Ferreira TF, De Andrade LR, Coelho MAZ, Da Rocha-Leão MHM A new method to obtain β-glucan from Saccharomyces cerevisiae cells Catalysis Science and Technology1(6) (2011)
1068-1071
Publication DOI:10.1039/c0cy00057d Journal NLM ID:101636664 Publisher: Cambridge: Royal Society of Chemistry Correspondence: Ferreira TF <tatianafelixufrj.br> Institutions: School of Chemistry, Federal University of Rio de Janeiro, Rio de Janeiro, Brazil, Institute of Biomedical Sciences, Federal University of Rio de Janeiro, Rio de Janeiro, Brazil
In this work, a simple method was developed to increase cell wall porosity and to achieve partial hydrolysis of β-glucan. First, the cells were permeabilized using ethanol under agitation. Then the cells were treated with glass beads to increase cell wall porosity and subjected to an enzymatic treatment to degrade glycogen at 65 °C for 30 minutes. Finally, the cells were incubated at 57 °C for 2 hours to partially degrade β-glucan. Whole cells, permeabilized cells and permeabilized cells with partially hydrolyzed β-glucan were evaluated by optical microscopy and transmission electron microscopy. From the images of permeabilized cells with partially hydrolyzed β-glucan it was possible to visualize structures named "ghosts", which are alike along microcapsules containing β-glucan. These structures can be used to aggregate β-glucan in food industrialized products.
Methods: acid hydrolysis, enzymatic digestion, cell growth, TEM, glucose oxidase method Enzymes that release or process the structure: A7255-amyloglucosidase Comments, role: β-glucan main chain
Related record ID(s): 43366 NCBI Taxonomy refs (TaxIDs):4932 Reference(s) to other database(s): GTC:G51056AN Show glycosyltransferases
Ferreira TF, De Andrade LR, Coelho MAZ, Da Rocha-Leão MHM A new method to obtain β-glucan from Saccharomyces cerevisiae cells Catalysis Science and Technology1(6) (2011)
1068-1071
Publication DOI:10.1039/c0cy00057d Journal NLM ID:101636664 Publisher: Cambridge: Royal Society of Chemistry Correspondence: Ferreira TF <tatianafelixufrj.br> Institutions: School of Chemistry, Federal University of Rio de Janeiro, Rio de Janeiro, Brazil, Institute of Biomedical Sciences, Federal University of Rio de Janeiro, Rio de Janeiro, Brazil
In this work, a simple method was developed to increase cell wall porosity and to achieve partial hydrolysis of β-glucan. First, the cells were permeabilized using ethanol under agitation. Then the cells were treated with glass beads to increase cell wall porosity and subjected to an enzymatic treatment to degrade glycogen at 65 °C for 30 minutes. Finally, the cells were incubated at 57 °C for 2 hours to partially degrade β-glucan. Whole cells, permeabilized cells and permeabilized cells with partially hydrolyzed β-glucan were evaluated by optical microscopy and transmission electron microscopy. From the images of permeabilized cells with partially hydrolyzed β-glucan it was possible to visualize structures named "ghosts", which are alike along microcapsules containing β-glucan. These structures can be used to aggregate β-glucan in food industrialized products.
Methods: acid hydrolysis, enzymatic digestion, cell growth, TEM, glucose oxidase method Enzymes that release or process the structure: A7255-amyloglucosidase Comments, role: β-glucan side chain
Related record ID(s): 43365 NCBI Taxonomy refs (TaxIDs):4932 Reference(s) to other database(s): GTC:G26777BZ Show glycosyltransferases
Neustroev KN, Golubev AM, Firsov LM, Ibatullin FM, Protasevich II, Makarov AA Effect of modification of carbohydrate component on properties of glucoamylase FEBS Letters316 (1993)
157-160
The structure was elucidated in this paper NCBI PubMed ID:8420800 Journal NLM ID:0155157 Publisher: Elsevier Institutions: Petersburg Nuclear Physics Institute, Gatchina, St. Petersburg, Russian Federation
In this study, we investigated enzymatic deglycosylation of glucoamylase from Aspergillus awamori X 100/D27, a glycoprotein which has two N-linked and about forty short mannose-bearing O-linked sugars per molecule. O-Linked sugars were modified by treatment with α-mannosidase and N-linked sugars were removed using endo-β-N-acetylglucosaminidase F. Analysis of conformational changes following deglycosylation suggests that O-linked sugars essentially contribute to the stabilization of glucoamylase domains. Modification of the carbohydrate component by adding 1-deoxymannojirimycin to the culture medium induced inhibition of α-mannosidases involved in the processing, leading to a more complete glycosylation and, consequently, to a higher stability of the enzyme.
Related record ID(s): 125758 NCBI Taxonomy refs (TaxIDs):105351 Reference(s) to other database(s): GTC:G33131BN, CCSD:26370, CBank-STR:3078 Show glycosyltransferases
There are 3 chemically distinct structures. Please, select:
Neustroev KN, Golubev AM, Firsov LM, Ibatullin FM, Protasevich II, Makarov AA Effect of modification of carbohydrate component on properties of glucoamylase FEBS Letters316 (1993)
157-160
The structure was elucidated in this paper NCBI PubMed ID:8420800 Journal NLM ID:0155157 Publisher: Elsevier Institutions: Petersburg Nuclear Physics Institute, Gatchina, St. Petersburg, Russian Federation
In this study, we investigated enzymatic deglycosylation of glucoamylase from Aspergillus awamori X 100/D27, a glycoprotein which has two N-linked and about forty short mannose-bearing O-linked sugars per molecule. O-Linked sugars were modified by treatment with α-mannosidase and N-linked sugars were removed using endo-β-N-acetylglucosaminidase F. Analysis of conformational changes following deglycosylation suggests that O-linked sugars essentially contribute to the stabilization of glucoamylase domains. Modification of the carbohydrate component by adding 1-deoxymannojirimycin to the culture medium induced inhibition of α-mannosidases involved in the processing, leading to a more complete glycosylation and, consequently, to a higher stability of the enzyme.
Related record ID(s): 125757 NCBI Taxonomy refs (TaxIDs):105351 Reference(s) to other database(s): GTC:G77553QO, CCSD:25067, CBank-STR:4514 Show glycosyltransferases
There are 3 chemically distinct structures. Please, select:
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