Purification and characterization of a novel halostable cellulase from Salinivibrio sp. strain NTU-05

Wang, Chung-Yi; Hsieh, Y. F.; Ng, Chang-Chai; Chan, Helen M.; Lin, Hsin-Tang; Tzeng, Wen-Sheng; Shyu, Yuan‐Tay

doi:10.1016/j.enzmictec.2009.02.006

Cited by 94 publications

(52 citation statements)

References 34 publications

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“…In the case of cellulase, to our knowledge, there are no such studies to recover the enzyme, apart from conventional salt precipitation techniques and ion-exchange or gel permeation chromatography using state-of-the-art polymeric resins (Avelino et al 1999;Roy et al 1999;Amritkar et al 2004;Mirzaakhmedov et al 2007;Wang et al 2009). …”

Section: Introductionmentioning

confidence: 99%

Adsorption of Cellulase Isolated from Aspergillus Niger on Chitosan/Alginate Particles Functionalized with Epichlorohydrin

Rodrigues

Bezerra

Farias

et al. 2013

Adsorption Science & Technology

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This work investigates the adsorption of cellulase (isolated from Aspergillus niger) in a fixed-bed column using chitosan/alginate particles functionalized with epichlorohydrin (Cs/Ag-E) as the adsorbent. The particles were prepared and characterized with respect to apparent density, particle porosity, particle size, surface chemistry and thermal stability. Cellulase solutions were prepared in sodium citrate buffer (20 mM) at pH 5. Several breakthrough curves were obtained by varying the flow rate and feed concentrations in order to evaluate the suitable bed height and determine the adsorption isotherm, respectively. The adsorption isotherm fitted well with Langmuir equation with maximum adsorption capacity of about 11 mg of cellulase/g of adsorbent. Successive cycles (adsorption/washing/elution) were performed and the results demonstrate the reversibility of the process and its potential for enzyme purification and separation. However, cellulase activity in the eluted fraction is only 29% of that of the fresh enzyme fed to the column.

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Section: Introductionmentioning

confidence: 99%

Adsorption of Cellulase Isolated from Aspergillus Niger on Chitosan/Alginate Particles Functionalized with Epichlorohydrin

Rodrigues

Bezerra

Farias

et al. 2013

Adsorption Science & Technology

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“…The cellulase was finally purified 22-fold with a recovery of 1.38% and a specific activity of 105.93 U mgG 1 protein as summarized in Table 1. The specific activity of M. gilvus cellulase was higher than those of cellulases produced from Salinivibrio sp., Clostridium thermocellum and Reticulitermes speratus (Wang et al, 2009;Ng and Zeikus, 1981;Watanabe et al, 1997). The SDS-PAGE revealed a few protein bands after purification (Fig.…”

Section: Resultsmentioning

confidence: 99%

“…For zymogram analysis, the clear zones under red background indicate the presence of cellulase enzyme. Arrows indicate the position of cellulase enzyme Lee et al, 2008), but different from the molecular weights of enzymes produced from some (Inoue et al, 2005;Harshvardhan et al, 2013;Mawadza et al, 2000;Annamalai et al, 2013;Wang et al, 2009;Thongekkaew et al, 2008;Lee et al, 2004;Tokuda et al, 1997;Rouland et al, 1988). Optimum condition for cellulase activity: As shown in Fig.…”

Section: Resultsmentioning

confidence: 99%

Purification, Biochemical Characterization of a Macrotermes gilvus Cellulase and Zymogram Analysis

Champasri¹,

Champasri²,

Woranam³

2015

Asian J. of Biochemistry

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Cellulase plays an important role in cellulose degradation. The enzyme catalyzes the cleavage of b-1,4 glycosidic bond between glucose residues. The Macrotermes gilvus cellulase was purified by using ammonium sulfate precipitation and anion exchange column with 1.38% recovery and 22-fold purification. The SDS-PAGE coupled with zymogram analysis revealed the molecular weights approximately of 54 kDa. The biochemical properties of the enzyme exhibited the optimum temperature and optimum pH of 45°C and 5.2. Interestingly, the enzyme was active over a wide range of temperatures (7-70°C) and a broad range of pH values (4.5-8). At the indicated temperatures and pH values, the enzyme exhibited more than 84 and 50% of its activity. The thermal stability and pH stability of the enzyme were also investigated. The result showed that the enzyme retained nearly 40% of its original activity after incubation in mild acidic (pH 5.2), neutral (pH 7.0) and basic (pH 10.0) conditions for 5 h. The enzyme retained its activity more than 70% of initial activity at both 37 and 45°C after incubation for 3 h. Moreover, the activity of the enzyme was strongly inhibited by Cu slightly increased the enzyme activity. Due to the wide temperature and pH range of enzyme activity, the Macrotermes gilvus cellulase might be potential enzyme for industrial or agricultural application.

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“…The Km value of endoxylanase from A. geliboluensis was lower than endoxylanase obtained from Streptomyces cyaneus SN32 (11.1 mg/mL) (Ninawe et al 2008) and Streptomyces althioticus LMZM (43.03 mg/mL) (Luo et al 2016). The Km value of endoglucanase has been reported in the range of 3.0 to 4.0 mg/mL for CMC (Wang et al 2009;Rastogi et al 2010). The kinetics of endoglucanase obtained from Actinomadura sp.…”

Section: Characterization Of Endoxylanase and Endoglucanasementioning

confidence: 99%

Production and Characterization of Partially Purified Thermostable Endoxylanase and Endoglucanase from Novel Actinomadura geliboluensis and the Biotechnological Applications in the Saccharification of Lignocellulosic Biomass

Adıgüzel¹,

Tunçer²

2017

BioResources

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Extracellular endoxylanase and endoglucanase from halo-and thermotolerant Actinomadura geliboluensis were produced, purified, characterized, and used in the saccharification of native and pretreated lignocellulosic biomasses. The molecular mass of endoxylanase and endoglucanase were 30 and 38 kDa, respectively. The optimum pH and temperature values for both endoxylanase and endoglucanase activities were pH 6.0 and 60 °C, respectively. They were both stable within a pH range of 4.0 to 8.0 and up to 70 °C. The half-lives of endoxylanase and endoglucanase at 70 °C were calculated as 180 min and 60 min, while their half-lives at 80 °C were detected as 60 min and 50 min, respectively. Both the endoxylanase and endoglucanase obeyed Michaelis-Menten kinetics. . The potential application of endoxylanase and endoglucanase in saccharification of lignocellulosic biomass was further evaluated. The reduced sugar was 265.12 mg/g biomass after both endoxylanase and endoglucanase were incubated with wheat straw, which was pretreated by 1 % NaOH at 121 °C for 15 min. Endoxylanase and endoglucanase were produced from novel A. geliboluensis, which could potentially be used in biotechnological applications.

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Purification and characterization of a novel halostable cellulase from Salinivibrio sp. strain NTU-05

Cited by 94 publications

References 34 publications

Adsorption of Cellulase Isolated from Aspergillus Niger on Chitosan/Alginate Particles Functionalized with Epichlorohydrin

Adsorption of Cellulase Isolated from Aspergillus Niger on Chitosan/Alginate Particles Functionalized with Epichlorohydrin

Purification, Biochemical Characterization of a Macrotermes gilvus Cellulase and Zymogram Analysis

Production and Characterization of Partially Purified Thermostable Endoxylanase and Endoglucanase from Novel Actinomadura geliboluensis and the Biotechnological Applications in the Saccharification of Lignocellulosic Biomass

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