Abstract
Z-Enzyme, which supplements the action of β-amylase or phosphorylase on amylose, has been isolated from the soya bean as a freeze-dried powder free from α- and β-amylases. Its function is the hydrolysis of the limited number of branch links in amylose which act as barriers to β-amylolysis or phosphorolysis. Z-Enzyme is shown to be a β-glucosidase and its action on amylose is simulated by the β-glucosidase of sweet almonds. The form of the β-glucosidic links in amylose is discussed.
| Original language | English |
|---|---|
| Pages (from-to) | 722-733 |
| Number of pages | 12 |
| Journal | Journal of the Chemical Society (Resumed) |
| State | Published - Dec 1 1952 |
| Externally published | Yes |
Fingerprint
ASJC Scopus subject areas
- Chemistry(all)
Cite this
The enzymic synthesis and degradation of starch. Part XVII. Z-Enzyme. / Peat, Stanley; Thomas, Gwen J.; Whelan, William J.
In: Journal of the Chemical Society (Resumed), 01.12.1952, p. 722-733.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - The enzymic synthesis and degradation of starch. Part XVII. Z-Enzyme
AU - Peat, Stanley
AU - Thomas, Gwen J.
AU - Whelan, William J.
PY - 1952/12/1
Y1 - 1952/12/1
N2 - Z-Enzyme, which supplements the action of β-amylase or phosphorylase on amylose, has been isolated from the soya bean as a freeze-dried powder free from α- and β-amylases. Its function is the hydrolysis of the limited number of branch links in amylose which act as barriers to β-amylolysis or phosphorolysis. Z-Enzyme is shown to be a β-glucosidase and its action on amylose is simulated by the β-glucosidase of sweet almonds. The form of the β-glucosidic links in amylose is discussed.
AB - Z-Enzyme, which supplements the action of β-amylase or phosphorylase on amylose, has been isolated from the soya bean as a freeze-dried powder free from α- and β-amylases. Its function is the hydrolysis of the limited number of branch links in amylose which act as barriers to β-amylolysis or phosphorolysis. Z-Enzyme is shown to be a β-glucosidase and its action on amylose is simulated by the β-glucosidase of sweet almonds. The form of the β-glucosidic links in amylose is discussed.
UR - http://www.scopus.com/inward/record.url?scp=37049166280&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=37049166280&partnerID=8YFLogxK
M3 - Article
AN - SCOPUS:37049166280
SP - 722
EP - 733
JO - Journal of the Chemical Society
JF - Journal of the Chemical Society
SN - 0577-6171
ER -