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Two new β-glucosidases from ethanol-fermenting fungus Mucor circinelloides NBRC 4572: enzyme purification, functional characterization, and molecular cloning of the gene

An Erratum to this article was published on 12 October 2013

Abstract

Two β-glucosidases (BGLs 1 and 2) were purified to homogeneity from the extracellular enzyme preparations of the ethanol-fermenting Mucor circinelloides NBRC 4572 statically grown on rice straw. BGLs 1 and 2 are monomeric glycoproteins whose apparent molecular masses (Ms) are around 78 kDa, which decreased by approximately 10 kDa upon enzymatic deglycosylation. Both BGLs showed similar enzyme characteristics in optimal temperature and pH, stability, and inhibitors. They were active against a wide range of aryl-β-glucosides and β-linked glucose oligosaccharides. Their amino acid sequences shared 81 % identity and exhibited less than 60 % identity with the known family-3 BGLs. Considering properties such as reduced inhibition by ethanol, glucose, and cellobiose, low transglucosylation activity, wider substrate range, less binding affinity to lignocellulosic materials, and abundant expression, BGL1 is likely to be more suitable for bioethanol production than BGL2 via simultaneous saccharification and fermentation of rice straw with M. circinelloides.

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Acknowledgment

This work was supported by a grant from the New Energy and Industrial Technology Development Organization (NEDO) project. The authors thank Ms. Haruna Tsubata and Ms. Rina Sakaguchi of Toyama Prefectural University for their technical assistance in the optimization of the cultivation conditions of M. circinelloides.

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Correspondence to Yasuo Kato.

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Kato, Y., Nomura, T., Ogita, S. et al. Two new β-glucosidases from ethanol-fermenting fungus Mucor circinelloides NBRC 4572: enzyme purification, functional characterization, and molecular cloning of the gene. Appl Microbiol Biotechnol 97, 10045–10056 (2013). https://doi.org/10.1007/s00253-013-5210-5

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Keywords

  • β-Glucosidase
  • Ethanol fermentation
  • Fungus
  • Mucor
  • Enzyme purification