Chitosan-Soyprotein Interaction as Determined by Thermal Unfolding Experiments

Takeuchi, Tomoko; Morita, Kazuhisa; Saito, Tsutomu; Kugimiya, Wataru; Fukamizo, Tamo

doi:10.1271/bbb.60015

Cited by 11 publications

(9 citation statements)

References 19 publications

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“…The results clearly indicated the protein channel was more resistant to thermal denaturation when bound to its sugar substrates, the degree of heat tolerance being greater with increasing binding affinity. Such observations have been reported in previous studies: for example, it was shown by Fukamizo's group that chitosan hexamer helped to stabilize the structure of the glucosamine-recognizing β3 conglycinin from soybean [37].…”

Section: Discussionsupporting

confidence: 83%

Vibrio campbellii chitoporin: Thermostability study and implications for the development of therapeutic agents against Vibrio infections

Aunkham

Schulte

Sim

et al. 2020

International Journal of Biological Macromolecules

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Vibrio campbellii (formerly Vibrio harveyi) is a bacterial pathogen that causes vibriosis, which devastates fisheries and aquaculture worldwide. V. campbellii expresses chitinolytic enzymes and chitin binding/transport proteins, which serve as excellent targets for antimicrobial agent development. We previously characterized VhChiP, a chitooligosaccharide-specific porin from the outer membrane of V. campbellii BAA-1116. This study employed far-UV circular dichroism and tryptophan fluorescence spectroscopy, together with single channel electrophysiology to demonstrate that the strong binding of chitoligosaccharides enhanced thermal stability of VhChiP. The alanine substitution of Trp 136 at the center of the affinity sites caused a marked decrease in the binding affinity and decreased the thermal stability of VhChiP. Tryptophan fluorescence titrations over a range of temperatures showed greater free-energy changes on ligand binding (Gbinding) with increasing chain length of the chitooligosaccharides. Our findings suggest the possibility of designing stable channel-blockers, using sugar-based analogs that serve as antimicrobial agents, active against Vibrio infection.

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Section: Discussionsupporting

confidence: 83%

Vibrio campbellii chitoporin: Thermostability study and implications for the development of therapeutic agents against Vibrio infections

Aunkham

Schulte

Sim

et al. 2020

International Journal of Biological Macromolecules

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“…The results clearly indicated the protein channel 303 was more resistant to thermal denaturation when bound to its sugar substrates, the degree of heat tolerance 304 being greater with increasing binding affinity. Such observations have been reported in previous studies: 305 for example, it was shown by Fukamizo's group that chitosan hexamer helped to stabilize the structure of 306 the glucosamine-recognizing β3 conglycinin from soybean [37].…”

supporting

confidence: 71%

Vibrio campbelliichitoporin: thermostability study and implications for the development of therapeutic agents againstVibrioinfections

Aunkham

Schulte

Sim

et al. 2020

Preprint

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1Vibrio campbellii (formerly Vibrio harveyi) is a bacterial pathogen that causes vibriosis, which 2 devastates fisheries and aquaculture worldwide. V. campbellii expresses chitinolytic enzymes and chitin 3 binding/transport proteins, which serve as excellent targets for antimicrobial agent development. We 4 previously characterized VhChiP, a chitooligosaccharide-specific porin from the outer membrane of V. 5 campbellii BAA-1116. This study employed far-UV circular dichroism and tryptophan fluorescence 6 spectroscopy, together with single channel electrophysiology to demonstrate that the strong binding of 7 chitoligosaccharides enhanced thermal stability of VhChiP. The alanine substitution of Trp 136 at the center 8 of the affinity sites caused a marked decrease in the binding affinity and decreased the thermal stability of 9 VhChiP. Tryptophan fluorescence titrations over a range of temperatures showed greater free-energy 10 changes on ligand binding (Gbinding) with increasing chain length of the chitooligosaccharides. Our 11 findings suggest the possibility of designing stable channel-blockers, using sugar-based analogs that serve 12 as antimicrobial agents, active against Vibrio infection. 13 14 Introduction 15Chitin is a natural, insoluble polysaccharide composed of repeating units of N-acetylglucosamine 16 (GlcNAc) linked by -1,4-glycosidic linkages, and is primarily found in the cell walls of fungi and the 17 exoskeletons of arthropods and crustaceans. Global demand for seafoods has promoted shellfish cultivation 18 worldwide, with the total world crab production, for instance, being over 200 million tons in 2016 as 19 reported by World Food Program (WFP) (https://www.wfp.org/). Since a large portion of the weight of a 20 crustacean is inedible, the shellfish farming and processing industry produces approximately 6 -8 million 21 tons of waste shells worldwide annually, of which 1.5 million is contributed by Southeast Asia. These waste 22 shells, which contain 20 -58% chitin, are often simply discarded, either in the ocean or into landfills. 23 Although chitin is biodegradable, its natural components are refractory to degradation by naturally 24 occurring enzymes, which has led to its accumulation over time and poses a serious threat to coastal 25 ecosystems [1,2,3,4]. Chitin has received much attention in recent years from entrepreneurs and researchers 26 who are working on eco-friendly technology for the development of renewable bioenergy, biomedicine and 27 biotechnology. Chitin serves as a suitable biomaterial because of its low cost but high availability as waste 28 biomass and its excellent biocompatibility. Chitin is therefore regarded as a sustainable future energy source 29 and an alternative to depleting non-renewable fossil fuel resources. Previous reports showed that the 30 chitinolytic bacteria Aeromonas hydrophila and Bacillus circulans can be used in microbial fuel cells for 31 electricity generation. [5,6]. In other applications, accelerating the biodegradation of chitin will not only 32 re...

