Purification of a thermostable chitinase from Bacillus cereus by chitin affinity and its application in microbial community changes in soil

Bioprocess Biosyst Eng. 2014 Jun;37(6):1201-9. doi: 10.1007/s00449-013-1092-2. Epub 2013 Dec 17.

Abstract

A thermostable chitinase was purified by chitin affinity from the culture supernatant of Bacillus cereus TKU028 with shrimp head powder (SHP) as the sole carbon/nitrogen source. TKU028 chitinase was purified using a one-step affinity adsorbent system, and the molecular mass of TKU028 chitinase (approximately 40 kDa) was then determined using SDS-PAGE. The enzyme was stable for 60 min at temperatures below 60 °C and stable over a broad pH range of 4-9 for 60 min. In addition, the temporal changes of a bacterial community in mangrove river sediment of the Tamsui River with added SHP were also analysed by PCR-denaturing gradient gel electrophoresis to investigate the effects of B. cereus TKU028 on the degradation of SHP. The 6-week incubation sample of SHP and B. cereus TKU028-amended mangrove river sediment displayed the highest amount of biomass, reducing sugar and total sugar, and some variance of bacterial community composition existed in the soils.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacillus cereus / enzymology*
  • Bacterial Proteins / chemistry*
  • Bacterial Proteins / isolation & purification*
  • Chitinases / chemistry*
  • Chitinases / isolation & purification*
  • Enzyme Stability
  • Hot Temperature

Substances

  • Bacterial Proteins
  • Chitinases