On the specificity of starch debranching enzymes

Drummond, George I.; Smith, Eric E.; Whelan, W. J.

doi:10.1016/0014-5793(70)80337-4

Cited by 33 publications

(3 citation statements)

References 19 publications

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“…Pullulanase (EC 3.2.1.41) is distributed in plants and bacteria. The enzyme in plants readily cleaves the α-1,6-glucosidic linkage in pullulan, β-limit dextrin, and α-limit dextrin, while it can debranch amylopectin to a lesser extent than polyglucans (Drummond et al, 1970;Lee et al, 1971;Dunn et al, 1973;Gordon et al, 1975;Yamada & Izawa 1979;Okita & Preiss, 1980;Li et al, 1992). Therefore, it has been suggested that pullulanase in plants is necessary for starch degradation in conjunction with α-β-amylases.…”

Section: Introductionmentioning

confidence: 99%

Pullulanase from rice endosperm.

Yamasaki¹,

Nakashima²,

Konno³

2008

Acta Biochim Pol

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Pullulanase (EC 3.2.1.41) in non-germinating seeds was compared with that in germinating seeds. Moreover, pullulanase from the endosperm of rice (Oryza sativa L., cv. Hinohikari) seeds was isolated and its properties investigated. The pI value of pullulanase from seeds after 8 days of germination was almost equal to that from non-germinating seeds, which shows that these two enzymes are the same protein. Therefore, the same pullulanase may play roles in both starch synthesis during ripening and starch degradation during germination in rice seeds. The enzyme was isolated by a procedure that included ammonium sulfate fractionation, DEAE-cellulofine column chromatography, preparative isoelectric focusing, and preparative disc gel electrophoresis. The enzyme was homogeneous by SDS/PAGE. The molecular weight of the enzyme was estimated to be 100 000 based on its mobility on SDS/PAGE and 105 000 based on gel filtration with TSKgel super SW 3000, which showed that it was composed of a single unit. The isoelectric point of the enzyme was 4.7. The enzyme was strongly inhibited by beta-cyclodextrin. The enzyme was not activated by thiol reagents such as dithiothreitol, 2-mercaptoethanol or glutathione. The enzyme most preferably hydrolyzed pullulan and liberated only maltotriose. The pullulan hydrolysis was strongly inhibited by the substrate at a concentration higher than 0.1%. The degree of inhibition increased with an increase in the concentration of pullulan. However, the enzyme hydrolyzed amylopectin, soluble starch and beta-limit dextrin more rapidly as their concentrations increased. The enzyme exhibited alpha-glucosyltransfer activity and produced an alpha-1,6-linked compound of two maltotriose molecules from pullulan.

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Section: Introductionmentioning

confidence: 99%

Pullulanase from rice endosperm.

Yamasaki¹,

Nakashima²,

Konno³

2008

Acta Biochim Pol

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“…Potato R-enzyme [1 ] and bacterial pullulanase [2,3] hydrolyse the a-1,6-linkages in pullulan and a-limit dextrins and also cleave the a-1,6-branch linkages in amylopectin [4]. The availability of highly purified preparations of pullulanase from Aerobacter aerogenes [5] has made this enzyme invaluable in the analysis of the fine structure of amylopectin [6].…”

Section: Introductionmentioning

confidence: 99%

A glycogen‐debranching enzyme from Cytophaga

et al. 1970

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“…Recently, Yamada purified a rice debranching enzymea) and studied its action mode.9) He also revealed interconversion be tween its active and inactive forms during ripening and germination of rice seeds.10,11) However, study on the debranching enzyme of potato tubers is only limited. Succeeding to its dis covery, Hobson et al purified the potato debranch ing enzyme to a certain extent.12) Drummond et al 13) reported that a potato debranching en zyme was purified to a state free from Q-enzyme. But its detailed enzymatic properties remained to be studied until present report.…”

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confidence: 99%