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“…The increase in the thermal unfolding temperature of the enzyme in the presence of chitosan was attributed to the stabilization of protein through electrostatic interaction with chitosan. 12 At pH > pI, where protein and chitosan have opposite charges, complex formation of faba bean legumin 13 with chitosan gave a small positive enthalpy change in contrast to the strongly exothermic interaction of chitosan with -lactoglobulin. 14 However, these variable observations do not preclude predominantly electrostatic interaction: Schaaf and co-workers 15 showed that complexation of oppositely charge polyelectrolytes can be either exothermic or endothermic.…”

Section: Introductionmentioning

confidence: 99%

Effect of Polyelectrolyte Structure on Protein−Polyelectrolyte Coacervates: Coacervates of Bovine Serum Albumin with Poly(diallyldimethylammonium chloride) versus Chitosan

et al. 2007

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Electrostatic interactions between synthetic polyelectrolytes and proteins can lead to the formation of dense, macroion-rich liquid phases, with equilibrium microheterogeneities on length scales up to hundreds of nanometers. The effects of pH and ionic strength on the rheological and optical properties of these coacervates indicate microstructures sensitive to protein-polyelectrolyte interactions. We report here on the properties of coacervates obtained for bovine serum albumin (BSA) with the biopolyelectrolyte chitosan and find remarkable differences relative to coacervates obtained for BSA with poly(diallyldimethylammonium chloride) (PDADMAC). Coacervation with chitosan occurs more readily than with PDADMAC. Viscosities of coacervates obtained with chitosan are more than an order of magnitude larger and, unlike those with PDADMAC, show temperature and shear rate dependence. For the coacervates with chitosan, a fast relaxation time in dynamic light scattering, attributable to relatively unrestricted protein diffusion in both systems, is diminished in intensity by a factor of 3-4, and the consequent dominance by slow modes is accompanied by a more heterogeneous array of slow apparent diffusivities. In place of a small-angle neutron scattering Guinier region in the vicinity of 0.004 Å -1 , a 10-fold increase in scattering intensity is observed at lower q. Taken together, these results confirm the presence of dense domains on length scales of hundreds of nanometers to micrometers, which in coacervates prepared with chitosan are less solidlike, more interconnected, and occupy a larger volume fraction. The differences in properties are thus correlated with differences in mesophase structure.

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Chitosan-Soyprotein Interaction as Determined by Thermal Unfolding Experiments

Cited by 11 publications

References 19 publications

Vibrio campbellii chitoporin: Thermostability study and implications for the development of therapeutic agents against Vibrio infections

Vibrio campbellii chitoporin: Thermostability study and implications for the development of therapeutic agents against Vibrio infections

Vibrio campbelliichitoporin: thermostability study and implications for the development of therapeutic agents againstVibrioinfections

Effect of Polyelectrolyte Structure on Protein−Polyelectrolyte Coacervates: Coacervates of Bovine Serum Albumin with Poly(diallyldimethylammonium chloride) versus Chitosan

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