The substrate specificity of amylopectin-debranching enzymes from sweet corn

E. Y.C. Lee; J. J. Marshall; W. J. Whelan

doi:10.1016/0003-9861(71)90223-2

The substrate specificity of amylopectin-debranching enzymes from sweet corn

E. Y.C. Lee, J. J. Marshall, W. J. Whelan

Biochemistry & Molecular Biology

Research output: Contribution to journal › Article › peer-review

47 Scopus citations

Abstract

An enzyme showing pullulanase activity has been purified from sweet corn, and separated on hydroxylapatite into what appear to be two isoenzyme forms. The specificities of the two fractions are identical. Pullulan, α-limit dextrins and amylopectin β-limit dextrin are rapidly hydrolyzed by the enzyme; amylopectin is slowly debranched, but there is no significant action on glycogen unless the enzyme is allowed to act simultaneously with β-amylase. The enzyme therefore resembles pullulanase [bacterial R-enzyme, EC 3.2.1.9] from Aerobacter aerogenes. The in vivo significance of this enzyme is discussed.

Original language	English (US)
Pages (from-to)	365-374
Number of pages	10
Journal	Archives of Biochemistry and Biophysics
Volume	143
Issue number	2
DOIs	https://doi.org/10.1016/0003-9861(71)90223-2
State	Published - Apr 1971

ASJC Scopus subject areas

Biophysics
Biochemistry
Molecular Biology

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10.1016/0003-9861(71)90223-2

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title = "The substrate specificity of amylopectin-debranching enzymes from sweet corn",

abstract = "An enzyme showing pullulanase activity has been purified from sweet corn, and separated on hydroxylapatite into what appear to be two isoenzyme forms. The specificities of the two fractions are identical. Pullulan, α-limit dextrins and amylopectin β-limit dextrin are rapidly hydrolyzed by the enzyme; amylopectin is slowly debranched, but there is no significant action on glycogen unless the enzyme is allowed to act simultaneously with β-amylase. The enzyme therefore resembles pullulanase [bacterial R-enzyme, EC 3.2.1.9] from Aerobacter aerogenes. The in vivo significance of this enzyme is discussed.",

author = "Lee, {E. Y.C.} and Marshall, {J. J.} and Whelan, {W. J.}",

note = "Funding Information: WC thank Mr. David Heigle and Mr. Granville Taylor fnr technical assistance and l)r. 14:. I?. Smith for helpful discussion. This work ww slip-ported I)> a grant from I htr Sat~iunal Soitwcc Foundation ((+I3 8342).",

year = "1971",

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doi = "10.1016/0003-9861(71)90223-2",

language = "English (US)",

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pages = "365--374",

journal = "Archives of Biochemistry and Biophysics",

issn = "0003-9861",

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T1 - The substrate specificity of amylopectin-debranching enzymes from sweet corn

AU - Lee, E. Y.C.

AU - Marshall, J. J.

AU - Whelan, W. J.

N1 - Funding Information: WC thank Mr. David Heigle and Mr. Granville Taylor fnr technical assistance and l)r. 14:. I?. Smith for helpful discussion. This work ww slip-ported I)> a grant from I htr Sat~iunal Soitwcc Foundation ((+I3 8342).

PY - 1971/4

Y1 - 1971/4

N2 - An enzyme showing pullulanase activity has been purified from sweet corn, and separated on hydroxylapatite into what appear to be two isoenzyme forms. The specificities of the two fractions are identical. Pullulan, α-limit dextrins and amylopectin β-limit dextrin are rapidly hydrolyzed by the enzyme; amylopectin is slowly debranched, but there is no significant action on glycogen unless the enzyme is allowed to act simultaneously with β-amylase. The enzyme therefore resembles pullulanase [bacterial R-enzyme, EC 3.2.1.9] from Aerobacter aerogenes. The in vivo significance of this enzyme is discussed.

AB - An enzyme showing pullulanase activity has been purified from sweet corn, and separated on hydroxylapatite into what appear to be two isoenzyme forms. The specificities of the two fractions are identical. Pullulan, α-limit dextrins and amylopectin β-limit dextrin are rapidly hydrolyzed by the enzyme; amylopectin is slowly debranched, but there is no significant action on glycogen unless the enzyme is allowed to act simultaneously with β-amylase. The enzyme therefore resembles pullulanase [bacterial R-enzyme, EC 3.2.1.9] from Aerobacter aerogenes. The in vivo significance of this enzyme is discussed.

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The substrate specificity of amylopectin-debranching enzymes from sweet corn

Abstract

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