333. The enzymic synthesis and degradation of starch. Part XIV. R-enzyme

P. N. Hobson, William J. Whelan, Stanley Peat

Research output: Contribution to journalArticle

37 Citations (Scopus)

Abstract

An enzyme (R-enzyme), which catalyses the scission of branch links in amylopectin, has been isolated from the potato and the broad bean as a stable amorphous powder. It is shown that R-enzyme operates by a purely hydrolytic process and that, unlike R-enzyme, it has no link-synthesising function. It is a "debranching" enzyme with respect to the predominant type of branch linkage in amylopectin, the 1:6-glucosidic link. It neither makes nor breaks chain-forming 1:4-links and has no action on amylose (synthetic or natural) or on the linear dextrins related to amylose. A convenient method of estimating the activity of R-enzyme is based on the fact that its action on amylopectin or limit β-dextrin is accompanied by a rise in the iodine-staining power of the substrate.

Original languageEnglish
Pages (from-to)1451-1459
Number of pages9
JournalJournal of the Chemical Society (Resumed)
DOIs
StatePublished - Dec 1 1951
Externally publishedYes

Fingerprint

Starch
Amylopectin
Degradation
Enzymes
Amylose
Dextrins
Solanum tuberosum
Iodine
Powders
Staining and Labeling
Substrates

ASJC Scopus subject areas

  • Chemistry(all)

Cite this

333. The enzymic synthesis and degradation of starch. Part XIV. R-enzyme. / Hobson, P. N.; Whelan, William J.; Peat, Stanley.

In: Journal of the Chemical Society (Resumed), 01.12.1951, p. 1451-1459.

Research output: Contribution to journalArticle

@article{b36b11f1290c4ce09d7f92a390da492c,
title = "333. The enzymic synthesis and degradation of starch. Part XIV. R-enzyme",
abstract = "An enzyme (R-enzyme), which catalyses the scission of branch links in amylopectin, has been isolated from the potato and the broad bean as a stable amorphous powder. It is shown that R-enzyme operates by a purely hydrolytic process and that, unlike R-enzyme, it has no link-synthesising function. It is a {"}debranching{"} enzyme with respect to the predominant type of branch linkage in amylopectin, the 1:6-glucosidic link. It neither makes nor breaks chain-forming 1:4-links and has no action on amylose (synthetic or natural) or on the linear dextrins related to amylose. A convenient method of estimating the activity of R-enzyme is based on the fact that its action on amylopectin or limit β-dextrin is accompanied by a rise in the iodine-staining power of the substrate.",
author = "Hobson, {P. N.} and Whelan, {William J.} and Stanley Peat",
year = "1951",
month = "12",
day = "1",
doi = "10.1039/JR9510001451",
language = "English",
pages = "1451--1459",
journal = "Journal of the Chemical Society",
issn = "0577-6171",
publisher = "Chemical Society",

}

TY - JOUR

T1 - 333. The enzymic synthesis and degradation of starch. Part XIV. R-enzyme

AU - Hobson, P. N.

AU - Whelan, William J.

AU - Peat, Stanley

PY - 1951/12/1

Y1 - 1951/12/1

N2 - An enzyme (R-enzyme), which catalyses the scission of branch links in amylopectin, has been isolated from the potato and the broad bean as a stable amorphous powder. It is shown that R-enzyme operates by a purely hydrolytic process and that, unlike R-enzyme, it has no link-synthesising function. It is a "debranching" enzyme with respect to the predominant type of branch linkage in amylopectin, the 1:6-glucosidic link. It neither makes nor breaks chain-forming 1:4-links and has no action on amylose (synthetic or natural) or on the linear dextrins related to amylose. A convenient method of estimating the activity of R-enzyme is based on the fact that its action on amylopectin or limit β-dextrin is accompanied by a rise in the iodine-staining power of the substrate.

AB - An enzyme (R-enzyme), which catalyses the scission of branch links in amylopectin, has been isolated from the potato and the broad bean as a stable amorphous powder. It is shown that R-enzyme operates by a purely hydrolytic process and that, unlike R-enzyme, it has no link-synthesising function. It is a "debranching" enzyme with respect to the predominant type of branch linkage in amylopectin, the 1:6-glucosidic link. It neither makes nor breaks chain-forming 1:4-links and has no action on amylose (synthetic or natural) or on the linear dextrins related to amylose. A convenient method of estimating the activity of R-enzyme is based on the fact that its action on amylopectin or limit β-dextrin is accompanied by a rise in the iodine-staining power of the substrate.

UR - http://www.scopus.com/inward/record.url?scp=0041623285&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0041623285&partnerID=8YFLogxK

U2 - 10.1039/JR9510001451

DO - 10.1039/JR9510001451

M3 - Article

AN - SCOPUS:0041623285

SP - 1451

EP - 1459

JO - Journal of the Chemical Society

JF - Journal of the Chemical Society

SN - 0577-6171

ER -