TY - JOUR
T1 - Low reaction temperature increases the selectivity in an enzymatic reaction due to substrate solvation effects
AU - Jönsson, Åsa
AU - Wehtje, Ernst
AU - Adlercreutz, Patrick
PY - 1997/3/8
Y1 - 1997/3/8
N2 - Immobilized α-chymotrypsin was used as catalyst for studying temperature effects on acyl transfer reactions (acyl-donor: Bz-TyrOEt) in a water-immiscible organic solvent. The solubility of the two nucleophiles, Phe-NH2 and water, decreased with decreasing temperature. The relative decrease for the amide was larger (2.4-fold) than for water. Therefore the thermodynamic activity (estimated by the relative saturation) increased more for this substrate and hence the selectivity in the reaction was increased.
AB - Immobilized α-chymotrypsin was used as catalyst for studying temperature effects on acyl transfer reactions (acyl-donor: Bz-TyrOEt) in a water-immiscible organic solvent. The solubility of the two nucleophiles, Phe-NH2 and water, decreased with decreasing temperature. The relative decrease for the amide was larger (2.4-fold) than for water. Therefore the thermodynamic activity (estimated by the relative saturation) increased more for this substrate and hence the selectivity in the reaction was increased.
UR - http://www.scopus.com/inward/record.url?scp=0031042081&partnerID=8YFLogxK
U2 - 10.1023/A:1018379423480
DO - 10.1023/A:1018379423480
M3 - Article
AN - SCOPUS:0031042081
SN - 0141-5492
VL - 19
SP - 85
EP - 88
JO - Biotechnology Letters
JF - Biotechnology Letters
IS - 1
ER -