Applied Microbiology and Biotechnology

, Volume 85, Issue 5, pp 1483–1490

Cloning, characterization, and antifungal activity of an endo-1,3-β-d-glucanase from Streptomyces sp. S27

  • Pengjun Shi
  • Guoyu Yao
  • Peilong Yang
  • Ning Li
  • Huiying Luo
  • Yingguo Bai
  • Yaru Wang
  • Bin Yao
Biotechnologically Relevant Enzymes and Proteins

DOI: 10.1007/s00253-009-2187-1

Cite this article as:
Shi, P., Yao, G., Yang, P. et al. Appl Microbiol Biotechnol (2010) 85: 1483. doi:10.1007/s00253-009-2187-1

Abstract

An endo-1,3-β-d-glucanase gene, designated as bglS27, was cloned from Streptomyces sp. S27 and successfully expressed in Escherichia coli BL21 (DE3). The full-length gene contains 1,362 bp and encodes a protein of 453 amino acids with a calculated molecular mass of 42.7 kDa. The encoded protein comprises a catalytic module of glycosyl hydrolase family 16, a short glycine linker region, and a family 13 carbohydrate-binding module. The purified recombinant enzyme (BglS27) showed optimal activity at 65°C and pH 5.5 and preferentially catalyzed the hydrolysis of glucans with a β-1,3-linkage using an endolytic mode of action. The specific activity and Km value of BglS27 for laminarin were 236.0 U mg–1 and 1.89 mg ml–1, respectively. In antifungal assay, BglS27 had the ability to inhibit the growth of phytopathogenic fungi Rhizoctonic solani and Fusarium oxysporum and some mycotoxin-producing fungi Fusarium crookwellense and Paecilomyces variotii. These favorable properties make BglS27 a good candidate for utilization in biotechnological applications such as plant protection, feed, and food preservation.

Keywords

Streptomyces sp. S27Endo-1,3-β-d-glucanaseAntifungal protein

Copyright information

© Springer-Verlag 2009

Authors and Affiliations

  • Pengjun Shi
    • 1
  • Guoyu Yao
    • 1
    • 2
  • Peilong Yang
    • 1
  • Ning Li
    • 1
  • Huiying Luo
    • 1
  • Yingguo Bai
    • 1
  • Yaru Wang
    • 1
  • Bin Yao
    • 1
  1. 1.Key Laboratory for Feed Biotechnology of the Ministry of Agriculture, Feed Research InstituteChinese Academy of Agricultural SciencesBeijingPeople’s Republic of China
  2. 2.Institute of Biochemistry and Molecular Biology, College of Life ScienceLanzhou UniversityLanzhouPeople’s Republic of China