NDLI: Characterization of UGPase from Aureobasidium pullulans NRRL Y-12974 and Application in Enhanced Pullulan Production

Content Provider	Springer Nature Link
Author	Li, Haifeng Zhang, Yunyi Gao, Yunyun Lan, Yuanyang Yin, Xiaopu Huang, Lifeng
Copyright Year	2015
Abstract	UDPG pyrophosphatase (UGPase) plays an important role in carbohydrate metabolism, catalyzing a reversible production of uridine diphosphate glucose (UDPG) and pyrophosphate (PPi) from Glc-1-P and UTP. UGPase gene from Aureobasidium pullulans NRRL Y-12974 was cloned, overexpressed in Escherichia coli. The recombinant UGPase possess molecular mass of 55 KDa and specific activity of 7.33 U/mg protein. The K $_{ m }$ values of rUGPase were 5.045 μM against UTP and 3.333 μM against Glc-1-P. The V $_{max}$ values of rUGPase were 3.467 μM min$^{−1}$against UTP and 2.817 μM min$^{−1}$ against Glc-1-P. And, it does not catalyze Glc-1-P and ATP, nor galactose-1-P and UTP. Homolgous expression of UGPase in native organism can improve the intracellular UDPG concentration by 4.7-fold time. The yield of pullulan in engineering strain A4 was improved to 18.2 g g$^{−1}$ cell dry weight which is 1.3-fold time of parent strain. No obvious change of growth was found between engineering strain and parent strain. To the best of our knowledge, this is the first report of improving pullulan yield in A. pullulans using metabolic engineering technique.
Starting Page	1141
Ending Page	1153
Page Count	13
File Format	PDF
ISSN	02732289
Journal	Applied Biochemistry and Biotechnology
Volume Number	178
Issue Number	6
e-ISSN	15590291
Language	English
Publisher	Springer US
Publisher Date	2015-11-27
Publisher Place	New York
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Aureobasidium pullulans UDPG pyrophosphatase Expression Pullulan Biotechnology Biochemistry
Content Type	Text
Resource Type	Article
Subject	Medicine Molecular Biology Environmental Engineering Biochemistry Bioengineering Applied Microbiology and Biotechnology Biotechnology

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