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Identification and Phylogenetic Characterization of a New Subfamily of α-Amylase Enzymes from Marine Microorganisms

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Abstract

A gene encoding a starch-hydrolyzing enzyme was isolated from a marine metagenomic library and overexpressed in Escherichia coli. The enzyme, designated AmyP, shows very low similarity to full-length sequences of known α-amylases, although a catalytic domain correlated with the α-amylase superfamily was identified. Based on the range of substrate hydrolysis and the product profile, the protein was clearly defined as a saccharifying-type α-amylase. Sequence comparison indicated that AmyP was related to four putative glycosidases previously identified only in bacterial genome sequences. They were all from marine bacteria and formed a new subfamily of glycoside hydrolase GH13. Moreover, this subfamily was closely related to the probable genuine bacterial α-amylases (GH13_19). The results suggested that the subfamily may be an independent clade of ancestral marine bacterial α-amylases.

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Acknowledgments

We thank Tong Zhang for providing the marine metagenomic library. This work was supported by the Natural Science Foundation of Anhui Province, China (11040606M65) and the Foundation for Key Program of Ministry of Education, China (211073).

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Authors and Affiliations

  1. Engineering Technology Research Center of Microorganisms and Biocatalysis, Anhui Province, School of Life Sciences, Anhui University, Hefei, 230039, Anhui, People’s Republic of China

    Yang Liu, Yin Lei, Xuecheng Zhang, Yazhong Xiao & Hui Peng

  2. School of Resources and Environmental Engineering, Anhui University, Hefei, 230039, Anhui, People’s Republic of China

    Yi Gao

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  1. Yang Liu
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  2. Yin Lei
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  3. Xuecheng Zhang
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  4. Yi Gao
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  5. Yazhong Xiao
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  6. Hui Peng
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Correspondence to Hui Peng.

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Liu, Y., Lei, Y., Zhang, X. et al. Identification and Phylogenetic Characterization of a New Subfamily of α-Amylase Enzymes from Marine Microorganisms. Mar Biotechnol 14, 253–260 (2012). https://doi.org/10.1007/s10126-011-9414-3

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  • DOI: https://doi.org/10.1007/s10126-011-9414-3

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