Aggregability of β(1→4)-linked glucosaminoglucan originating from a sulfur-oxidizing bacterium Thiothrix nivea

Aggregability of β(1→4)-linked glucosaminoglucan originating from a sulfur-oxidizing bacterium Thiothrix nivea

β-1,4-glucosaminoglucan (GG) was prepared from the sheath of a sulfur-oxidizing bacterium Thiothrix nivea. Recently, GG was found to be adsorbed by cellulose (paper) and is therefore potentially applicable as an aminating agent for cellulose. We attempted to increase the yield of GG using a fed-batc...

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Published in:Bioscience, biotechnology, and biochemistry Vol. 84; no. 10; pp. 2085 - 2095
Main Authors: Takeda, Minoru, Kondo, Keiko, Tominaga, Ryo, Mori, Honomi, Kato, Mana, Usami, Ryoji, Murakami, Tomoi, Ueda, Kazuyoshi, Suzuki, Ichiro, Katahira, Masato
Format: Journal Article
Language:English
Published: England Taylor & Francis 02-10-2020
Oxford University Press
Subjects:
adsorption
aggregation
cellulose
Glucosaminoglucan
Glycosaminoglycans - chemistry
Glycosaminoglycans - metabolism
Molecular Weight
Oxidation-Reduction
Solubility
Sulfur - metabolism
Thiothrix - metabolism
Thiothrix nivea
Glucosaminoglucan
adsorption
aggregation
cellulose
Thiothrix nivea
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Summary:β-1,4-glucosaminoglucan (GG) was prepared from the sheath of a sulfur-oxidizing bacterium Thiothrix nivea. Recently, GG was found to be adsorbed by cellulose (paper) and is therefore potentially applicable as an aminating agent for cellulose. We attempted to increase the yield of GG using a fed-batch cultivation method. Furthermore, the behavior of GG molecules in water was theoretically and experimentally investigated. NMR analysis in combination with molecular dynamics calculation suggested that GG molecules tend to form soluble aggregates in water. It was experimentally revealed that the self-aggregation is enhanced by the addition of NaCl and reduced temperature. Adsorption of GG onto cellulose via hydrogen bonding was confirmed by molecular dynamics simulation. Adsorption was also promoted in the presence of NaCl but was inhibited by a reduction in temperature. Only 11% of the amino groups in the GG-treated paper was reactive, suggesting that GG molecules adsorbed by the paper were forming aggregates. Attachment of glucosaminoglucan chains and their self-aggregates to cellulose crystalline assemblage via hydrogen bond during molecular dynamics simulation.
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content type line 23
ISSN:0916-8451
1347-6947
DOI:10.1080/09168451.2020.1785838