• Applied Biological Chemistry
• /
• v.34 no.1
• /
• pp.54-60
• /
• 1991

Serratia marcescens CK-3, decomposing chitin which is a mar component of cell wall in phyitopathogenic fungi, was isolated from the continuous cropping rhizosphere of pepper and cucumber and its enzymatic property was examined. S. marcescens CK-3 was found tn have an tagonistic effects against, Fusarium axysporum and Rhizoctonia solani and to have complex enzyme system such as chitinase, laminarinase, and proteinase. The preferable composition of the medium for production of chitinase was fond and was as follows : colloidal chitin 1.5%, tryptone 0.5%, glucose 1.0%, peptone 0.2%, $MgSO_4{\cdot}7H_2O\;0.1%,\;K_2HPO_4\;0.1%,\;and\;NaCl\;0.1%$(w/v), pH 6.8. The maximum enzyme production was observed after culture of 72 hours at $30^{\circ}C$ using a medium containing the above chemical composition. The optimal pH and temperature for in vitro activity of chitinase from S. marcescens CK-3 were pH 7.5 and $50^{\circ}C$, respectively. The enzyme activity in-creased by metal ions such as$Ag^+$ and $Mn^{++}$.

• BMB Reports
• /
• v.38 no.1
• /
• pp.82-88
• /
• 2005

Bacillus cereus 28-9 is a chitinolytic bacterium isolated from lily plant in Taiwan. This bacterium exhibited biocontrol potential on Botrytis leaf blight of lily as demonstrated by a detached leaf assay and dual culture assay. At least two chitinases (ChiCW and ChiCH) were excreted by B. cereus 28-9. The ChiCW-encoding gene was cloned and moderately expressed in Escherichia coli DH5$\alpha$. Near homogenous ChiCW was obtained from the periplasmic fraction of E. coli cells harboring chiCW by a purification procedure. An in vitro assay showed that the purified ChiCW had inhibitory activity on conidial germination of Botrytis elliptica, a major fungal pathogen of lily leaf blight.

• Proceedings of the Zoological Society Korea Conference
• /
• 1998.10b
• /
• pp.265.1-265
• /
• 1998

No Abstract, See Full Text

• The Plant Pathology Journal
• /
• v.17 no.6
• /
• pp.365.1-365
• /
• 2001

• The Plant Pathology Journal
• /
• v.17 no.6
• /
• pp.365.3-365
• /
• 2001

• Korean Journal of Soil Science and Fertilizer
• /
• v.21 no.2
• /
• pp.129-134
• /
• 1988

Enzymatical properties of Streptomyces sp. S-45 producing chitinase and ${\beta}$-1.3-glucanase isolated from soil were investigated. Chitinase activity was 3.01(U/ml) and ${\beta}$-1.3-glucanase activity was 2.49(U/ml). The optimum medium for mycolytic enzyme production of strain was composed of 0.7% colloidal chitin, 0.3% glucose, 0.5% asparagine, 0.2% peptone, 0.01% NaCl, 0.01% $K_2HPO_4$ and 0.01% $MgSO_4{\cdot}7H_2O$ in intial pH 7.0. The optimal condition for mycolytic enzyme activities were: pH 6.5-7.0, $45-50^{\circ}C$. Enzyme activities were activated by metal ion as $10^{-2}M\;Co^{{+}{+}}$, $Cu^{{+}{+}}$, $Mn^{{+}{+}}$, $Al^{{+}{+}{+}}$ and $10^{-3}M\;Sn^{{+}{+}}$ but $Ag^{{+}{+}}$, $Hg^{{+}{+}}$ inhibited.

