Purification and Mode of Action of Chitosanolytic Enzyme from<i>Enterobacter</i>sp. G-1

Yamasaki, Yukikazu; Hayashi, Isami; Ohta, Yutaka; Nakagawa, Tsuyoshi; Kawamukai, Makoto; Matsuda, Hideyuki

doi:10.1271/bbb.57.444

Cited by 28 publications

(11 citation statements)

References 4 publications

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“…4) glycoside linkage, can be manufactured by hydrolyzing chitosan with chitosanase. Chitosanases are produced by many microorganisms, including fungi, actinomycetes, and bacteria (Boucher, Dupuy, Vidal, Neugebauer & Brzezinski, 1992;Fenton & Eveleigh, 1981;Izume, Nagae, Kawagishi, Mitsutomi, & Ohtakara, 1992;Seino, Tsukud, & Shimasue, 1991;Yamasaki et al, 1993;Yoshihara, Hosokawa, Kubo, Nishiyama & Koba, 1993). The bacterial chitosanases are especially useful for industrial applications because the enzyme can be easily prepared (Akiyama et al, 1999).…”

Section: Introductionmentioning

confidence: 99%

Production of high degree polymerized chitooligosaccharides in a membrane reactor using purified chitosanase from Bacillus cereus

Lin

Hsiao

Chiang

2009

Food Research International

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Section: Introductionmentioning

confidence: 99%

Production of high degree polymerized chitooligosaccharides in a membrane reactor using purified chitosanase from Bacillus cereus

Lin

Hsiao

Chiang

2009

Food Research International

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“…It is thought that the ability to hydrolyze a 100% deacetylated chitin is an important criterion for classifying an enzyme as a chitosanase. Chitosanases are produced by many organisms, including actinomycetes (2,17), fungi (4,27), plants (6,18), and bacteria (7,16,22,29,30). Bacterial chitosanases have received special attention because they are important for the maintenance of the ecological balance and have been used to determine the mechanism of chitosan hydrolysis at both biochemical and molecular levels.…”

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confidence: 99%

Purification, Characterization, and Gene Analysis of a Chitosanase (ChoA) from Matsuebacter chitosanotabidus 3001

et al. 1999

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The extracellular chitosanase (34,000 M r) produced by a novel gram-negative bacterium Matsuebacter chitosanotabidus 3001 was purified. The optimal pH of this chitosanase was 4.0, and the optimal temperature was between 30 and 40°C. The purified chitosanase was most active on 90% deacetylated colloidal chitosan and glycol chitosan, both of which were hydrolyzed in an endosplitting manner, but this did not hydrolyze chitin, cellulose, or their derivatives. Among potential inhibitors, the purified chitosanase was only inhibited by Ag+. Internal amino acid sequences of the purified chitosanase were obtained. A PCR fragment corresponding to one of these amino acid sequences was then used to screen a genomic library for the entire choA gene encoding chitosanase. Sequencing of the choA gene revealed an open reading frame encoding a 391-amino-acid protein. The N-terminal amino acid sequence had an excretion signal, but the sequence did not show any significant homology to other proteins, including known chitosanases. The 80-amino-acid excretion signal of ChoA fused to green fluorescent protein was functional in Escherichia coli. Taken together, these results suggest that we have identified a novel, previously unreported chitosanase.

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“…On the basis of substrate specificity, the previously described chitosanases included enzymes that act toward chitosan specifically (DAVID and EVELEIGH 1984, FENTON and EVELEIGH 1981, PRICE and STORCK 1975, TOMINAGA and TSUJISAKA 1975; enzymes that showed activity toward both chitosan and CMC (HEDGES andWOLFE 1974, OHTAKARA et al 1984); and the chitosanase from Enterobacter sp. G-1 (YAMASAKI et al 1993) which possessed the ability to degrade both chitin and chitosan. B. alvei strain produces two different types of chitosanases, chitosanase A effectively degraded chitosan and chitosanase B displayed detectable activity toward glycol chitin and colloidal chitin.…”

Section: Discussionmentioning

confidence: 99%

Production and some properties of two chitosanases fromBacillus alvei

Abdel-Aziz¹

1999

J. Basic Microbiol.

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Bacillus alvei, a potent chitosanase producer, secreted an extracellular chitosan‐degrading enzyme in the absence of chitosan. Extracellular secretion of chitosanase reached levels corresponding to 2.3 U/ml after less than two days. The enzyme was purified by precipitation with ammonium sulfate followed by CM‐cellulose chromatography. Two chitosanases, chitosanase A and B were purified from the culture fluid. Chitosanase A exhibited substrate specificity for chitosan, while chitosanase B possessed comparable specific activities toward glycol chitin and colloidal chitin. The apparent Km and Vmax, determined at 37 °C and pH 5.6, were 0.8 mg/ml and 2.5 μmol/min, respectively. The enzyme showed an endo‐splitting type of cleavage reaction and the end products of chitosan hydrolysis were oligomeric products.

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Purification and Mode of Action of Chitosanolytic Enzyme fromEnterobactersp. G-1

Cited by 28 publications

References 4 publications

Production of high degree polymerized chitooligosaccharides in a membrane reactor using purified chitosanase from Bacillus cereus

Production of high degree polymerized chitooligosaccharides in a membrane reactor using purified chitosanase from Bacillus cereus

Purification, Characterization, and Gene Analysis of a Chitosanase (ChoA) from Matsuebacter chitosanotabidus 3001

Production and some properties of two chitosanases fromBacillus alvei

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