ABBAdvances in Bioscience and Biotechnology2156-8456Scientific Research Publishing10.4236/abb.2018.98025ABB-86735ArticlesBiomedical&Life Sciences Erratum to “Expression, Purification and Crystallization of Thermostable Mutant of Cutinase Est1 from <i>Thermobifida alba</i>.” [Advances in Bioscience and Biotechnology 9 (2018), 215-223] KengoKitadokoro1ShingoMatsui1RyouheiOsokoshi1KensukeNakata1UscharaThumarat2FusakoKawai3ShigekiKamitani4Department of Biomolecular Engineering, Graduate School of Science and Technology, Kyoto Institute of Technology, Kyoto, JapanGraduate School of Comprehensive Rehabilitation, College of Health and Human Sciences, Osaka Prefecture University, Osaka, JapanDepartment of Industrial Biotechnology, Faculty of Agro-Industry, Prince of Songkla University, Hat Yai, Songkhla, ThailandCenter for Fiber and Textile Science, Kyoto Institute of Technology, Kyoto, Japan10082018090837837917, March 201827, May 2018 30, May 2018© Copyright 2014 by authors and Scientific Research Publishing Inc. 2014This work is licensed under the Creative Commons Attribution International License (CC BY). http://creativecommons.org/licenses/by/4.0/

The original online version of this article (Kitadokoro, K., Matsui, S., Osokoshi, R., Nakata, K. and Kamitani, S. (2018) Expression, Purification and Crystallization of Thermostable Mutant of Cutinase Est1 from Thermobifida alba. Advances in Bioscience and Biotechnology, 9, 215-223. https://doi.org/10.4236/abb.2018.95015 ) unfortunately contains some mistakes. The author wishes to correct the errors.

ErratumDetermination of Specific Activity

Enzymatic activities were determined by using p-nitrophenylbutyrate (pNPB) ester substrates as previously described [6]. The reaction was performed at 310 K in 1 mL of the mixture containing 50 mM Tris-HCl buffer (pH 8.0), 1 mM pNPB and 0.001 mM enzyme. The reaction mixture without the enzyme was used as the control. Reactions were started by the addition of pNPB.

Acknowledgements

We are grateful to all members of beamline BL44XU at SPring-8 for their help in collecting data. Use of the synchrotron beamline BL44XU at SPring-8 was obtained through the Cooperative Research Program of the Institute for Protein Research, Osaka University.

Macromolecule production information [<xref ref-type="bibr" rid="scirp.86735-ref6">6</xref>]
Source organismThermobifida alba
DNA sourceGenbank AB445476
Forward primer5’- CGCGGATCCAACCCCTACGAACGCGGC -3’
Reverse primer5’- GCGAAGCTTGAACGGGCAGGTGGAGCGGT -3’
Expression vectorpQE80L- est1(A68V/T253P)
Expression hostE. coli Rosetta-gami (DE3)
Complete amino acid sequence of the construct producedMRGSHHHHHHGSNPYERGPNPTESMLEARSGPFSVS EERVSRLGADGFGGGTIYYPRENNTYGAIAISPGYTG TQSSIAWLGERIASHGFVVIAIDTNTTLDQPDSRARQL NAALDYMLTDASSSVRNRIDASRLAVMGHSMGGGG TLRLASQRPDLKAAIPLTPWHLNKSWRDITVPTLIIGA DLDTIAPVSSHSEPFYNSIPSSTDKAYLELNNATHFAPN IPNKTIGMYSVAWLKRFVDEDTRYTQFLCPGPRTGLLS DVDEYRSTCPF
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