Adsorption and reactions of chitinase and lysozyme on chitin

Skujiņš, J.; Pukite, A. H.; Ad, Mclaren

doi:10.1007/bf01795475

Cited by 34 publications

(14 citation statements)

References 18 publications

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“…Besides specific chitosanases, also cellulases can possess considerable chitosan-cleaving activity (Xia et al, 2008). Furthermore, lysozyme has also been shown to hydrolyze chitin, even if processivity is low when compared to true chitinases (Skujiņš et al, 1973). Cellulases can also bind directly to chitin (Ekborg et al, 2007; Li and Wilson, 2008), but there are no reports of these enzymes actually hydrolyzing the polymers.…”

Section: Introductionmentioning

confidence: 99%

Bacterial chitin degradation—mechanisms and ecophysiological strategies

Beier¹,

Bertilsson²

2013

Front. Microbiol.

384

295

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Chitin is one the most abundant polymers in nature and interacts with both carbon and nitrogen cycles. Processes controlling chitin degradation are summarized in reviews published some 20 years ago, but the recent use of culture-independent molecular methods has led to a revised understanding of the ecology and biochemistry of this process and the organisms involved. This review summarizes different mechanisms and the principal steps involved in chitin degradation at a molecular level while also discussing the coupling of community composition to measured chitin hydrolysis activities and substrate uptake. Ecological consequences are then highlighted and discussed with a focus on the cross feeding associated with the different habitats that arise because of the need for extracellular hydrolysis of the chitin polymer prior to metabolic use. Principal environmental drivers of chitin degradation are identified which are likely to influence both community composition of chitin degrading bacteria and measured chitin hydrolysis activities.

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Section: Introductionmentioning

confidence: 99%

Bacterial chitin degradation—mechanisms and ecophysiological strategies

Beier¹,

Bertilsson²

2013

Front. Microbiol.

384

295

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“…The ChBD-CadA was almost completely immobilized on chitin within 10 min with a maximum specific activity of 86.33 U/mg, which was consistent with our previous result of chitinase (CmChi1) adsorption by chitin. Skujins et al (1973) reported the adsorption reaction between chitin and ChBD in chitinase was very fast and was nearly accomplished within 2 min (Skujins et al, 1973). With extended adsorption time, the concentration of protein adsorbed didn't obviously increase, nor did the specific activity or CadA activity.…”

Section: Simultaneous Purification and Immobilization Of Chbd-cada Bymentioning

confidence: 99%

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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“…The universal buffer: 5 M Na 2 HPO 4; 5 M H 3 BO 3; 3.6 M citric acid; 25 M NaOH; pH 5.5 or 9.5 (Skujins et al, 1973) was used in all assays.…”

Section: Enzyme Assaysmentioning

confidence: 99%

The Efficiency of Viral and Bacterial Entomopathogens Formulated with Chitinase for Biocontrol of Lepidopteran Cabbage Pests

Штерншис

Ovchinnikova

Duzhak

et al. 2002

Archives Of Phytopathology And Plant Protection

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Preparations of Bacillus thuringiensis subspecies galleriae (Bt), Mamestra brassicae nucleopolyhedrovirus (MbNPV) and chitinase were used in laboratory and field experiments to investigate the efficiency of this triple composition against Lepidopteran cabbage pests. Bt subspecies galleriae was shown to be the most relevant among three Bt subspecies against the cabbage moth Mamestra brassicae L. (Lepidoptera: Noctuidae), the diamondback moth, Plutella xyllostella L. (Lepidoptera: Plutellidae) and the large white butterfly, Pieris brassicae L. (Lepidoptera: Pierilidae). Synergistic toxic effect against pests mentioned above was obtained when the Bt and chitinase were used together. M. brassicae larvae on cabbage were much less susceptible to Bt than other pests. It was necessary to include MbNPV in the mixture. Analysis of the different mixtures allowed us to develop the optimal one containing 2.5×10 7 spores ml -1 of Bt, 1×10 7 polyhedra ml -1 of MbNPV and 0.5 mU ml -1 of chitinase. Such triple composition was much more effective against M. brassicae larvae than the mixture of Bt with chitinase and provided simultaneous biological control of all lepidopteran cabbage pests infesting host plants.

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Adsorption and reactions of chitinase and lysozyme on chitin

Cited by 34 publications

References 18 publications

Bacterial chitin degradation—mechanisms and ecophysiological strategies

Bacterial chitin degradation—mechanisms and ecophysiological strategies

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

The Efficiency of Viral and Bacterial Entomopathogens Formulated with Chitinase for Biocontrol of Lepidopteran Cabbage Pests

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