Advances in Bioscience and Biotechnology
Vol.09 No.08(2018), Article ID:86735,2 pages

Erratum to “Expression, Purification and Crystallization of Thermostable Mutant of Cutinase Est1 from Thermobifida alba.” [Advances in Bioscience and Biotechnology 9 (2018), 215-223]

Kengo Kitadokoro1*, Shingo Matsui1, Ryouhei Osokoshi1, Kensuke Nakata1, Uschara Thumarat2, Fusako Kawai3, Shigeki Kamitani4

1Department of Biomolecular Engineering, Graduate School of Science and Technology, Kyoto Institute of Technology, Kyoto, Japan

2Department of Industrial Biotechnology, Faculty of Agro-Industry, Prince of Songkla University, Hat Yai, Songkhla, Thailand

3Center for Fiber and Textile Science, Kyoto Institute of Technology, Kyoto, Japan

4Graduate School of Comprehensive Rehabilitation, College of Health and Human Sciences, Osaka Prefecture University, Osaka, Japan

Copyright © 2018 by authors and Scientific Research Publishing Inc.

This work is licensed under the Creative Commons Attribution International License (CC BY 4.0).

Received: March 17, 2018; Accepted: May 27, 2018; Published: May 30, 2018

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. unfortunately contains some mistakes. The author wishes to correct the errors.

2.1. Protein Expression and Purification

Est1(A68V/T253P) was used throughout this study (Table 1) [6]. Briefly, 20 mL of an overnight culture of E.coli cells Rosetta-gami B (DE3) transformed with pQE80L-est1(A68V/T253P) was inoculated to 400 mL of LB medium with 50 µg∙ml−1 ampicillin.

Determination 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.


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.

Table 1. Macromolecule production information [6].