Chemical modification causes similar change in dependence on water activity of chymotrypsin hydration and catalysis in hexane

D.G. Rees, ll. Gerashchenko, E.V. Kudryashova, V.V. Mozhaev, P.J. Halling

Research output: Contribution to journal › Article

7 Citations (Scopus)

Abstract

Amino groups in alpha-chymotrypsin were reacted with pyromellitic anhydride, introducing 17 to 32 additional carboxyl groups. This modification causes a major change in the water adsorption isotherm of the lyophilized protein powder. Little water is bound by the modified enzyme at water activity (a(w)) below 0.35, but it shows increased water binding at a(w) over 0.5. This correlates with a similar change in the a(w) dependence of the catalytic activity of the enzyme powder suspended in hexane, with a much steeper increase in activity of the modified chymotrypsin.
Original languageEnglish
Pages (from-to)161-166
Number of pages5
JournalBiocatalysis and Biotransformation
Volume20
Issue number3
DOIs
Publication statusPublished - Jun 2002

Fingerprint

Chemical modification
Chymotrypsin
Hexanes
Hexane
Catalysis
Hydration
Thermodynamic properties
Water
Powders
Enzymes
Anhydrides
Adsorption isotherms
Adsorption
Catalyst activity
Proteins

Keywords

  • water adsorption
  • low-water nonpolar media
  • chymotrypsin
  • chemical modification
  • pyromellitic acid
  • Organic media
  • alpha-chymotrypsin
  • enzyme-activity
  • stability
  • solvents
  • protein
  • esterification

Cite this

Rees, D.G. ; Gerashchenko, ll. ; Kudryashova, E.V. ; Mozhaev, V.V. ; Halling, P.J. / Chemical modification causes similar change in dependence on water activity of chymotrypsin hydration and catalysis in hexane. In: Biocatalysis and Biotransformation. 2002 ; Vol. 20, No. 3. pp. 161-166.
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abstract = "Amino groups in alpha-chymotrypsin were reacted with pyromellitic anhydride, introducing 17 to 32 additional carboxyl groups. This modification causes a major change in the water adsorption isotherm of the lyophilized protein powder. Little water is bound by the modified enzyme at water activity (a(w)) below 0.35, but it shows increased water binding at a(w) over 0.5. This correlates with a similar change in the a(w) dependence of the catalytic activity of the enzyme powder suspended in hexane, with a much steeper increase in activity of the modified chymotrypsin.",
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author = "D.G. Rees and ll. Gerashchenko and E.V. Kudryashova and V.V. Mozhaev and P.J. Halling",
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Rees, DG, Gerashchenko, L, Kudryashova, EV, Mozhaev, VV & Halling, PJ 2002, 'Chemical modification causes similar change in dependence on water activity of chymotrypsin hydration and catalysis in hexane', Biocatalysis and Biotransformation, vol. 20, no. 3, pp. 161-166. https://doi.org/10.1080/10242420290020688

Chemical modification causes similar change in dependence on water activity of chymotrypsin hydration and catalysis in hexane. / Rees, D.G.; Gerashchenko, ll.; Kudryashova, E.V.; Mozhaev, V.V.; Halling, P.J.

In: Biocatalysis and Biotransformation, Vol. 20, No. 3, 06.2002, p. 161-166.

Research output: Contribution to journal › Article

TY - JOUR

T1 - Chemical modification causes similar change in dependence on water activity of chymotrypsin hydration and catalysis in hexane

AU - Rees, D.G.

AU - Gerashchenko, ll.

AU - Kudryashova, E.V.

AU - Mozhaev, V.V.

AU - Halling, P.J.

PY - 2002/6

Y1 - 2002/6

N2 - Amino groups in alpha-chymotrypsin were reacted with pyromellitic anhydride, introducing 17 to 32 additional carboxyl groups. This modification causes a major change in the water adsorption isotherm of the lyophilized protein powder. Little water is bound by the modified enzyme at water activity (a(w)) below 0.35, but it shows increased water binding at a(w) over 0.5. This correlates with a similar change in the a(w) dependence of the catalytic activity of the enzyme powder suspended in hexane, with a much steeper increase in activity of the modified chymotrypsin.

AB - Amino groups in alpha-chymotrypsin were reacted with pyromellitic anhydride, introducing 17 to 32 additional carboxyl groups. This modification causes a major change in the water adsorption isotherm of the lyophilized protein powder. Little water is bound by the modified enzyme at water activity (a(w)) below 0.35, but it shows increased water binding at a(w) over 0.5. This correlates with a similar change in the a(w) dependence of the catalytic activity of the enzyme powder suspended in hexane, with a much steeper increase in activity of the modified chymotrypsin.

KW - water adsorption

KW - low-water nonpolar media

KW - chymotrypsin

KW - chemical modification

KW - pyromellitic acid

KW - Organic media

KW - alpha-chymotrypsin

KW - enzyme-activity

KW - stability

KW - solvents

KW - protein

KW - esterification

UR - http://dx.doi.org/10.1080/10242420290020688

U2 - 10.1080/10242420290020688

DO - 10.1080/10242420290020688

M3 - Article

VL - 20

SP - 161

EP - 166

JO - Biocatalysis and Biotransformation

JF - Biocatalysis and Biotransformation

SN - 1024-2422

IS - 3

ER -

Rees DG, Gerashchenko L, Kudryashova EV, Mozhaev VV, Halling PJ. Chemical modification causes similar change in dependence on water activity of chymotrypsin hydration and catalysis in hexane. Biocatalysis and Biotransformation. 2002 Jun;20(3):161-166. https://doi.org/10.1080/10242420290020688

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