scholarly journals Purification, Molecular Cloning, and Enzymatic Properties of a Family 12 Endoglucanase (EG-II) from Fomitopsis palustris: Role of EG-II in Larch Holocellulose Hydrolysis

2008 ◽  
Vol 74 (18) ◽  
pp. 5857-5861 ◽  
Author(s):  
Tomoko Shimokawa ◽  
Hajime Shibuya ◽  
Masanobu Nojiri ◽  
Shigeki Yoshida ◽  
Mitsuro Ishihara
Keyword(s):  
Molecular Mass ◽  
Molecular Cloning ◽  
Cell Walls ◽  
Brown Rot ◽  
Enzymatic Properties ◽  
Wood Degradation ◽  
Fomitopsis Palustris

ABSTRACT A family 12 endoglucanase with a molecular mass of 23,926 Da (EG-II) from the brown-rot basidiomycete Fomitopsis palustris was purified and characterized. One of the roles of EG-II in wood degradation is thought to be to loosen the polysaccharide network in cell walls by disentangling hemicelluloses that are associated with cellulose.

Role of (1,3)(1,4)-β-Glucan in Cell Walls: Interaction with Cellulose

2014 ◽  
Vol 15 (5) ◽  
pp. 1727-1736 ◽  
Author(s):  
Sarah N. Kiemle ◽  
Xiao Zhang ◽  
Alan R. Esker ◽  
Guillermo Toriz ◽  
Paul Gatenholm ◽  
...  
Keyword(s):  
Cell Walls

Etude ultrastructurale des relations hôte–parasite au cours de l'infection des pommes par le Phytophthora cactorum

1981 ◽  
Vol 59 (2) ◽  
pp. 251-263 ◽  
Author(s):  
X. Mourichon ◽  
G. Sallé
Keyword(s):  
Cell Walls ◽  
Susceptible Variety ◽  
Host Cells ◽  
Phytophthora Cactorum ◽  
Electron Microscopic ◽  
Susceptible Host ◽  
Golden Delicious ◽  
Extrahaustorial Matrix ◽  
Apple Fruits

An electron microscopic study was performed on haustoria of Phytophthora cactorum (L. et C.) Schroeter developed in tissues of two cultivars of apple fruits: a susceptible variety ('Golden delicious') and a resistant one ('Belle de Boskoop'). Ultrastructure of intercellular hyphae and some aspects of their penetration between contiguous host cells were described. A light dissolution of the host cell walls was observed. Ontogenic investigations indicated that in the susceptible host, the wall of the fungal haustoria was covered with a dense-stained extrahaustorial matrix. Its origin and its polysaccharide nature were demonstrated. On the other hand, the resistant host developed, immediately after the inoculation, a papilla which gave rise, later on, to a sheath enclosing adult haustoria. The role of these callosic structures in the phenomenon of resistance was discussed.

A metalloproteinase extracellularly released byCrithidia deanei

2003 ◽  
Vol 49 (10) ◽  
pp. 625-632 ◽  
Author(s):  
Claudia Masini d'Avila-Levy ◽  
Rodrigo F Souza ◽  
Rosana C Gomes ◽  
Alane B Vermelho ◽  
Marta H Branquinha
Keyword(s):  
Molecular Mass ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Gel Filtration ◽  
Residual Activity ◽  
Major Protein ◽  
Motile Cells ◽  
Sds Page ◽  
Triton X

Actively motile cells from a cured strain of Crithidia deanei released proteins in phosphate buffer (pH 7.4). The molecular mass of the released polypeptides, which included some proteinases, ranged from 19 to 116 kDa. One of the major protein bands was purified to homogeneity by a combination of anion-exchange and gel filtration chromatographs. The apparent molecular mass of this protein was estimated to be 62 kDa by sodium dodecyl sulfate – polyacrylamide gel electrophoresis (SDS–PAGE). The incorporation of gelatin into SDS–PAGE showed that the purified protein presented proteolytic activity in a position corresponding to a molecular mass of 60 kDa. The enzyme was optimally active at 37 °C and pH 6.0 and showed 25% of residual activity at 28 °C for 30 min. The proteinase was inhibited by 1,10-phenanthroline and EDTA, showing that it belonged to the metalloproteinase class. A polyclonal antibody to the leishmanial gp63 reacted strongly with the released C. deanei protease. After Triton X-114 extraction, an enzyme similar to the purified metalloproteinase was detected in aqueous and detergent-rich phases. The detection of an extracellular metalloproteinase produced by C. deanei and some other Crithidia species suggests a potential role of this released enzyme in substrate degradation that may be relevant to the survival of trypanosomatids in the host.Key words: endosymbiont, trypanosomatid, extracellular, proteinase.

scholarly journals Role of chemokines and cytokines in a reactivation model of arthritis in rats induced by injection with streptococcal cell walls

1998 ◽  
Vol 63 (3) ◽  
pp. 359-363 ◽  
Author(s):  
D. J. Schrier ◽  
R. C. Schimmer ◽  
C. M. Flory ◽  
D. K.-L. Tung ◽  
P. A. Ward
Keyword(s):  
Cell Walls

The role of low-molecular-mass electrolyte drug substances in the modification of the chitosan matrix

2015 ◽  
Vol 57 (3) ◽  
pp. 244-251 ◽  
Author(s):  
E. I. Kulish ◽  
A. S. Shurshina ◽  
V. V. Chernova ◽  
V. P. Zakharov
Keyword(s):  
Molecular Mass ◽  
Chitosan Matrix ◽  
Drug Substances

scholarly journals The role of benzoate secreted by Desulfotomaculum acetoxidans DSM 771 in sulfate uptake.

2005 ◽  
Vol 52 (4) ◽  
pp. 797-802
Author(s):  
Lucyna Pawłowska-Cwiek ◽  
Ryszard Pado
Keyword(s):  
Salicylic Acid ◽  
Hydrogen Sulfide ◽  
Aromatic Compound ◽  
Spectrum Analysis ◽  
Cell Walls ◽  
Sulfonic Acid ◽  
Sulfate Uptake ◽  
Diammonium Salt ◽  
Benzoate Derivatives

This work was designed to find the cause of the delay in hydrogen sulfide dissimilation in Desulfotomaculum acetoxidans DSM 771, which is dependent on the sulfate uptake. This bacterium grown without addition of any aromatic compound was shown by spectrum analysis with the methylene method to contain hydroxy-benzoate derivatives. The presence of these compounds was confirmed by HPLC in fractions obtained from cell walls after 15 days of culture. The test with 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) diammonium salt seemed to indicate the presence of peroxidase, which probably oxidized benzoate to its hydroxy derivatives. The test with 5-sulfo-salicylic acid proved the ability of the investigated strain to utilize arylsulfates and to reduce sulfate group to hydrogen sulfide. On the basis of the above data, we propose the following sequence of reactions: 1, benzoate secretion; 2, benzoate hydroxylation; 3, sulfonation of hydroxy-benzoate derivatives.

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