Pullulanase from rice endosperm.

作者: Yoshiki Yamasaki , Susumu Nakashima , Haruyoshi Konno

DOI: 10.18388/ABP.2008_3056

关键词:

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

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