Purification, characterization, and action mode of a chitosanase from Streptomyces roseolus induced by chitin

Jiang, Xia-Yun; Chen, Daochun; Chen, Liehuan; Yang, Guoning; Zou, Shu‐Ming

doi:10.1016/j.carres.2012.05.002

Cited by 43 publications

(33 citation statements)

References 26 publications

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“…This study was generally consistent with the results of packed purification of another chitosanase, reporting a final yield of 23.6 , 30 , and 17.1% . Regarding applications on unpacked bed purifications, these results are similar to the findings regarding the purification of a C‐phycocyanin , an E. coli ‐based therapeutic and β‐galactosidase .…”

Section: Resultssupporting

confidence: 89%

Recovery and purification of chitosanase produced by Bacillus cereus using expanded bed adsorption and central composite design

Araújo

Pimentel

Silva

et al. 2016

J of Separation Science

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This study presents a system for expanded bed adsorption for the purification of chitosanase from broth extract in a single step. A chitosanase-producing strain was isolated and identified as Bacillus cereus C-01 and used to produce chitosanases. The expanded bed adsorption conditions for chitosanase purification were optimized statistically using STREAMLINE(TM) DEAE and a homemade column (2.6 × 30.0 cm). Dependent variables were defined by the quality criteria purification factor (P) and enzyme yield to optimize the chromatographic process. Statistical analyses showed that the optimum conditions for the maximum P were 150 cm/h load flow velocity, 6.0 cm settled bed height, and 7.36 cm distributor height. Distributor height had a strong influence on the process, considerably affecting both the P and enzyme yield. Optimizing the purification variables resulted in an approximately 3.66-fold increase in the P compared with the value under nonoptimized conditions. This system is promising for the recovery of chitosanase from B. cereus C-01 and is economically viable because it promotes the reduction steps.

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Section: Resultssupporting

confidence: 89%

Recovery and purification of chitosanase produced by Bacillus cereus using expanded bed adsorption and central composite design

Araújo

Pimentel

Silva

et al. 2016

J of Separation Science

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“…The TKU033 chitosanase became more sensitive to pH changes below pH 5 and above pH 9. The decrease of activity at lower and higher pH ranges may be due to the instability of the protein, rather than an acid-base catalytic mechanism, as reported in previous results [ 3 , 21 ].…”

Section: Resultssupporting

confidence: 63%

“…The pH activity profiles of the TKU033 chitosanase revealed maximum activity at pH 5 ( Figure 3 a). The optimum pH (pH 5) for TKU033 chitosanase activity was similar to that of most bacterial chitosanases, which display optimum activities at acidic pH values in a range from 4.5 to 6.5 [ 2 , 3 ]. The pH stability profiles of the TKU033 chitosanase were determined by measurement of the residual activity at pH 7 after incubation at various pH values at 37 °C for 60 min.…”

Section: Resultsmentioning

confidence: 99%

“…These enzymes have been found in abundance in a variety of bacteria [ 1 , 2 , 3 , 4 , 5 , 6 , 7 , 8 , 9 ]. Although chitosanases are efficient in producing chitosan [ 2 , 3 , 4 , 6 ], chitosan has been produced on an industrial scale mostly by the N -deacetylation of chitin using sodium hydroxide [ 10 ]. Among the natural chitinous resources, fishery wastes (crustaceans shells and squid pens) have an especially high content of chitin.…”

