Zobrazeno 1 - 7
of 7
pro vyhledávání: '"Helen J. Gasdorf"'
Autor:
Lawrence K. Nakamura, Terry C. Nelsen, Thomas P. Abbott, Gabrielle Buchholz, Doris M. Palmer, Walter J. Wolf, Robert Kleiman, Helen J. Gasdorf
Publikováno v:
Journal of Agricultural and Food Chemistry. 39:1488-1493
Autor:
Glenn A. Bennett, Thomas P. Abbott, Helen J. Gasdorf, Robert Kleiman, Terry C. Nelsen, Lawrence K. Nakamura
Publikováno v:
Applied Microbiology and Biotechnology. 34:270-273
Four microorganisms that metabolize simmondsin (S) and related cyanogenic toxins from jojoba (Simmondsia chinensis) were isolated by enrichment: Pseudallescheria boydii, a fungus which specifically degrades simmondsin ferulate but not S; Fusarium mon
Publikováno v:
Journal of Bacteriology. 90:147-150
Gasdorf, Helen J. (Northern Regional Research Laboratory, Peoria, Ill.), R. G. Benedict, M. C. Cadmus, R. F. Anderson, and R. W. Jackson . Polymer-producing species of Arthrobacter . J. Bacteriol. 90: 147–150.1965.—Two slime-producing microorgani
Publikováno v:
Applied Microbiology. 11:488-492
A bacterial strain (NRRL B-1973) isolated from soil at Guatemala City and tentatively identified as an Arthrobacter species produced a polysaccharide with unusual properties. Conditions were studied for the production of this microbial gum in shaken
Publikováno v:
Applied and Environmental Microbiology. 31:615-617
Soybean milk serves as a base for a variety of beverages designed for consumption in developing countries. Soybean flour contains raffinose and stachyose considered to be responsible for flatulence often associated with these products (J.J. Rackis, D
Publikováno v:
Carbohydrate research. 42(1)
Glucoamylase isozymes from black Aspergillus species have been freed of all traces of alpha -amylase by chromatography on Bio-Gel P-100, as evidenced by limited hydrolysis of oxidized amylose. Glucoamylase I retains its ability to hydrolyse rabbit-li
Publikováno v:
Archives of biochemistry and biophysics. 144(2)
The existence of multiple forms of glucoamylase has been known for some time. However, little information is available to differentiate these isozymes other than their electrophoretic mobility. It has now been found that the two forms of glucoamylase