Atomic Force Microscopic Study of Chitinase Binding onto Chitin and Cellulose Surfaces

Kikkawa, Yoshihiro; Fukuda, Masato; Kimura, Tomoe; Kashiwada, Ayumi; Matsuda, Kazuo; Kanesato, Masatoshi; Wada, Masahisa; Imanaka, Tadayuki; Tanaka, Takeshi

doi:10.1021/bm500046f

Cited by 10 publications

(4 citation statements)

References 31 publications

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“…In large number of the contacts there are CH/π interactions; 1054 contacts (55%) have CH/π interactions, while 859 contacts are without CH/π interactions (45%). These data on large number of CH/π interactions is in accordance with an atomic force microscopic study suggesting that the CH/π interaction between the aromatic residues in chitinase from Thermococcus kodakarensis and pyranose ring of chitin/cellulose is the major interaction and that the side chain groups of the polysaccharide do not affect the binding event [26].…”

Section: Geometry and Type Of Carbohydrate/aromatic Interactionssupporting

confidence: 89%

“…The interaction energy between different aromatic rings and simple monosaccharides, based on quantum mechanical calculations in the gas phase ranges from -3.0 to -6.0 kcal/mol [19,24]. It was found that the interactions between carbohydrates and aromatic amino acid side chains are aided by nonconventional hydrogen bonds: the CH/π interactions [19,[25][26][27].…”

Section: Introductionmentioning

confidence: 99%

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Carbohydrate – Protein aromatic ring interactions beyond CH/π interactions: A Protein Data Bank survey and quantum chemical calculations

Stanković

Filipović²,

Zarić

2020

International Journal of Biological Macromolecules

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Section: Geometry and Type Of Carbohydrate/aromatic Interactionssupporting

confidence: 89%

Section: Introductionmentioning

confidence: 99%

Carbohydrate – Protein aromatic ring interactions beyond CH/π interactions: A Protein Data Bank survey and quantum chemical calculations

Stanković

Filipović²,

Zarić

2020

International Journal of Biological Macromolecules

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“…The amino acids residues (His31, Thr32, Trp39, Trp126, and Trp127) in the functional domains of ChBD from CmChi1 are highly conserved, compared with that of reported ChBD (Hashimoto et al, 2000). Among, these residues (His31, Thr32, Trp39, and Trp127) are located on one face of the conformation and are much exposed to the chitin surface ( Supplementary Figure S6), which are proposed to bind with the GlcNAc residues of chitin chains through hydrophobic and π/π interactions (Bernard et al, 2004;Kikkawa et al, 2014).…”

Section: The Effect Of Chbd On 3d Structure Of Cadamentioning

confidence: 95%

Cadaverine Production From L-Lysine With Chitin-Binding Protein-Mediated Lysine Decarboxylase Immobilization

Zhou

Zhang

Wei

et al. 2020

Front. Bioeng. Biotechnol.

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Lysine decarboxylase (CadA) can directly convert L-lysine to cadaverine, which is an important platform chemical that can be used to produce polyamides. However, the non-recyclable and the poor pH tolerance of pure CadA hampered its practical application. Herein, a one-step purification and immobilization procedure of CadA was established to investigate the cadaverine production from L-lysine. Renewable biomass chitin was used as a carrier for lysine decarboxylase (CadA) immobilization via fusion of a chitin-binding domain (ChBD). Scanning electron microscopy, laser scanning confocal microscopy, fourier transform infrared spectra, elemental analysis, and thermal gravimetric analysis proved that the fusion protein ChBD-CadA can be adsorbed on chitin effectively. Furthermore, the fusion protein (ChBD-CadA) existed better pH stability compared to wild CadA, and kept over 73% of the highest activity at pH 8.0. Meanwhile, the ChBD-CadA showed high specificity toward chitin and reached 93% immobilization yield within 10 min under the optimum conditions. The immobilized ChBD-CadA (I-ChBD-CadA) could efficiently converted L-lysine at 200.0 g/L to cadaverine at 135.6 g/L in a batch conversion within 120 min, achieving a 97% molar yield of the substrate L-lysine. In addition, the I-ChBD-CadA was able to be reused under a high concentration of L-lysine and retained over 57% of its original activity after four cycles of use without acid addition to maintain pH. These results demonstrate that immobilization of CadA using chitin-binding domain has the potential in cadaverine production on an industrial scale.

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“…Chitin has a linear structure composed of β-(1-4)-linked 2-deoxy-2-acetamido- d -glucose units (Glu-NHCOCH 3 ) [61,62,63]. After chitin is deacetylated with a degree of deacetylation over 75% the so called chitosan (Glu-NH 2 ) is obtained.…”

Section: Biofibersmentioning

confidence: 99%

A Review on Grafting of Biofibers for Biocomposites

2016

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A recent increase in the use of biofibers as low-cost and renewable reinforcement for the polymer biocomposites has been seen globally. Biofibers are classified into: lignocellulosic fibers (i.e., cellulose, wood and natural fibers), nanocellulose (i.e., cellulose nanocrystals and cellulose nanofibrils), and bacterial cellulose, while polymer matrix materials can be petroleum based or bio-based. Green biocomposites can be produced using both biobased fibers and polymers. Incompatibility between the hydrophilic biofibers and hydrophobic polymer matrix can cause performance failure of resulting biocomposites. Diverse efforts have focused on the modification of biofibers in order to improve the performances of biocomposites. “Grafting” copolymerization strategy can render the advantages of biofiber and impart polymer properties onto it and the performance of biocomposites can be tuned through changing grafting parameters. This review presents a short overview of various “grafting” methods which can be directly or potentially employed to enhance the interaction between biofibers and a polymer matrix for biocomposites. Major grafting techniques, including ring opening polymerization, grafting via coupling agent and free radical induced grafting, have been discussed. Improved properties such as mechanical, thermal, and water resistance have provided grafted biocomposites with new opportunities for applications in specific industries.

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Atomic Force Microscopic Study of Chitinase Binding onto Chitin and Cellulose Surfaces

Cited by 10 publications

References 31 publications

Carbohydrate – Protein aromatic ring interactions beyond CH/π interactions: A Protein Data Bank survey and quantum chemical calculations

Carbohydrate – Protein aromatic ring interactions beyond CH/π interactions: A Protein Data Bank survey and quantum chemical calculations

Cadaverine Production From L-Lysine With Chitin-Binding Protein-Mediated Lysine Decarboxylase Immobilization

A Review on Grafting of Biofibers for Biocomposites

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