- Identification of an Extracellular Thermostable Glycosyl Hydrolase Family 13 α-Amylase from Thermotoga neapolitana
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Kyoung-Hwa Choi , Sungmin Hwang , Hee-Seob Lee , Jaeho Cha
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J. Microbiol. 2011;49(4):628-634. Published online September 2, 2011
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DOI: https://doi.org/10.1007/s12275-011-0432-7
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We cloned the gene for an extracellular α-amylase, AmyE, from the hyperthermophilic bacterium Thermotoga
neapolitana and expressed it in Escherichia coli. The molecular mass of the enzyme was 92 kDa as a monomer.
Maximum activity was observed at pH 6.5 and temperature 75°C and the enzyme was highly thermostable.
AmyE hydrolyzed the typical substrates for α-amylase, including soluble starch, amylopectin, and maltooligosaccharides.
The hydrolytic pattern of AmyE was similar to that of a typical α-amylase; however, unlike
most of the calcium (Ca2+)-dependent α-amylases, the activity of AmyE was unaffected by Ca2+. The specific
activities of AmyE towards various substrates indicated that the enzyme preferred maltooligosaccharides
which have more than four glucose residues. AmyE could not hydrolyze maltose and maltotriose. When
maltoheptaose was incubated with AmyE at the various time courses, the products consisting of maltose
through maltopentaose was evenly formed indicating that the enzyme acts in an endo-fashion. The specific
activity of AmyE (7.4 U/mg at 75°C, pH 6.5, with starch as the substrate) was extremely lower than that
of other extracellular α-amylases, which indicates that AmyE may cooperate with other highly active extracellular
α-amylases for the breakdown of the starch or α-glucans into maltose and maltotriose before transport
into the cell in the members of Thermotoga sp.
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Citations
Citations to this article as recorded by  - From Batch to Pilot Scale: Continuous Biohydrogen Production from Potato Peel Residues by Thermotoga neapolitana
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Li Zhoukun, Zheng Wenwen, Zhang Lei, Wang Yanxin, Zhang Yajuan, Qiao Yan, Luo Xue, Huang Yan, Cui Zhongli
Starch - Stärke.2019;[Epub] CrossRef - The hyperthermophilic α-amylase from Thermococcus sp. HJ21 does not require exogenous calcium for thermostability because of high-binding affinity to calcium
Huaixu Cheng, Zhidan Luo, Mingsheng Lu, Song Gao, Shujun Wang
Journal of Microbiology.2017; 55(5): 379. CrossRef - Cloning, Purification and Characterization of a Highly Thermostable Amylase Gene of Thermotoga petrophila into Escherichia coli
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Applied Biochemistry and Biotechnology.2016; 178(4): 831. CrossRef - Hydrogen Production by the Thermophilic Bacterium Thermotoga neapolitana
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International Journal of Molecular Sciences.2015; 16(6): 12578. CrossRef
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