/fisiologia
Proteínas de Plantas/metabolismo
Estresse Fisiológico
beta-Amilase/metabolismo
[Mh] Termos MeSH secundário: Membrana Celular/metabolismo
Temperatura Baixa
Perfilação da Expressão Gênica
Regulação da Expressão Gênica de Plantas
Maltose/metabolismo
Mutação
Oryza/genética
Proteínas de Plantas/genética
Plantas Geneticamente Modificadas
Regiões Promotoras Genéticas
Amido/metabolismo
Fatores de Transcrição/genética
Fatores de Transcrição/metabolismo
beta-Amilase/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Plant Proteins); 0 (Transcription Factors); 69-79-4 (Maltose); 9005-25-8 (Starch); EC 3.2.1.2 (beta-Amylase)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171003
[Lr] Data última revisão:
171003
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170108
[St] Status:MEDLINE
[do] DOI:10.1104/pp.16.01725


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[PMID]:27664602
[Au] Autor:Arijaje EO; Wang YJ
[Ad] Endereço:Department of Food Science, University of Arkansas, 2650 N. Young Avenue, Fayetteville, AR 72704, USA.
[Ti] Título:Effects of chemical and enzymatic modifications on starch-linoleic acid complex formation.
[So] Source:Food Chem;217:9-17, 2017 Feb 15.
[Is] ISSN:0308-8146
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:This study investigated the complexation yield and physicochemical properties of soluble and insoluble starch complexes with linoleic acid when a ß-amylase treatment was applied to acetylated and debranched potato starch. The degree of acetylation was generally higher in the soluble complexes than in the insoluble ones. The insoluble complexes from the acetylated starch displayed the V-type pattern, whereas, the soluble complexes displayed a mixture of either the A-/V-type or the B-/V-type pattern. Acetylation decreased onset and peak melting temperatures for the insoluble complexes, whereas no melting endotherm was observed in the soluble complexes. Acetylation substantially increased the amount of complexed linoleic acid in the insoluble complexes, but had little positive effect on the formation of the soluble complexes. The ß-amylase treatment significantly increased the complexed linoleic content in both soluble and insoluble complexes for the low acetylated starch, but not for the high acetylated starch.
[Mh] Termos MeSH primário: Ácido Linoleico/química
Amido/química
beta-Amilase/metabolismo
[Mh] Termos MeSH secundário: Acetilação
Metabolismo dos Carboidratos
Fenômenos Químicos
Ácido Linoleico/metabolismo
Amido/metabolismo
Temperatura Ambiente
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
9005-25-8 (Starch); 9KJL21T0QJ (Linoleic Acid); EC 3.2.1.2 (beta-Amylase)
[Em] Mês de entrada:1701
[Cu] Atualização por classe:170902
[Lr] Data última revisão:
170902
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160925
[St] Status:MEDLINE


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[PMID]:27562405
[Au] Autor:Antonyuk M; Navalikhina A; Ternovska T
[Ad] Endereço:National University of Kyiv-Mohyla Academy, 2 Skovorody vul., Kyiv, 04655, Ukraine.
[Ti] Título:Beta-amylase gene variability in introgressive wheat lines.
[So] Source:J Appl Genet;58(2):143-149, 2017 May.
[Is] ISSN:2190-3883
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Variability of the beta-amylase gene in bread wheat, artificial amphidiploids, and derived introgression wheat lines was analyzed. Variation in homeologous beta-amylase sequences caused by the presence of MITE (Miniature Inverted-Repeat Transposable Element) and its footprint has been identified in bread wheat. The previously unknown location of MITE in Triticum urartu and T. aestivum L. beta-amylase gene has been found. These species have a MITE sequence in the third intron of beta-amylase, as opposed to Aegilops comosa and a number of other Triticeae species, which have it in the fourth intron. These two MITEs from Ae. comosa and T. aestivum were shown to have low identity scores. Miosa, an artificial amphidiploid, which has the M genome from Ae. comosa was shown to lose the MITE sequences. This loss might be caused by genomic shock due to allopolyploidization.
[Mh] Termos MeSH primário: Elementos de DNA Transponíveis
Genes de Plantas
Triticum/genética
beta-Amilase/genética
[Mh] Termos MeSH secundário: Sequência de Bases
DNA de Plantas/genética
Variação Genética
Íntrons
Poaceae/genética
Triticum/enzimologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (DNA Transposable Elements); 0 (DNA, Plant); EC 3.2.1.2 (beta-Amylase)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:171111
[Lr] Data última revisão:
171111
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160827
[St] Status:MEDLINE
[do] DOI:10.1007/s13353-016-0364-3


