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Determining the inhibition constants in the HCH‐1 model of cellulose hydrolysis
Author(s) -
Holtzapple Mark T.,
Caram Hugo S.,
Humphrey Arthur E.
Publication year - 1984
Publication title -
biotechnology and bioengineering
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.136
H-Index - 189
eISSN - 1097-0290
pISSN - 0006-3592
DOI - 10.1002/bit.260260719
Subject(s) - cellobiose , hydrolysis , cellulose , cellulase , chemistry , reaction rate constant , non competitive inhibition , biochemistry , chromatography , organic chemistry , kinetics , enzyme , physics , quantum mechanics
The products of cellulose hydrolysis, glucose and cellobiose, caused noncompetitive inhibition patterns to be exhibited when Thermomonospora sp. YX cellulase hydrolyzed dyed cellulose. The glucose binding constant, β 1 , was 0.00683 ± 0.00031 L/g and the cellobiose binding constant, β 2 , was 0.095 ± 0.0058 L/g. Thus, cellobiose was about 14 times more inhibitory than glucose.
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