Results 161 to 170 of about 59,813 (190)

Purification and characterization of chitin deacetylase active on insoluble chitin from Nitratireductor aquimarinus MCDA3-3

International Journal of Biological Macromolecules, 2020
The chitin deacetylase produced by marine strain Nitratireductor aquimarinus MCDA3-3 (NaCDA) was purified by using ammonium sulfate precipitation, Q Sepharose, and Superdex column chromatography. The purified NaCDA showed 75-fold purity, 50 U/mg specific activity with 28.5% yield. The purified CDA molecular weight was about 36 kDa.
Jinlong, Chai, Jiahao, Hang, Chunguang, Zhang, Jie, Yang, Shujun, Wang, Shu, Liu, Yaowei, Fang   +6 more
openaire   +2 more sources

A search of an optimal carrier for immobilization of chitin deacetylase

Cellulose, 2008
Chitin deacetylase is an enzyme that can play an important role in enzymatic deacetylation of chitosan to obtain polymers with a lower degree of acetylation. As this enzyme has never been immobilized up to now, efforts were directed towards determining both the most suitable carrier and the best method of covalent attachment to the selected carrier. In
Małgorzata M. Jaworska, Jolanta Bryjak, Jolanta Liesiene   +2 more
openaire   +1 more source

A comprehensive account of fungal chitin deacetylases: Aspects and prospects

International Journal of Biological Macromolecules
Chitin deacetylases (CDA, EC 3.5.1.41), found in bacteria, insects and fungi, are the only enzymes in nature that catalyzes the conversion of chitin (polymer of N-acetyl-β-D-glucosamine) to chitosan (polymer of β-D-glucosamine). Presently, the commercial production of chitosan involves using harsh chemicals at high temperatures, causing pollution ...
Namrata, Raghavan, Ejaj K, Pathan
openaire   +2 more sources

Cloning and Expression of Two Chitin Deacetylase Genes ofSaccharomyces cerevisiae

Yeast, 1997
Chitin deacetylase (EC 3.5.1.41), which hydrolyses the N-acetamido groups of N-acetyl-D-glucosamine residues in chitin, has been demonstrated in crude extracts from sporulating Saccharomyces cerevisiae. Two S. cerevisiae open reading frames (ORFs), identified by the Yeast Genome Project, have protein sequence homology to a chitin deacetylase from Mucor
C, Mishra, C E, Semino, K J, McCreath, H, de la Vega, B J, Jones, C A, Specht, P W, Robbins   +6 more
openaire   +2 more sources

Chitinase and Deacetylase-Based Chitin-Degrading Bacteria: One-Pot Cascade Bioconversion of Chitin to Chitooligosaccharides

Journal of Agricultural and Food Chemistry
Cascade conversion of chitin into soluble and functional chitooligosaccharides has gained great attention. However, the biotransformation route is still limited to the low catalytic performances of chitin deacetylases (CDAs) and complicated procedures. In this study, a CDA from Arthrobacter sp.
Liwei Qing, Jing Gao, Liuhuan Du, Yiying Liu, Na Guo, Jianan Sun, Hao Dong, Xiangzhao Mao   +7 more
openaire   +2 more sources

Screening and identification of novel chitin deacetylases for the sustainable valorisation of chitin

Chitin is one of the most abundant organic molecules after lignocellulose, yearly produced in nature in the range of 1010-1011 tons. However, its direct applications are mainly restricted to low value-added products (e.g., animal feed and agricultural fertilizers) because of the high crystallinity and inflexibility of its structure.
Melissa Bisaccia, Ana Šimatović, Immacolata Serra, Elisa Margherita Maffioli, Gabriella Tedeschi, Flavia Marinelli, Francesca Berini   +6 more
openaire   +1 more source

Chitin deacetylase

1991
Dietmar Schomburg, Margit Salzmann
openaire   +1 more source

Expression and Molecular Modification of Chitin Deacetylase from Streptomyces bacillaris

Molecules, 2023
Xiangzhao Mao, Jianan Sun
exaly  

Chitin deacetylase

1988
Yoshio Araki, Eiji Ito
openaire   +1 more source

Rationally engineered chitin deacetylase from Arthrobacter sp. AW19M34-1 with improved catalytic activity toward crystalline chitin

Carbohydrate Polymers, 2021
Yaowei Fang, Sibtain Ahmed
exaly