Chitinase from soybean seeds: purification and some properties of the enzyme system
1984
A:PS
Details
Title
Chitinase from soybean seeds: purification and some properties of the enzyme system
Author
Wadsworth, S.A.
Zikakis, J.P.
Zikakis, J.P.
Publication Date
1984
Call Number
A:PS
Summary
Chitinase was isolated and purified from soybean seed extract for the first time by ammonium sulfate precipitation followed by chromatography on ground chitin. Five protein peaks containing chitinase activity were eluted, with three peaks containing chitobiase activity as well. Purification was up to 258-fold. The procedure is simple, inexpensive and yielded chitinase of higher specific activity than two out of three commerical enzymes tested. The average molecular weight of the chitinase was 31600 as determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Preliminary results indicate the enzyme acts as an endochitinase and that isoenzymes may be present. The enzyme exhibited a relatively low pH optimum in the range of 3.3-4.0. Activity on regenerated chitin was considerably greater than on more crystalline native substrates. [AS/SS]
Journal Citation
v.32(6):1284-1288, JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY
Contact Information
harvest@worldveg.org
Record Appears in
Research > Published Articles