scholarly journals Effect of N-acetyl substitution at the amino sugar residues on PL-1 muramidase-catalyzed hydrolysis of cell wall peptidoglycan of Lactobacillus casei.

1986 ◽  
Vol 50 (10) ◽  
pp. 2685-2687 ◽  
Author(s):  
Mikie HAYASHIDA ◽  
Kenji WATANABE
1973 ◽  
Vol 51 (6) ◽  
pp. 1147-1153 ◽  
Author(s):  
James L. Harris ◽  
Willard A. Taber

The composition of the cell walls of synnemal and vegetative hyphae of Ceratocystis ulmi was studied by fractionation and assay of released compounds. Residues after enzymatic hydrolyses were examined by electron microscopy. The synnemal wall was found to have 67% carbohydrate, 4.52% amino sugar, 5.02% protein, 1.6% lipid, and 0.59% ash, which accounted for 78.7% of the cell wall. The vegetative hyphal wall contained 56% carbohydrate, 3.44% amino sugar, 7.92% protein, 4.5% lipid, and 1.45% ash, which totaled 73.3% of the wall weight. Sugars identified were D-glucose, D-mannose, D-galactose, and L-rhamnose. Enzymatic hydrolysis of both wall types by cellulase and laminaranase indicated the presence of beta-1,3 and beta-1,4 linkages of glucose polymers. N-acetylglucosamine was liberated by chitinase. Most of the 16 amino acids detected in each wall type were at least twice as abundant in vegetative hyphal walls as in synnemal hyphal walls. Cellulase and laminaranase treatment of cell walls revealed a fibrillar structure. Chitinase-treated walls did not appear as fibrous, suggesting that the fibrous structure may be mostly chitinous. Synnemal cell walls are covered by electron-dense granules which may correspond to the pigment in the synnemal hyphae.


2010 ◽  
Vol 9 (11) ◽  
pp. 1650-1660 ◽  
Author(s):  
Encarnación Dueñas-Santero ◽  
Ana Belén Martín-Cuadrado ◽  
Thierry Fontaine ◽  
Jean-Paul Latgé ◽  
Francisco del Rey ◽  
...  

ABSTRACT In yeast, enzymes with β-glucanase activity are thought to be necessary in morphogenetic events that require controlled hydrolysis of the cell wall. Comparison of the sequence of the Saccharomyces cerevisiae exo-β(1,3)-glucanase Exg1 with the Schizosaccharomyces pombe genome allowed the identification of three genes that were named exg1 + (locus SPBC1105.05), exg2 + (SPAC12B10.11), and exg3 + (SPBC2D10.05). The three proteins have different localizations: Exg1 is secreted to the periplasmic space, Exg2 is a membrane protein, and Exg3 is a cytoplasmic protein. Characterization of the biochemical activity of the proteins indicated that Exg1 and Exg3 are active only against β(1,6)-glucans while no activity was detected for Exg2. Interestingly, Exg1 cleaves the glucans with an endohydrolytic mode of action. exg1 + showed periodic expression during the cell cycle, with a maximum coinciding with the septation process, and its expression was dependent on the transcription factor Sep1. The Exg1 protein localizes to the septum region in a pattern that was different from that of the endo-β(1,3)-glucanase Eng1. Overexpression of Exg2 resulted in an increase in cell wall material at the poles and in the septum, but the putative catalytic activity of the protein was not required for this effect.


RSC Advances ◽  
2017 ◽  
Vol 7 (76) ◽  
pp. 48444-48453 ◽  
Author(s):  
Benjarat Bunterngsook ◽  
Thanaporn Laothanachareon ◽  
Suda Natrchalayuth ◽  
Sirithorn Lertphanich ◽  
Tatsuya Fujii ◽  
...  

Cassava pulp is an underused agricultural by-product comprising residual starch granules entrapped in cell wall polysaccharides, making it unique from other lignocellulosic wastes in terms of enzymatic processing.


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