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Title of Journal: Appl Microbiol Biotechnol

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Abbravation: Applied Microbiology and Biotechnology

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Springer-Verlag

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DOI

10.1002/sd.478

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1432-0614

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Characterization of an exoacting intracellular α

Authors: KyungMin Park SoYoung Jun KyoungHwa Choi KwanHwa Park CheonSeok Park Jaeho Cha
Publish Date: 2009/10/16
Volume: 86, Issue: 2, Pages: 555-566
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Abstract

We cloned and expressed the gene for an intracellular αamylase designated AmyB from the hyperthermophilic bacterium Thermotoga neapolitana in Escherichia coli The putative intracellular amylolytic enzyme contained four regions that are highly conserved among glycoside hydrolase family GH 13 αamylases AmyB exhibited maximum activity at pH 65 and 75°C and its thermostability was slightly enhanced by Ca2+ However Ca2+ was not required for the activity of AmyB as EDTA had no effect on enzyme activity AmyB hydrolyzed the typical substrates for αamylase including soluble starch amylose amylopectin and glycogen to liberate maltose and minor amount of glucose The hydrolytic pattern of AmyB is most similar to those of maltogenic amylases EC 321133 among GH 13 αamylases however it can be distinguished by its inability to hydrolyze pullulan and βcyclodextrin AmyB enzymatic activity was negligible when acarbose a maltotetraose analog in which a maltose residue at the nonreducing end was replaced by acarviosine was present indicating that AmyB cleaves maltose units from the nonreducing end of maltooligosaccharides These results indicate that AmyB is a new type exoacting intracellular αamylase possessing distinct characteristics that distinguish it from typical αamylase and cyclodextrin/pullulanhydrolyzing enzymesThis study was supported in part by the Marine and Extreme Genome Research Center Program of the Ministry of Land Transportation and Maritime Affairs and by the Korea Research Foundation Grant funded by the Korean Government MOEHRD KRF2007521F00056 Republic of Korea

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