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[PMID]:27754395
[Au] Autor:Qin Y; Zhu H; Zhang M; Zhang H; Xiang C; Li B
[Ad] Endereço:Faculty of Life Science and Technology, Kunming University of Science and Technology, Kunming 650500, China. qiny1985@163.com.
[Ti] Título:GC-MS Analysis of Membrane-Graded Fulvic Acid and Its Activity on Promoting Wheat Seed Germination.
[So] Source:Molecules;21(10), 2016 Oct 13.
[Is] ISSN:1420-3049
[Cp] País de publicação:Switzerland
[La] Idioma:eng
[Ab] Resumo:The chemical composition of fulvic acid (FA) with a molecular weight below 500 (FA-500) was analyzed, and its activity on promoting the seed germination of wheat was studied in this paper. The FA-500 was obtained by membrane separation technology and qualitatively and quantitatively analyzed by using gas chromatography-mass spectrometry combined with the retention index. Forty-seven constituents were identified, including structures with ester, acid and alcohol groups, which accounted for 95% of the total composition. The highest relative content of compounds was diethyl succinate and diethyl malonate, accounting for 29% and 17% of the total, respectively. Yannong 19 and Luyuan 301 wheat seeds were steeped with the FA-500 solution of different concentration respectively for two hours. Several markers were assessed: germination rate, coleoptile and radicle length, germination index, vitality index and the activity of α-amylase and (α+ß) amylase. The results indicated that FA-500 had a significant effect on promoting seed germination within an appropriate concentration range. The best concentration was 0.5‰, and an inhibiting effect would appear with the increase of concentration. In the process of seed germination, FA-500 may affect the growth of the seed through influencing the amylase activity, which was related to respiration.
[Mh] Termos MeSH primário: Benzopiranos/química
Benzopiranos/farmacologia
Cromatografia Gasosa-Espectrometria de Massas/métodos
Germinação/efeitos dos fármacos
Triticum/efeitos dos fármacos
[Mh] Termos MeSH secundário: Regulação da Expressão Gênica de Plantas/efeitos dos fármacos
Peso Molecular
Proteínas de Plantas/metabolismo
Sementes/efeitos dos fármacos
Sementes/crescimento & desenvolvimento
Triticum/crescimento & desenvolvimento
alfa-Amilases/metabolismo
beta-Amilase/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Benzopyrans); 0 (Plant Proteins); EC 3.2.1.1 (alpha-Amylases); EC 3.2.1.2 (beta-Amylase); XII14C5FXV (fulvic acid)
[Em] Mês de entrada:1704
[Cu] Atualização por classe:170403
[Lr] Data última revisão:
170403
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161019
[St] Status:MEDLINE


