Characterization of a novel debranching enzyme from Nostoc punctiforme possessing a high specificity for long branched chains
- Center for Agricultural Biomaterials and Department of Food Science and Biotechnology, Seoul National University, Seoul 151-921 (Korea, Republic of)
- Department of Food science and Nutrition, Pusan National University, Busan 609-735 (Korea, Republic of)
- Department of Food and Biotechnology, Korea University, Chochiwon, Chungnam 339-700 (Korea, Republic of)
- Translational Research Center, Korea Research Institute of Bioscience and Biotechnology, 111 Gwahangno, Yuseong-gu, Daejeon 305-806 (Korea, Republic of)
- Food Research Institute and School of Food and Life Science, and Biohealth Products Research Center, Inje University, Gimhae 621-749 (Korea, Republic of)
- Department of Microbiology and Immunology, McGill University, Montreal, Que., Canada H3A 2B4/AAFC (Canada)
A novel debranching enzyme from Nostoc punctiforme PCC73102 (NPDE) exhibits hydrolysis activity toward both {alpha}-(1,6)- and {alpha}-(1,4)-glucosidic linkages. The action patterns of NPDE revealed that branched chains are released first, and the resulting maltooligosaccharides are then hydrolyzed. Analysis of the reaction with maltooligosaccharide substrates labeled with {sup 14}C-glucose at the reducing end shows that NPDE specifically liberates glucose from the reducing end. Kinetic analyses showed that the hydrolytic activity of NPDE is greatly affected by the length of the substrate. The catalytic efficiency of NPDE increased considerably upon using substrates that can occupy at least eight glycone subsites such as maltononaose and maltooctaosyl-{alpha}-(1,6)-{beta}-cyclodextrin. These results imply that NPDE has a unique subsite structure consisting of -8 to +1 subsites. Given its unique subsite structure, side chains shorter than maltooctaose in amylopectin were resistant to hydrolysis by NPDE, and the population of longer side chains was reduced.
- OSTI ID:
- 21255825
- Journal Information:
- Biochemical and Biophysical Research Communications, Vol. 378, Issue 2; Other Information: DOI: 10.1016/j.bbrc.2008.11.020; PII: S0006-291X(08)02212-2; Copyright (c) 2008 Elsevier Science B.V., Amsterdam, The Netherlands, All rights reserved; Country of input: International Atomic Energy Agency (IAEA); ISSN 0006-291X
- Country of Publication:
- United States
- Language:
- English
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