Section: Introductionmentioning

confidence: 99%

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Squid Pen Chitin Chitooligomers as Food Colorants Absorbers

et al. 2015

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One of the most promising applications of chitosanase is the conversion of chitinous biowaste into bioactive chitooligomers (COS). TKU033 chitosanase was induced from squid pen powder (SPP)-containing Bacillus cereus TKU033 medium and purified by ammonium sulfate precipitation and column chromatography. The enzyme was relatively more thermostable in the presence of the substrate and had an activity of 93% at 50 °C in a pH 5 buffer solution for 60 min. Furthermore, the enzyme used for the COS preparation was also studied. The enzyme products revealed various mixtures of COS that with different degrees of polymerization (DP), ranging from three to nine. In the culture medium, the fermented SPP was recovered, and it displayed a better adsorption rate (up to 96%) for the disperse dyes than the water-soluble food colorants, Allura Red AC (R40) and Tartrazne (Y4). Fourier transform-infrared spectroscopic (FT-IR) analysis proved that the adsorption of the dyes onto fermented SPP was a physical adsorption. Results also showed that fermented SPP was a favorable adsorber and could be employed as low-cost alternative for dye removal in wastewater treatment.

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“…[16] and Streptomyces sp. [17]. However, most chitosanases have optimum pH values of approximately 5–6 and weak acidic conditions.…”

Section: Introductionmentioning

confidence: 99%

An Amphiprotic Novel Chitosanase from Bacillus mycoides and Its Application in the Production of Chitooligomers with Their Antioxidant and Anti-Inflammatory Evaluation

Liang

Chen

Lin

et al. 2016

IJMS

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The objectives of this investigation were to produce a novel chitosanase for application in industries and waste treatment. The transformation of chitinous biowaste into valuable bioactive chitooligomers (COS) is one of the most exciting applications of chitosanase. An amphiprotic novel chitosanase from Bacillus mycoides TKU038 using squid pen powder (SPP)-containing medium was retrieved from a Taiwan soil sample, which was purified by column chromatography, and characterized by biochemical protocol. Extracellular chitosanase (CS038) was purified to 130-fold with a 35% yield, and its molecular mass was roughly 48 kDa. CS038 was stable over a wide range of pH values (4–10) at 50 °C and exhibited an optimal temperature of 50 °C. Interestingly, the optimum pH values were estimated as 6 and 10, whereas CS038 exhibited chitosan-degrading activity (100% and 94%, respectively). CS038 had Km and Vmax values of 0.098 mg/mL and 1.336 U/min, separately, using different concentrations of water-soluble chitosan. A combination of the high performance liquid chromatography (HPLC) and matrix-assisted laser desorption ionization-time of flight (MALDI-TOF) mass spectrometer data revealed that the chitosan oligosaccharides obtained from the hydrolysis of chitosan by CS038 comprise oligomers with multiple degrees of polymerization (DP), varying from 3–9, as well as CS038 in an endolytic fashion. The TKU038 culture supernatant and COS mixture exhibited 2,2-diphenyl-1-picrylhydrazyl (DPPH) scavenging activities. The COS activities were dose dependent and correlated to their DP. The COS with high DP exhibited enhanced DPPH radical scavenging capability compared with COS with low DP. Furthermore, the COS exhibited inhibitory behavior on nitric oxide (NO) production in murine RAW 264.7 macrophage cells, which was induced by Escherichia coli O111 lipopolysaccharide (LPS). The COS with low DP possesses a more potent anti-inflammatory capability to decrease NO production (IC50, 76.27 ± 1.49 µg/mL) than that of COS with high DP (IC50, 82.65 ± 1.18 µg/mL). Given its effectiveness in production and purification, acidophilic and alkalophilic properties, stability over ranges of pH values, ability to generate COS, antioxidant activity, and anti-inflammatory, CS038 has potential applications in SPP waste treatment and industries for COS production as a medical prebiotic.

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Purification, characterization, and action mode of a chitosanase from Streptomyces roseolus induced by chitin

Cited by 43 publications

References 26 publications

Recovery and purification of chitosanase produced by Bacillus cereus using expanded bed adsorption and central composite design

Recovery and purification of chitosanase produced by Bacillus cereus using expanded bed adsorption and central composite design

Squid Pen Chitin Chitooligomers as Food Colorants Absorbers

An Amphiprotic Novel Chitosanase from Bacillus mycoides and Its Application in the Production of Chitooligomers with Their Antioxidant and Anti-Inflammatory Evaluation

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