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Analysis of the <i>Salmonella enterica</i> serovar Typhimurium Chitobiose ( <i>chb</i> ) Operon. [PDF]
Hobson K, Higgins M.
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Chitosan Derivatives: Challenges and Opportunities in the Green and Sustainable Transition Era. [PDF]
Morais A +4 more
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How post-translational modifications in pathogenic fungi inform pathogenesis and immune responses. [PDF]
Sahu SR, Specht CA, Levitz SM.
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International Journal of Biological Macromolecules, 2022
In this study, chitin deacetylase from Microbacterium esteraromaticum MCDA02 (MeCDA) was purified by ammonium sulfate precipitation, anion exchange chromatography, and superdex column chromatography. The molecular weight of purified MeCDA was approximately 26 kDa. The optimum pH and temperature of purified MeCDA were 8.0 and 30 °C, respectively.
Minbo Wang, Yichen Huang, Yaowei Fang
exaly +3 more sources
In this study, chitin deacetylase from Microbacterium esteraromaticum MCDA02 (MeCDA) was purified by ammonium sulfate precipitation, anion exchange chromatography, and superdex column chromatography. The molecular weight of purified MeCDA was approximately 26 kDa. The optimum pH and temperature of purified MeCDA were 8.0 and 30 °C, respectively.
Minbo Wang, Yichen Huang, Yaowei Fang
exaly +3 more sources
Carbohydrate Polymers, 2023
Chitin deacetylase (CDA) catalyzing the deacetylation of crystal chitin is a crucial step in the biosynthesis of chitosan, and also a scientific problem to be solved, which restricts the high-value utilization of chitin resources. This study aims to improve the catalytic efficiency of AsCDA from Acinetobacter schindleri MCDA01 by a semi-rational design
Guang, Yang +8 more
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Chitin deacetylase (CDA) catalyzing the deacetylation of crystal chitin is a crucial step in the biosynthesis of chitosan, and also a scientific problem to be solved, which restricts the high-value utilization of chitin resources. This study aims to improve the catalytic efficiency of AsCDA from Acinetobacter schindleri MCDA01 by a semi-rational design
Guang, Yang +8 more
openaire +2 more sources
Shrimp chitin as substrate for fungal chitin deacetylase
Applied Microbiology and Biotechnology, 2001The fungal chitin deacetylases (CDA) studied so far are able to perform heterogeneous enzymatic deacetylation on their solid substrate, but only to a limited extent. Kinetic data show that about 5-10% of the N-acetyl glucosamine residues are deacetylated rapidly. Thereafter enzymatic deacetylation is slow.
N N, Win, W F, Stevens
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Recent Patents on Biotechnology, 2013
Chitin is an extremely insoluble material with very limited industrial use; however it can be deacetylated to soluble chitosan which has a wide range of applications. The enzymatic deacetylation of various chitin samples was investigated using the bacterial chitin deacetylase (CDA), which was partially purified from Alcaligenes sp.
Ahmed, ElMekawy +3 more
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Chitin is an extremely insoluble material with very limited industrial use; however it can be deacetylated to soluble chitosan which has a wide range of applications. The enzymatic deacetylation of various chitin samples was investigated using the bacterial chitin deacetylase (CDA), which was partially purified from Alcaligenes sp.
Ahmed, ElMekawy +3 more
openaire +2 more sources
The chitin deacetylase PoCda7 is involved in the pathogenicity of Pyricularia oryzae
Microbiological Research, 2021The fungal cell wall plays an essential role in maintaining cellular integrity and facing complex and changing environmental conditions. Whether a fungus successfully invades a host depends on whether it evades the plant's innate immune system, which recognizes the conserved components of the fungal cell wall, such as chitin.
Meng-Di, Dai +5 more
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Carbohydrate Polymers, 2019
Chitin deacetylase, an enzyme isolated from Cryptococcus laurentii RY1, catalyzes the hydrolysis of acetamido group of N-acetyl-D-glucosamine unit of chitin. The primary objective of this study was to characterize and comprehend the activation of chitin deacetylase by DMSO. The secondary structure of the protein was determined by circular dichroism(CD).
Soumyadev Sarkar +2 more
exaly +3 more sources
Chitin deacetylase, an enzyme isolated from Cryptococcus laurentii RY1, catalyzes the hydrolysis of acetamido group of N-acetyl-D-glucosamine unit of chitin. The primary objective of this study was to characterize and comprehend the activation of chitin deacetylase by DMSO. The secondary structure of the protein was determined by circular dichroism(CD).
Soumyadev Sarkar +2 more
exaly +3 more sources

