Purification and properties of a chitinase from Penicillium sp. LYG 0704.
The chitinase producing Penicillium sp. LYG 0704 was procured from soil of the Chonnam National University crop field. The chitinase activity was detected after the first day which increased gradually and reached its maximum after 3 days of cultivation. The chitinase was purified from a culture medium by precipitation with isopropanol and column chromatography with Mono Q and Butyl-Sepharose. The molecular mass of chitinase was estimated to be 47 kDa by SDS-PAGE. Optimal pH and temperature were 5.0 and 40 degrees C, respectively. The N-terminal amino acid sequence of the enzyme was determined to be (1)AGSYRSVAYFVDWAI(15). The fully cloned gene, 1287 bp in size, encoded a single peptide of 429 amino acids. BLAST search of the chitinase gene sequence showed similarity with chitinase of Aspergillus fumigatus Af293 chitinase gene (58%) and A. fumigatus class V chitinase ChiB1 gene (56%).
Lee
Yoon Gyo
YG
Department of Wood Science and Engineering, BK21 Program, Chonnam National University, Gwangju 500-757, Republic of Korea.
Chung
Ki-Chul
KC
Wi
Seung Gon
SG
Lee
Jae Chang
JC
Bae
Hyeun-Jong
HJ
D019840:2-Propanol / Q000737:chemistry; D002688:Chitinases / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism*; D003001:Cloning, Molecular; D004591:Electrophoresis, Polyacrylamide Gel; D004789:Enzyme Activation; D004795:Enzyme Stability; D004926:Escherichia coli / Q000235:genetics / Q000378:metabolism; D006863:Hydrogen-Ion Concentration; D008970:Molecular Weight; D010407:Penicillium / Q000201:enzymology*; D011993:Recombinant Fusion Proteins / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism*; D013696:Temperature
D011993:Recombinant Fusion Proteins; D002688:Chitinases; D019840:2-Propanol