Biotechnology and Bioprocess Engineering

, Volume 7, Issue 1, pp 38–42 | Cite as

Molecular cloning and characterization of 58 kDa chitinase gene fromSerratia marcescens KCTC 2172

  • Sang Wan Gal
  • S. W. Lee
  • Y. J. Choi


A chitinase gene (pCHi58) encoding a 58 kDa chitinase was isolated from theSerratia marcescens KCTC 2172 cosmid library. The chitinase gene consisted of a 1686 bp open reading frame that encoded 562 amino acids.Escherichia coil harboring the pChi58 gene secreted a 58 kDa chitinase into the culture supernatant. The 58 kDa chitinase was purified using a chitin affinity column and mono-S column. A nucleotide andN-terminal amino acid sequence analysis showed that the 58 kDa chitinase had a leader peptide consisting of 23 amino acids which was cleaved prior to the 24th alanine. The 58 KDa chitinase exhibited a 98% similarity to that ofS. marcescens QMB 1466 in its nuclotide sequence. The chitinolytic patterns of the 58 kDa chitinase released N,N′-diacetyl chitobiose (NAG2) as the major hydrolysis end-product with a trace amount ofN-acetylglucosamine. When a 4-methylumbellyferyl-N-acetylglucosamin monomer, dimmer, and tetramer were used as substrates, the 58 kDa chitinase did not digest the 4-Mu-NAG monomer (analogue of NAG2), thereby indicating that the 58 kDa chitinase was likely an endochitinase. The optimum reaction temperature and pH of the enzyme were 50°C and 5.0, respectively.


Serratia marcescens chitinase endochitinase 


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Copyright information

© The Korean Society for Biotechnology and Bioengineering 2002

Authors and Affiliations

  1. 1.Department of Microbiological EngineeringChinju National UniversityChinjuKorea
  2. 2.Department of Food and NutritionSila UniversityPusanKorea

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