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[PMID]:27581558
[Au] Autor:Kocabay S; Çetinkaya S; Akkaya B; Yenidünya AF
[Ad] Endereço:Inönü University, Faculty of Science, Department of Molecular Biology and Genetic, Malatya, Turkey.
[Ti] Título:Characterization of thermostable ß-amylase isozymes from Lactobacillus fermentum.
[So] Source:Int J Biol Macromol;93(Pt A):195-202, 2016 Dec.
[Is] ISSN:1879-0003
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:A strain of Lactobacillus fermentum producing two isozymes of a 20kDa ß-amylase was isolated from the faecal sample of a newborn. The starin was identified by sequencing its 16S rRNA gene. The two ß-amylase isozymes were resolved and visualized by two dimensional protein gel electrophoresis (2-D gel electrophoresis). Some of the physical and biochemical properties of the enzymes were characterized. The ß-amylase displayed two optimum pH s, 5.0 and 10.0 and two optimum temperatures, 45°C and 37°C, respectively. The isozymes hydrolyzed different substrates: glycogen at pH 5.0, and corn starch at pH 10.0. The activity did not require Ca , though the activity at pH 10.0 was enhanced in the presence of 5.0mM and 10.0mM CaCl 110% and 130%, respectively.
[Mh] Termos MeSH primário: Lactobacillus fermentum/enzimologia
Temperatura Ambiente
beta-Amilase/química
beta-Amilase/metabolismo
[Mh] Termos MeSH secundário: Estabilidade Enzimática
Glicogênio/metabolismo
Concentração de Íons de Hidrogênio
Hidrólise
Isoenzimas/química
Isoenzimas/isolamento & purificação
Isoenzimas/metabolismo
Cinética
Metais/farmacologia
Desnaturação Proteica/efeitos dos fármacos
Cloreto de Sódio/farmacologia
Amido/metabolismo
Especificidade por Substrato
beta-Amilase/isolamento & purificação
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Isoenzymes); 0 (Metals); 451W47IQ8X (Sodium Chloride); 9005-25-8 (Starch); 9005-79-2 (Glycogen); EC 3.2.1.2 (beta-Amylase)
[Em] Mês de entrada:1704
[Cu] Atualização por classe:170404
[Lr] Data última revisão:
170404
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160902
[St] Status:MEDLINE


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[PMID]:27341479
[Au] Autor:Olaerts H; Roye C; Derde LJ; Sinnaeve G; Meza WR; Bodson B; Courtin CM
[Ad] Endereço:Laboratory of Food Chemistry and Biochemistry & Leuven Food Science and Nutrition Research Centre (LFoRCe), KU Leuven , Kasteelpark Arenberg 20, B-3001 Leuven, Belgium.
[Ti] Título:Evolution and Distribution of Hydrolytic Enzyme Activities during Preharvest Sprouting of Wheat (Triticum aestivum) in the Field.
[So] Source:J Agric Food Chem;64(28):5644-52, 2016 Jul 20.
[Is] ISSN:1520-5118
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:To date, research on preharvest sprouted (PHS) wheat has mostly been conducted on kernels germinated under laboratory conditions, which differ widely from conditions in the field. To obtain detailed knowledge of the evolution of hydrolytic enzyme activities in PHS wheat (Triticum aestivum), a broad collection of samples from three varieties was obtained by harvesting before, at, and after maturity. Delaying harvest time coupled with periods of heavy rainfall caused sprouting in the kernels, observed as a drop in Falling Number and an increase in α-amylase activity. The appearance of α- and ß-amylase, peptidase, and endoxylanase activity during field sprouting was independent from each other. Consequently, Falling Number could not be used to predict activity of other hydrolytic enzymes. When differentiating endogenous from kernel-associated microbial enzymes, results showed that α- and ß-amylase and peptidase activity of PHS kernels were predominantly of endogenous origin, whereas endoxylanase activity was largely from microbial origin.
[Mh] Termos MeSH primário: Proteínas de Plantas/metabolismo
Sementes/enzimologia
Triticum/crescimento & desenvolvimento
[Mh] Termos MeSH secundário: Endo-1,4-beta-Xilanases/análise
Endo-1,4-beta-Xilanases/metabolismo
Germinação
Peptídeo Hidrolases/análise
Peptídeo Hidrolases/metabolismo
Proteínas de Plantas/análise
Sementes/química
Sementes/crescimento & desenvolvimento
Triticum/química
Triticum/enzimologia
alfa-Amilases/análise
alfa-Amilases/metabolismo
beta-Amilase/análise
beta-Amilase/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Plant Proteins); EC 3.2.1.1 (alpha-Amylases); EC 3.2.1.2 (beta-Amylase); EC 3.2.1.8 (Endo-1,4-beta Xylanases); EC 3.4.- (Peptide Hydrolases)
[Em] Mês de entrada:1704
[Cu] Atualização por classe:170414
[Lr] Data última revisão:
170414
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160625
[St] Status:MEDLINE
[do] DOI:10.1021/acs.jafc.6b01711


