Uncoupling chitosanase production from chitosan

Brzeziński, Ryszard

doi:10.4161/bbug.2.4.16111

Cited by 9 publications

(3 citation statements)

References 23 publications

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“…Chitosan is a deacetylated product of chitin consisting of a polymer of N ‐acetyl glucosamine that is generally thought to contain more than 50% glucosamine (GlcN). Chitosanases (EC 3.2.1.132) hydrolyse chitosan into oligomers and dimers of GlcN; hence, they are useful for producing chitooligosaccharides and GlcN for use in the food and pharmacological industries . Chitosanases belong to glycoside hydrolase (GH) families 5, 7, 8, 46, 75 and 80, based on the classification of Henrissat .…”

Section: Characteristics Of Mcchoa Chitosanase From Mitsuaria Chitosamentioning

confidence: 99%

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Crystal structure of a family 80 chitosanase from Mitsuaria chitosanitabida

et al. 2017

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Chitosanases belong to glycoside hydrolase families 5, 7, 8, 46, 75 and 80 and hydrolyse glucosamine polymers produced by partial or full deacetylation of chitin. Herein, we determined the crystal structure of chitosanase from the β-proteobacterium, Mitsuaria chitosanitabida, (McChoA) at 1.75 Å resolution; the first structure of a family 80 chitosanase. McChoA is a 34 kDa extracellular protein of 301 amino acids that fold into two (upper and lower) globular domains with an active site cleft between them. Key substrate-binding features are conserved with family 24 lysozymes and family 46 chitosanases. The distance between catalytic residues E41 and E61 (10.8 Å) indicates an inverting type mechanism. Uniquely, three disulphide bridges and the C terminus might contribute to enzyme activity.

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Section: Characteristics Of Mcchoa Chitosanase From Mitsuaria Chitosamentioning

confidence: 99%

“…GlcN for use in the food and pharmacological industries [1,2]. Chitosanases belong to glycoside hydrolase (GH) families 5,7,8,46, 75 and 80, based on the classification of Henrissat [3].…”

Section: Abstract: Chitosan; Chitosanase; Crystal Structure; Mitsuariamentioning

confidence: 99%

Crystal structure of a family 80 chitosanase from Mitsuaria chitosanitabida

et al. 2017

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“…Chitosanases, enzymes that catalyze the endo-hydrolysis of glycolytic links in chitosan, belong to glycoside hydrolase families. They are useful for producing chit oligosaccharides a GlcN using in the food and pharmacological industries [1,2]. Chitosanases EAG1 is a classical glycoside hydrolase from Bacillus ehimensis.…”

Section: Introductionmentioning

confidence: 99%

A Study of the Structural Properties and Thermal Stability of Chitosanases EAG1 by Molecular Dynamics Simulations

Li¹,

Xu²,

Xu³

2018

JBiSE

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Chitosanases EAG1, a classical glycoside hydrolase from Bacillus ehimensis, is relatively unstable with higher temperature. This shortcoming seriously restricts its industrial application. Therefore, it is crucial to clarify the theoretical basis of thermo stability and to produce enzymes with high activity and stability. Using the structural modeling and molecular dynamical simulation, residues Leu84, Gly113, Asp116, Ala207 and Leu286 were believed to be the key residues for structural stability. Then the predicted residue Leu84 was mutated to ALA. It was shown that the L84A mutation can improve the thermal stability of chitosanases EAG1. Together with previous studies, mutations of G113C, D116C, A207C and L286C forms two sulfur bonds can change the thermal stability of EAG1. The results suggest that the thermal stability of EAG1 could be engineered by site-directed mutagenesis on the conserved residues. This protocol could be employed for improving thermal stability of other chitosanases EAG1.

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Diversity of family GH46 chitosanases in Kitasatospora setae KM-6054

Zitouni

Viens

Ghinet

et al. 2017

Appl Microbiol Biotechnol

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The genome of Kitasatospora setae KM-6054, a soil actinomycete, has three genes encoding chitosanases belonging to GH46 family. The genes (csn1-3) were cloned in Streptomyces lividans and the corresponding enzymes were purified from the recombinant cultures. The csn2 clone yielded two proteins (Csn2BH and Csn2H) differing by the presence of a carbohydrate-binding domain. Sequence analysis showed that Csn1 and Csn2H were canonical GH46 chitosanases, while Csn3 resembled chitosanases from bacilli. The activity of the four chitosanases was tested in a variety of conditions and on diverse chitosan forms, including highly N-deacetylated chitosan or chitosan complexed with humic or polyphosphoric acid. Kinetic parameters were also determined. These tests unveiled the biochemical diversity among these chitosanases and the peculiarity of Csn3 compared with the other three enzymes. The observed biochemical diversity is discussed based on structural 3D models and sequence alignment. This is a first study of all the GH46 chitosanases produced by a single microbial strain.

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Uncoupling chitosanase production from chitosan

Cited by 9 publications

References 23 publications

Crystal structure of a family 80 chitosanase from Mitsuaria chitosanitabida

Crystal structure of a family 80 chitosanase from Mitsuaria chitosanitabida

A Study of the Structural Properties and Thermal Stability of Chitosanases EAG1 by Molecular Dynamics Simulations

Diversity of family GH46 chitosanases in Kitasatospora setae KM-6054

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