Abstract
A method is described for the purification of the β-amylase of soya bean, the product of which is amorphous but is virtually free from Z-enzyme as well as from α-amylase and maltase. The elimination of Z-enzyme has been studied in detail and it is shown that for the structural analysis of amylaceous polysaccharides the purified soya-bean β-amylase is exactly equivalent to the crystalline enzyme of sweet potato. It is established that the amyloses of sago, tapioca, and maize are branched in the same way as potato amylose and that the branch points are attacked by Z-enzyme.
Original language | English (US) |
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Pages (from-to) | 714-722 |
Number of pages | 9 |
Journal | Journal of the Chemical Society (Resumed) |
DOIs | |
State | Published - Jan 1 1952 |
Externally published | Yes |
ASJC Scopus subject areas
- Chemistry(all)