• Applied Biological Chemistry
• /
• v.39 no.6
• /
• pp.466-471
• /
• 1996

The survey on the chitinolytic activity of some plants was performed for the purpose of obtaining some reliable and inexpensive sources of chitinase. Rice, soybean for sprouting, kiwi fruit, almond and crude papain were investigated. Rice bran, seed coat of the soybean and the pericarp of kiwi fruit showed a considerable activity, while the bean after the removal of the seed coat, the mixture of rice integument and endosperm, polished rice, and defatted soybean powder didn't have any detectable activity. These crude enzymes have shown to contain both endo- and exochitinase activity. The effects of pH and temperature on the enzyme activity were variable. Furthermore we have observed the chitosanolytic activity from these enzyme Preparations. The rice bran had the highest activity in the enzymatic degradation of chitosan, and seed coat of soybean and the pericarp of kiwi fruit followed. On the basis of the fact that crude papain was not only commercially available but also the most potent in the endochitinase activity and the lowest in the exochitinase activity, we could conclude that crude papain was considered as the most suitable source of the chitinase among plants studied in this paper. In addition, rice bran was worth further investigation from the point of utilizing agricultural by-product.

• Applied Biological Chemistry
• /
• v.40 no.2
• /
• pp.95-100
• /
• 1997

This study was aimed to survey inexpensive and reliable sources of chitinase from the animal origin. The stomach and its content of the broiler, the cod, the yellowtail and ${\beta}-glucuronidase$ from snail gut showed a considerable chitinolytic activity, while those of the bas didn't have any detectable activity. These crude enzymes was found to have both endo- and exochitinase activity. The effects of pH and temperature on the enzyme activity were variable. The hydrolytic products of colloidal chitin by the enzyme preparation from the broiler and the cod were chitooligomers having the degree of polymerization between 3 and 5. Furthermore we observed the chitosanolytic activity from these enzymes. In the degradation of chitosan the chyme of the broiler had the highest activity and ${\beta}-glucuronidase$ from snail gut followed. On the basis of the fact that the by-product of the broiler was not only commercially available but also the most potent in the endochitinase activity and the lowest in the exochitinase activity, we conclude that the gizzard and its chyme are considered as the most suitable source of the industrial chitinase among animals studied in this paper.

• The Korean Journal of Mycology
• /
• v.26 no.4 s.87
• /
• pp.496-501
• /
• 1998

The mycelia of Tricholoma matsutake DGUM 26001, 26101, 26210 and FRI 91024 were used to determine the extracellular enzyme activity in mycelia. When the filtrate of culture broth after 30-day cultivation at $24^{\circ}C$ was used as a crude solution of extracellular enzyme, the average specific activity of ${\alpha}-amylase$ was 6142.3 unit/mg protein. The specific activity of xylanase was comparatively high. However, little or no enzyme activities were found for ${\beta}-glucosidase$, ligninase, CMCase, chitinase, protease, and lipase.

• Journal of Microbiology and Biotechnology
• /
• v.14 no.2
• /
• pp.337-343
• /
• 2004

A bacterial strain concurrently producing extracellular chitosanase and chitinase was isolated from soil and identified as a member of the $\beta$-subgroup of Proteobacteria through its 16S rRNA analysis and some biochemical analyses. The newly discovered strain, named as KNU3, had 99% homology of its 16S rRNA sequence with chitinolytic $\beta$-Proteobacterium CTE108. Strain KNU3 produced 34 kDa of chitosanase in addition to two chitinases of 68 kDa and 30 kDa, respectively. The purified chitosanase protein (ChoK) showed activity toward soluble, colloidal, and glycol chitosan, but did not exhibit any activity toward colloidal chitin. The optimum pH and temperature of ChoK were 6.0 and $70^{\circ}C$, respectively. The chitosanase was stable in the pH 4.0 to 8.0 range at $70^{\circ}C$, while enzyme activity was relatively stable at below $45^{\circ}C$. MALDI-TOF MS and N-terminal amino acid sequence analyses indicated that ChoK protein is related to chitosanases from Matsuebacter sp. and Sphingobacterium multivorum. HPLC analysis of chitosan lysates revealed that glucosamine tetramers and hexamers were the major products of hydrolysis.