Adsorption of α-Chymotrypsin on Plant Biomass Charcoal

Noritomi, Hidetaka; Hishinuma, Keito; Kurihara, Shunichi; Nishigami, Jumpei; Takemoto, Tetsuya; Endo, Nobuyuki; Kato, Satoru

doi:10.4236/jsemat.2013.34036

Cited by 7 publications

(17 citation statements)

References 17 publications

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“…We have found that enzymes are effectively adsorbed onto biomass charcoal powder (Noritomi et al, 2013a;Noritomi et al, 2013b), and biomass charcoal powder imparts high heat stress resistance to enzymes through the adsorption (Noritomi et al, 2011;Noritomi et al, 2012;Noritomi et al, 2014;Noritomi et al, 2016). Furthermore, we have reported that the adsorption of enzymes onto biomass charcoal powder can sufficiently improve the organic solvent resistance of enzymes in hydrophilic organic solvents (Noritomi et al, 2017).…”

Section: Introductionmentioning

confidence: 86%

Influence of Water Activity on Protease Adsorbed on Biochar in Organic Solvents

Noritomi¹,

Nishigami²,

Endo³

et al. 2017

JMSR

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We have found that the organic solvent-resistance of α-chymotrypsin (α-CT) is enhanced by adsorbing α-CT onto bamboo charcoal powder (BCP), which is obtained by pyrolyzing bamboo waste under nitrogen atmosphere, and is markedly dependent on the thermodynamic water activity (a w ) in organic solvents. When BCP-adsorbed α-CT was immersed in acetonitrile at an appropriate water activity, it effectively enhanced the transesterification of Nacetyl-L-tyrosine ethyl ester (N-Ac-Tyr-OEt) with n-butanol (BuOH) to produce N-acetyl-L-tyrosine butyl ester (N-Ac-Tyr-OBu), compared to the hydrolysis of N-Ac-Tyr-OEt with water to give N-acetyl-L-tyrosine (N-Ac-Tyr-OH). When the water activity was 0.28, the initial rate of transesterification catalyzed by BCP-adsorbed α-CT was about sixty times greater than that catalyzed by free α-CT. Regarding the reaction selectivity which is defined as a ratio of the initial rate of transesterification to that of hydrolysis, BCP-adsorbed α-CT was much superior to free α-CT. The catalytic activity of BCP-adsorbed α-CT was markedly dependent on the reaction temperature. Furthermore, concerning the thermal stability at 50 ℃, the half-life of BCP-adsorbed α-CT exhibited 3.8-fold, compared to that of free α-CT.

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Section: Introductionmentioning

confidence: 86%

Influence of Water Activity on Protease Adsorbed on Biochar in Organic Solvents

Noritomi¹,

Nishigami²,

Endo³

et al. 2017

JMSR

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“…Furthermore, the writers have found out that the temperature markedly affects the amount of proteins adsorbed onto BCP [11], [12].…”

Section: Effect Of Temperature Of Adsorption Medium On Thermal Stabilmentioning

confidence: 99%

“…Researches have previously reported that the amount of proteins adsorbed onto BCP is strongly dependent upon the ionic strength of adsorption medium [11], [12]. So as to estimate the influence of ionic strength of adsorption medium on the thermal stability of BCP-adsorbed HEWL, authors have carried out the adsorption of HEWL onto BCP at pH 7 and different KCl concentrations.…”

Section: Effect Of Ionic Strength Of Adsorption Medium On Thermal Stamentioning

confidence: 99%

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Effect of Adsorption Condition on Thermal Stability of Proteins Adsorbed Onto Biomass Charcoal Powder

Noritom¹

2016

geomate

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ABSTRACT:Authors have found out that bamboo charcoal powder (BCP), which is prepared from bamboo wastes by pyrolysis at low temperatures, is very useful as a carrier for the thermal stabilization of proteins. Hen egg white lysozyme (HEWL) and α-chymotrypsin (CT) were effectively adsorbed onto BCP. The thermal stability of BCP-adsorbed HEWL was strongly dependent upon the adsorption conditions such as solution pH, ionic strength, and temperature. Moreover, writers have revealed the heat-resistant mechanism on the basis of the structure of HEWL. Likewise, the thermal stability of BCP-adsorbed CT could be enhanced by selecting the adsorption condition.

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“…We have found out that proteins are effectively adsorbed onto BCP [18], [19], and BCPadsorbed proteins exhibit the enhanced storage stability and the high heat stress resistance in an aqueous solution, compared to free proteins [20]- [23].…”

Section: Introductionmentioning

confidence: 99%

Organic Solvent-Resistant Properties of Proteins Adsorbed Onto Biomass Charcoal Powder

Noritomi¹

2017

GEOMATE

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ABSTRACT:We have found out that biomass charcoal powder (BCP), which is prepared from plant biomass wastes by pyrolysis at low temperatures under nitrogen atmosphere, imparts organic solvent resistance to proteins by using BCP as a protein carrier. α-Chymotrypsin (α-CT), which was used as a model protein, was sufficiently adsorbed onto the surface of BCP. When free α-CT and BCP-adsorbed α-CT were immersed in acetonitrile containing 5%(v/v) water, they catalyzed the transesterification of N-acetyl-L-tyrosine ethyl ester (N-Ac-Tyr-OEt) with n-butanol (BuOH) to produce N-acetyl-L-tyrosine butyl ester (N-Ac-Tyr-OBu), which did not proceed in an aqueous solution, where α-CT worked as a hydrolase. The initial rate of transesterification catalyzed by BCP-adsorbed α-CT was strongly dependent upon the kind of BCP, and was about fifty times higher than that catalyzed by free α-CT when bamboo charcoal powder was used as a carrier.

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Adsorption of α-Chymotrypsin on Plant Biomass Charcoal

Cited by 7 publications

References 17 publications

Influence of Water Activity on Protease Adsorbed on Biochar in Organic Solvents

Influence of Water Activity on Protease Adsorbed on Biochar in Organic Solvents

Effect of Adsorption Condition on Thermal Stability of Proteins Adsorbed Onto Biomass Charcoal Powder

Organic Solvent-Resistant Properties of Proteins Adsorbed Onto Biomass Charcoal Powder

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