Characterization of a polysaccharide hydrogel with high elasticity produced by a mutant strain Sphingomonas sanxanigenens NX03

2021 ◽  
pp. 119030
Author(s):  
Mengmeng Wu ◽  
Yaqi Shen ◽  
Yue Ming ◽  
Zhuangzhuang Shi ◽  
Zhong Shi ◽  
...  
Keyword(s):  
Mutant Strain ◽  
High Elasticity ◽  
Polysaccharide Hydrogel

Fabrication and characterization of tunable polysaccharide hydrogel blends for neural repair

2011 ◽  
Vol 7 (4) ◽  
pp. 1634-1643 ◽  
Author(s):  
Jonathan M. Zuidema ◽  
Matthew M. Pap ◽  
David B. Jaroch ◽  
Faith A. Morrison ◽  
Ryan J. Gilbert
Keyword(s):  
Neural Repair ◽  
Fabrication And Characterization ◽  
Polysaccharide Hydrogel

Purification and characterization of 4-hydroxybenzoate 3-hydroxylase from a Klebsiella pneumoniae mutant strain

1995 ◽  
Vol 164 (1) ◽  
pp. 70-77
Author(s):  
Mónica Suárez ◽  
M. Martín ◽  
Estrella Ferrer ◽  
Amando Garrido-Pertierra
Keyword(s):  
Klebsiella Pneumoniae ◽  
Mutant Strain ◽  
Purification And Characterization

scholarly journals Characterization of Acp, a Peptidoglycan Hydrolase of Clostridium perfringens with N-Acetylglucosaminidase Activity That Is Implicated in Cell Separation and Stress-Induced Autolysis

2010 ◽  
Vol 192 (9) ◽  
pp. 2373-2384 ◽  
Author(s):  
Emilie Camiade ◽  
Johann Peltier ◽  
Ingrid Bourgeois ◽  
Evelyne Couture-Tosi ◽  
Pascal Courtin ◽  
...  
Keyword(s):  
Mutant Strain ◽  
Clostridium Perfringens ◽  
Vegetative Growth ◽  
Cell Separation ◽  
Catalytic Domain ◽  
Peptidoglycan Hydrolase ◽  
Wild Type ◽  
Induced Autolysis

ABSTRACT This work reports the characterization of the first known peptidoglycan hydrolase (Acp) produced mainly during vegetative growth of Clostridium perfringens. Acp has a modular structure with three domains: a signal peptide domain, an N-terminal domain with repeated sequences, and a C-terminal catalytic domain. The purified recombinant catalytic domain of Acp displayed lytic activity on the cell walls of several Gram-positive bacterial species. Its hydrolytic specificity was established by analyzing the Bacillus subtilis peptidoglycan digestion products by coupling reverse phase-high-pressure liquid chromatography (RP-HPLC) and matrix-assisted laser desorption ionization-time of flight mass spectrometry (MALDI-TOF MS) analysis, which displayed an N-acetylglucosaminidase activity. The study of acp expression showed a constant expression during growth, which suggested an important role of Acp in growth of C. perfringens. Furthermore, cell fractionation and indirect immunofluorescence staining using anti-Acp antibodies revealed that Acp is located at the septal peptidoglycan of vegetative cells during exponential growth phase, indicating a role in cell separation or division of C. perfringens. A knockout acp mutant strain was obtained by using the insertion of mobile group II intron strategy (ClosTron). The microscopic examination indicated a lack of vegetative cell separation in the acp mutant strain, as well as the wild-type strain incubated with anti-Acp antibodies, demonstrating the critical role of Acp in cell separation. The comparative responses of wild-type and acp mutant strains to stresses induced by Triton X-100, bile salts, and vancomycin revealed an implication of Acp in autolysis induced by these stresses. Overall, Acp appears as a major cell wall N-acetylglucosaminidase implicated in both vegetative growth and stress-induced autolysis.

Screening and characterization of an Agrobacterium tumefaciens mutant strain producing high level of coenzyme Q10

2015 ◽  
Vol 50 (1) ◽  
pp. 33-39 ◽  
Author(s):  
Tae-Su Kim ◽  
Ji-Hyun Yoo ◽  
Sang-Yong Kim ◽  
Cheol-Ho Pan ◽  
Vipin C. Kalia ◽  
...  
Keyword(s):  
Agrobacterium Tumefaciens ◽  
Mutant Strain ◽  
Coenzyme Q10 ◽  
High Level
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