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[PMID]:27160849
[Au] Autor:Zamoner LO; Aragão-Leoneti V; Mantoani SP; Rugen MD; Nepogodiev SA; Field RA; Carvalho I
[Ad] Endereço:School of Pharmaceutical Sciences of Ribeirão Preto, University of São Paulo, Av. do Café s/n, Monte Alegre, Ribeirão Preto 14040-930, Brazil.
[Ti] Título:CuAAC click chemistry with N-propargyl 1,5-dideoxy-1,5-imino-D-gulitol and N-propargyl 1,6-dideoxy-1,6-imino-D-mannitol provides access to triazole-linked piperidine and azepane pseudo-disaccharide iminosugars displaying glycosidase inhibitory properties.
[So] Source:Carbohydr Res;429:29-37, 2016 Jun 24.
[Is] ISSN:1873-426X
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Protecting group-free synthesis of 1,2:5,6-di-anhydro-D-mannitol, followed by ring opening with propargylamine and subsequent ring closure produced a separable mix of piperidine N-propargyl 1,5-dideoxy-1,5-imino-D-gulitol and azepane N-propargyl 1,6-dideoxy-1,6-imino-D-mannitol. In O-acetylated form, these two building blocks were subjected to CuAAC click chemistry with a panel of three differently azide-substituted glucose building blocks, producing iminosugar pseudo-disaccharides in good yield. The overall panel of eight compounds, plus 1-deoxynojirimycin (DNJ) as a benchmark, was evaluated as prospective inhibitors of almond ß-glucosidase, yeast α-glucosidase and barley ß-amylase. The iminosugar pseudo-disaccharides showed no inhibitory activity against almond ß-glucosidase, while the parent N-propargyl 1,5-dideoxy-1,5-imino-D-gulitol and N-propargyl 1,6-dideoxy-1,6-imino-D-mannitol likewise proved to be inactive against yeast α-glucosidase. Inhibitory activity could be reinstated in the former series by appropriate substitution on nitrogen. The greater activity of the piperidine could be rationalized based on docking studies. Further, potent inhibition of ß-amylase was observed with compounds from both the piperidine and azepane series.
[Mh] Termos MeSH primário: Inibidores Enzimáticos/síntese química
Compostos Heterocíclicos com 1 Anel/síntese química
Imino Açúcares/síntese química
Piperidinas/síntese química
Triazóis/síntese química
alfa-Glucosidases/química
beta-Amilase/química
beta-Glucosidase/química
[Mh] Termos MeSH secundário: 1-Desoxinojirimicina/química
Azidas/química
Química Click/métodos
Dissacarídeos/química
Inibidores Enzimáticos/química
Glucose/química
Compostos Heterocíclicos com 1 Anel/química
Hordeum/química
Hordeum/enzimologia
Imino Açúcares/química
Manitol/química
Pargilina/análogos & derivados
Pargilina/química
Piperidinas/química
Propilaminas/química
Prunus dulcis/química
Prunus dulcis/enzimologia
Saccharomyces cerevisiae/química
Saccharomyces cerevisiae/enzimologia
Triazóis/química
beta-Amilase/antagonistas & inibidores
beta-Glucosidase/antagonistas & inibidores
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Azides); 0 (Disaccharides); 0 (Enzyme Inhibitors); 0 (Heterocyclic Compounds, 1-Ring); 0 (Imino Sugars); 0 (Piperidines); 0 (Propylamines); 0 (Triazoles); 19130-96-2 (1-Deoxynojirimycin); 2450-71-7 (propargylamine); 3OWL53L36A (Mannitol); 9MV14S8G3E (Pargyline); EC 3.2.1.2 (beta-Amylase); EC 3.2.1.20 (alpha-Glucosidases); EC 3.2.1.21 (beta-Glucosidase); IY9XDZ35W2 (Glucose)
[Em] Mês de entrada:1701
[Cu] Atualização por classe:170119
[Lr] Data última revisão:
170119
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160511
[St] Status:MEDLINE



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