Isolation and characterization of a novel hen egg white lysozyme inhibitor from Bacillus subtilis I-139.

Murao, Sawao; Kato, Masataka; Wang, San-Lang; Hoshino, Masami; Arai, Motoo

doi:10.1271/bbb1961.54.1129

Cited by 6 publications

(4 citation statements)

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“…Plant and animal sources of chitinase/lysozyme have been frequently reported (1,2,9,14,17,19,47), whereas, bifunctionality of microbial chitinases is rare. It is interesting that the lytic activity (against M. lysodeikticus cells) of chitinases from plant sources is low in comparison to chitinase activity and that the chitinolytic activity (against colloidal chitin) of chitinases from animal sources is low in comparison to lytic activity (21). The K-187 chitinases seem to be similar to the enzymes from plant sources.…”

Section: Discussionmentioning

confidence: 99%

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Purification and characterization of two bifunctional chitinases/lysozymes extracellularly produced by Pseudomonas aeruginosa K-187 in a shrimp and crab shell powder medium

Wang

Chang

1997

Appl Environ Microbiol

203

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Two extracellular chitinases (FI and FII) were purified from the culture supernatant of Pseudomonas aeruginosa K-187. The molecular weights of FI and FII were 30,000 and 32,000, respectively, by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and 60,000 and 30,000, respectively, by gel filtration. The pIs for FI and FII were 5.2 and 4.8, respectively. The optimum pH, optimum temperature, pH stability, and thermal stability of FI were pH 8, 50؇C, pH 6 to 9, and 50؇C; those of FII were pH 7, 40؇C, pH 5 to 10, and 60؇C. The activities of both enzymes were activated by Cu 2؉ ; strongly inhibited by Mn 2؉ , Mg 2؉ , and Zn 2؉ ; and completely inhibited by glutathione, dithiothreitol, and 2-mercaptoethanol. Both chitinases showed lysozyme activity. The purified enzymes had antibacterial and cell lysis activities with many kinds of bacteria. This is the first report of a bifunctional chitinase/lysozyme from a prokaryote. Chitin, a homopolymer of N-acetyl-D-glucosamine (Glc-NAc) residues linked by ␤1-4 bonds, is the most abundant renewable natural resource after cellulose (4). It is widely distributed in nature as the integuments of insects and crustaceans and as a component of fungi and algae (23). It is estimated that the worldwide annual recovery of chitin from the processing of marine invertebrates, for example, is 37,300 metric tons (32). Chitin and its derivatives are of interest because they have various biological activities, such as those of an immunoadjuvant and a flocculant of wastewater sludge, and agrochemical uses (7). Chitooligosaccharides are prepared by partial hydrolysis of chitin with hydrochloric acid or enzymatically by degradation and transglycosylation. This pretreated chitin is then mixed with a chitinolytic enzyme to hydrolyze it to the monomer or oligomer of N-acetylglucosamine. Chitinases, a group of enzymes capable of degrading chitin directly to low-molecular-weight products, have been shown to be produced by a number of microorganisms. Almost all of the reported chitinase-producing strains will use chitin or colloidal chitin as a carbon source (42). Commercial interest in the utilization of chitin and its derivatives has led to the need for inexpensive, reliable sources of active and stable chitinase preparations. The production of inexpensive chitinolytic enzymes is an important element in the utilization of shellfish wastes that not only solves environmental problems but also promotes the economic value of the marine products (42). Some animal and higher plant chitinases have lysozyme activity (chitinase/lysozyme), while bifunctional chitinases have not been isolated from microorganisms. We reported the medium composition and the character of crude chitinase from Pseudomonas aeruginosa K-187 in a previous paper (42). In the present study, we isolated two kinds of bifunctional chitinases/ lysozymes from K-187 cell-free culture broth. This paper describes the purification and characterization of these enzymes. MATERIALS AND METHODS Materials. The shrimp and crab shell powder (SCSP) ...

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Section: Discussionmentioning

confidence: 99%

“…The turbidimetric assay for bacterial cell-lytic enzyme was performed by the same method described above. Lysozyme activity was also measured as an increase in reducing power resulting from hydrolysis of EGC (in 50 mM phosphate buffer, pH 7) at 37ЊC for 30 min (21).…”

mentioning

confidence: 99%

Purification and characterization of two bifunctional chitinases/lysozymes extracellularly produced by Pseudomonas aeruginosa K-187 in a shrimp and crab shell powder medium

Wang

Chang

1997

Appl Environ Microbiol

203

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“…If this were indeed the case, one would expect to find lysozyme inhibitors to be widely distributed in bacteria. However, a [38,39], two proteins in P. aeruginosa [40] and a glycoprotein in Enterobacter cloacae [41]. We have constructed an E. coli MG1655 derivative that overexpresses Ivy from an arabinose-inducible promoter and one in which the ivy gene was knocked out by insertion of a Kan resistance cassette.…”

Section: Discussionmentioning

confidence: 99%

Periplasmic lysozyme inhibitor contributes to lysozyme resistance in Escherichia coli

Deckers

Masschalck

Aertsen

et al. 2004

Cellular and Molecular Life Sciences (CMLS)

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The product of the Escherichia coli ORFan gene ykfE was recently shown to be a strong inhibitor of C-type lysozyme in vitro. The gene was correspondingly renamed ivy (inhibitor of vertebrate lysozyme), but its biological function in E. coli remains unknown. In this work, we investigated the role of Ivy in the resistance of E. coli to the bactericidal effect of lysozyme in the presence of outer-membrane-permeabilizing treatments. Both in the presence of lactoferrin (3.0 mg/ml) and under high hydrostatic pressure (250 MPa), the lysozyme resistance of E. coli MG1655 was decreased by knock-out of Ivy, and increased by overexpression of Ivy. However, knock-out of Ivy did not increase the lysozyme sensitivity of an E. coli MG1655 mutant previously described to be resistant to lysozyme under high pressure. These results indicate that Ivy is one of several factors that affect lysozyme resistance in E. coli, and suggest a possible function for Ivy as a host interaction factor in commensal and pathogenic E. coli.

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“…The mixture was incubated at 37 o C for 30 min. (Murao et al, 1990). Table 1 summarizes the results of the purification of chitinase from Streptomyces sp.…”

Section: Activity Of Chitinase On Different Substratesmentioning

confidence: 99%

Purification and Characterization of Chitinase from Streptomyces sp. M-20

Kim¹,

Yang²,

Kim³

2003

BMB Reports

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Isolation and characterization of a novel hen egg white lysozyme inhibitor from Bacillus subtilis I-139.

Cited by 6 publications

References 1 publication

Purification and characterization of two bifunctional chitinases/lysozymes extracellularly produced by Pseudomonas aeruginosa K-187 in a shrimp and crab shell powder medium

Purification and characterization of two bifunctional chitinases/lysozymes extracellularly produced by Pseudomonas aeruginosa K-187 in a shrimp and crab shell powder medium

Periplasmic lysozyme inhibitor contributes to lysozyme resistance in Escherichia coli

Purification and Characterization of Chitinase from Streptomyces sp. M-20

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