NDLI: Construction of multi-chimeric pyrroloquinoline quinone glucose dehydrogenase with improved enzymatic properties and application in glucose monitoring

Content Provider	Springer Nature Link
Author	Yoshida, Hiromi Iguchi, Tsuyoshi Sode, Koji
Copyright Year	2000
Abstract	A multi-chimeric enzyme was constructed by combining the protein regions responsible for the enzymatic properties of Escherichia coli and Acinetobacter calcoaceticus pyrroloquinoline quinone glucose dehydrogenase (PQQGDH). The constructed multi-chimeric PQQGDH showed increased co-factor binding stability, thermal stability, an alteration in substrate specificity and a 10-fold increase in the K m value for glucose compared with the wild-type E. coli PQQGDH. The cumulative effect of each introduced protein region on the improvement of enzymatic properties was observed. The application of the multi-chimeric PQQGDH in amperometric glucose sensor construction achieved an expanded dynamic range together with increased operational stability and narrower substrate specificity. The glucose sensor can measure glucose from 5 to 40 mM, suggesting its potential for the direct measurement of high blood-glucose levels in diabetic patients.
Starting Page	1505
Ending Page	1510
Page Count	6
File Format	PDF
ISSN	01415492
Journal	Biotechnology Letters
Volume Number	22
Issue Number	18
e-ISSN	15736776
Language	English
Publisher	Kluwer Academic Publishers-Plenum Publishers
Publisher Date	2000-01-01
Publisher Place	New York
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Biotechnology Organic Chemistry Bioorganic Chemistry Biochemistry Microbiology Animal Anatomy / Morphology / Histology
Content Type	Text
Resource Type	Article
Subject	Medicine Bioengineering Applied Microbiology and Biotechnology Biotechnology

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