World Journal of Microbiology and Biotechnology

, Volume 25, Issue 4, pp 583–590

Isolation and characterization of a new Bacillus sp. 50-3 with highly alkaline keratinase activity from Calotes versicolor faeces

  • Bin Zhang
  • DanDan Jiang
  • WenWen Zhou
  • HuaKun Hao
  • TianGui Niu
Original Paper

DOI: 10.1007/s11274-008-9926-9

Cite this article as:
Zhang, B., Jiang, D., Zhou, W. et al. World J Microbiol Biotechnol (2009) 25: 583. doi:10.1007/s11274-008-9926-9

Abstract

A new native feather-degrading bacterium has been isolated from the faeces of the agamid lizard Calotes versicolor, collected from the Beijing Zoo in China. The isolate, which has been identified as Bacillus sp. 50-3 based on morphological and biochemical and 16S rDNA tests, was shown to degrade native feather completely at 37°C and pH 7.0 within 36 h when using chicken feathers as the sole carbon and nitrogen source. Bacillus sp. 50-3 presented optimum growth at 37°C and pH 7.0 in feather meal medium. Under these conditions, the maximum keratinase activity (680 ± 25 U/ml) was also achieved. The keratinase of Bacillus sp. 50-3 was active over a broad range of pH values and temperatures toward azokeratin, and presented an optimum pH and temperature of 10.0 and 60°C, respectively. Furthermore, it was relatively heat-and alkali-stable. Inhibitor studies showed that it seemed to belong to the serine-metalloprotease type. Therefore, the enzyme from Bacillus sp. 50-3 is a novel, high alkaline keratinase, suggesting its potential use in biotechnological processes.

Keywords

Alkaline keratinase Animal faeces Bacillus Native chicken feather Serine-metalloprotease 

Copyright information

© Springer Science+Business Media B.V. 2008

Authors and Affiliations

  • Bin Zhang
    • 1
  • DanDan Jiang
    • 1
  • WenWen Zhou
    • 1
  • HuaKun Hao
    • 1
  • TianGui Niu
    • 1
  1. 1.College of Food Science and Nutritional EngineeringChina Agricultural UniversityBeijingChina

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