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beta glucosidase/karies

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ArtikkelitKliiniset tutkimuksetPatentit
Sivu 1 alkaen 33 tuloksia
Bacteria species involved in degradation of cellulosic substrates produce a variety of enzymes for processing related compounds along the hydrolytic pathway. Paenibacillus polymyxa encodes two homologous beta-glucosidases, BglA and BglB, presenting different quaternary structures and substrate

Effect of xylitol on salivary β-glucosidase in humans.

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Dental biofilm - in which a diverse set of microorganisms are embedded in a complex polysaccharide matrix that adheres to oral components - is one of the most complex microbial communities in the human body. As biofilm formation is related to oral infections, such as caries and periodontal diseases,
The increasing development of the biotechnology industry demands the design of enzymes suitable to be used in conditions that often require broad resistance against adverse conditions. beta-glucosidase A from Bacillus polymyxa is an interesting model for studies of protein engineering. This is a

Functional analysis of the aglycone-binding site of the maize beta-glucosidase Zm-p60.1.

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Beta-glucosidases such as Zm-p60.1 (Zea mays) and Bgl4:1 (Brassica napus) have implicated roles in regulating plant development by releasing biologically active cytokinins from O-glucosides. A key determinant of substrate specificity in Zm-p60.1 is the F193-F200-W373-F461 cluster. However, despite

Activity of hydrolytic enzymes of Candida albicans strains isolated from patients with periodontal and membrane mucosae of oral cavity diseases.

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Fungi are elements of the ontocenosis of the oral cavity and causal factors of inflammatory lesions in its mucous membrane. The objective of the study was to find differences in the activity of hydrolytic enzymes of Candida albicans isolated from patients with diseases of the periodontium and mucous

Directed Evolution of Clostridium thermocellum β-Glucosidase A Towards Enhanced Thermostability.

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β-Glucosidases are key enzymes in the process of cellulose utilization. It is the last enzyme in the cellulose hydrolysis chain, which converts cellobiose to glucose. Since cellobiose is known to have a feedback inhibitory effect on a variety of cellulases, β-glucosidase can prevent this inhibition

Cariogenic actinomyces identified with a beta-glucosidase-dependent green color reaction to Gardenia jasminoides extract.

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The oral bacteria Actinomyces naeslundii and Actinomyces viscosus are known to contribute to the initiation and progression of human dental caries, especially root caries. We report that both A. naeslundii and A. viscosus react with a component in the Gardenia jasminoides extract to produce a

Cyclodextrin-mediated crystallization of acid β-glucosidase in complex with amphiphilic bicyclic nojirimycin analogues.

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Cyclodextrin-based host-guest chemistry has been exploited to facilitate co-crystallization of recombinant human acid β-glucosidase (β-glucocerebrosidase, GlcCerase) with amphiphilic bicyclic nojirimycin analogues of the sp(2)-iminosugar type. Attempts to co-crystallize GlcCerase with
Gaucher disease is caused by mutations in the gene encoding acid beta-glucosidase (GlcCerase), resulting in glucosylceramide (GlcCer) accumulation. The only currently available orally administered treatment for Gaucher disease is N-butyl-deoxynojirimycin (Zavesca, NB-DNJ), which partially inhibits

Prevotella fusca sp. nov. and Prevotella scopos sp. nov., isolated from the human oral cavity.

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Two strains of anaerobic, Gram-negative bacilli isolated from the human oral cavity were subjected to a comprehensive range of phenotypic and genotypic tests and were found to belong to two separate taxa. Phylogenetic analysis of full-length 16S rRNA gene sequences showed that the strains were both

Streptococcus crista sp. nov., a viridans streptococcus with tufted fibrils, isolated from the human oral cavity and throat.

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We studied strains of an unusual streptococcus that superficially resembles Streptococcus sanguis but has fibrils that are arranged in lateral tufts. These strains were originally isolated from human throats and oral cavities and have been referred to previously as "Streptococcus sanguis I," the "CR

In-Silico Characterization of Glycosyl Hydrolase Family 1 β-Glucosidase from Trichoderma asperellum UPM1

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β-glucosidases (Bgl) are widely utilized for releasing non-reducing terminal glucosyl residues. Nevertheless, feedback inhibition by glucose end product has limited its application. A noticeable exception has been found for β-glucosidases of the glycoside hydrolase (GH) family 1, which exhibit

Structural basis for glucose tolerance in GH1 β-glucosidases.

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Product inhibition of β-glucosidases (BGs) by glucose is considered to be a limiting step in enzymatic technologies for plant-biomass saccharification. Remarkably, some β-glucosidases belonging to the GH1 family exhibit unusual properties, being tolerant to, or even stimulated by, high glucose

Crystal structure of beta-glucosidase A from Bacillus polymyxa: insights into the catalytic activity in family 1 glycosyl hydrolases.

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Family 1 glycosyl hydrolases are a very relevant group of enzymes because of the diversity of biological roles in which they are involved, and their generalized occurrence in all sorts of living organisms. The biological plasticity of these enzymes is a consequence of the variety of beta-glycosidic

Leptotrichia hongkongensis sp. nov., a novel Leptotrichia species with the oral cavity as its natural reservoir.

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A straight, non-sporulating, Gram-variable bacillus (HKU24(T)) was recovered from the blood culture of a patient with metastatic breast carcinoma. After repeated subculturing in BACTEC Plus Anaerobic/F blood culture broth, HKU24(T) grew on brucella agar as non-hemolytic, pinpoint colonies after 96 h
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