Abstract
The end-products of the action of purified salivary α-amylase on amylose and the maltodextrins derived from it have been examined. Only two end-products are found, namely, maltose and maltotriose. This examination supports the theory of α-amylase action first advanced by Meyer and Bernfeld, which states that in an amylose-type chain, α-amylase can hydrolyse any except the two terminal α-1:4-linkages. The ratios of maltose to maltotriose which are produced by α-amylolysis of these substrates are found to be in exact agreement with values obtained by calculation on the basis of Meyer's theory. It is also demonstrated that the susceptible linkages in a given substrate molecule are all hydrolysed by α-amylase at the same rate.
| Original language | English |
|---|---|
| Pages (from-to) | 1298-1304 |
| Number of pages | 7 |
| Journal | Journal of the Chemical Society (Resumed) |
| State | Published - Dec 1 1953 |
| Externally published | Yes |
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ASJC Scopus subject areas
- Chemistry(all)
Cite this
The mechanism of carbohydrate action. Part II. α-Amylolysis of linear substrates. / Whelan, William J.; Roberts, P. J P.
In: Journal of the Chemical Society (Resumed), 01.12.1953, p. 1298-1304.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - The mechanism of carbohydrate action. Part II. α-Amylolysis of linear substrates
AU - Whelan, William J.
AU - Roberts, P. J P
PY - 1953/12/1
Y1 - 1953/12/1
N2 - The end-products of the action of purified salivary α-amylase on amylose and the maltodextrins derived from it have been examined. Only two end-products are found, namely, maltose and maltotriose. This examination supports the theory of α-amylase action first advanced by Meyer and Bernfeld, which states that in an amylose-type chain, α-amylase can hydrolyse any except the two terminal α-1:4-linkages. The ratios of maltose to maltotriose which are produced by α-amylolysis of these substrates are found to be in exact agreement with values obtained by calculation on the basis of Meyer's theory. It is also demonstrated that the susceptible linkages in a given substrate molecule are all hydrolysed by α-amylase at the same rate.
AB - The end-products of the action of purified salivary α-amylase on amylose and the maltodextrins derived from it have been examined. Only two end-products are found, namely, maltose and maltotriose. This examination supports the theory of α-amylase action first advanced by Meyer and Bernfeld, which states that in an amylose-type chain, α-amylase can hydrolyse any except the two terminal α-1:4-linkages. The ratios of maltose to maltotriose which are produced by α-amylolysis of these substrates are found to be in exact agreement with values obtained by calculation on the basis of Meyer's theory. It is also demonstrated that the susceptible linkages in a given substrate molecule are all hydrolysed by α-amylase at the same rate.
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UR - http://www.scopus.com/inward/citedby.url?scp=37049165164&partnerID=8YFLogxK
M3 - Article
SP - 1298
EP - 1304
JO - Journal of the Chemical Society
JF - Journal of the Chemical Society
SN - 0577-6171
ER -