Abstract
Cellulases can be added to the list of enzymes that are inactivated by shaking, agitation, or shearing. Of the cellulases, the most susceptible component is cellobiohydrolase (CBH). A survey of compounds that protect CBH against shaking reveals that some non-ionic surfactants are most potent, being active in the range of one molecule per molecule of enzyme. Under shaking conditions (50°, 350 rpm) where the CBH half-life is 1.5 hours, the presence of Zonyl·FSN increased the half-life to 180 hours. The addition of surfactant to enzyme already inactivated by shaking does not lead to recovery of activity. The presence of surfactant does not improve heat stability of the enzyme under unshaken conditions; nor does it affect the initial rate of hydrolysis. Long time (3 day) hydrolyses of crystalline cellulose under shaking conditions are markedly improved by the presence of surfactant, the improvement resulting from protection of the CBH against inactivation.
This is a preview of subscription content, log in via an institution to check access.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Preview
Unable to display preview. Download preview PDF.
References
T. Asakura, K. Adachi and E. Schwartz, J. Biol. Chem., 253, 6423 (1977).
T. Asakura, P. Herridge, P. K. Ghory and K. Adachi, J. Biol. Chem., 252, 1829 (1977).
S. N. Basu and P. M. Pal, Science, 178, 312 (1956).
F. H. Bissett, J. Chrmatog., 178, 515-(1979).
S. E. Charm and B. L. Wong, Biotechn. Bioeng., 12, 1103-(1970).
S. E. Charm and B. L. Wong, Science, 170, pp. 466-(1970).
S. E. Charm and B. L. Wong, Biotechn. & Bioeng., 12, 451-(1978).
J. Feder, D. Kochavi, R. G. Anderson and B. S. Wilde, Biotechn Bioeng., 20, 1865 (1978).
R. G. Kelsey and F. Shafizadeh, Biotechn. Bioeng., 22, 1025-(1979).
F. Macritchie, Adv. Prtoein Chem., 32, 283-(1978).
M. Mandels, R. Andreotti and C. Roche, Biotechn. Bioeng. Symp. 5, 21-(1976).
M. Mandels, S. Dorval and J. Medeiros, Proc. Second Ann. Symposium Fuels from Biomass, R.P.I., pp. 627–669, Ed. W. W. Schuster (1978).
B. J. Montenecourt and D. E. Eveleigh, Appl. Env. Microbiol., 34, 777-(1977).
T. Ohnishi and T. Asakura, Biochem. Biophys. Acta, 453, 93- (1976).
E. T. Reese, Biotechn. Bioeng. Symp., 3, “Enzyme Engineering”, pp. 43–62, John Wiley and Sons, Inc., NYC (1972).
E. T. Reese and M. Mandels, Biotechn. Bioeng., 22, 323- (1980).
E. T. Reese and D. Ryu, Enz. and Microbiol. Techn., 2: 239–40.
J. J. Sedmak and S. E. Grossberg, Texas Rept. an Biology and Medicine, 35, 198- (1977).
D. Sternberg, P. Vijayakumar and E. T. Reese, Can. J. Microbiol., 23, 139- (1977).
M. Tanaka, S. Takenawa, R. Matsuno and I. Kamikubo, J. Ferment Techn., 56, 108- (1978).
C. R. Thomas, A. W. Nienow and P. Dunnill, Biotechn. Bioeng., 21, 2263- (1979).
C. R. Thomas and P. Dunhill, Biotechn. Bioeng., 21, 2279- (1979).
M. Tirrell and S. Middleman, AIChE Symp. Ser. Diorheology, 74, 102- (1978).
M. Tirrell and S. Middleman, Biophys. J., 23, 121- (1978).
M. Tirrell, J. Bioeng., 2, 183- (1978).
N. Toyama and K. Ogawa, in “Enz. Hydrolysis of Cellulose” Symp., (SITRA), Aulanko, Finland, Edit. M. Bailey, T. M. Enari, and M. Linko, pp. 375–387 (1978).
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 1982 Plenum Press, New York
About this chapter
Cite this chapter
Reese, E.T. (1982). Protection of Trichoderma Reesei Cellulase from Inactivation Due to Shaking. In: Mittal, K.L., Fendler, E.J. (eds) Solution Behavior of Surfactants. Springer, Boston, MA. https://doi.org/10.1007/978-1-4613-3494-1_50
Download citation
DOI: https://doi.org/10.1007/978-1-4613-3494-1_50
Publisher Name: Springer, Boston, MA
Print ISBN: 978-1-4613-3496-5
Online ISBN: 978-1-4613-3494-1
eBook Packages: Springer Book Archive