Optimization and partial characterization of endoglucanase produced by Streptomyces sp. B-PNG23

Bettache, Azzeddine; Messis, Abdelaziz; Copinet, Estelle; Kecha, Mouloud; Boucherba, Nawel; Belhamiche, N.; Duchiron, Francis; Benallaoua, Saı̈d

doi:10.2298/abs1302549a

Cited by 26 publications

(12 citation statements)

References 30 publications

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“…NTU-05 (Wanga et al 2009) and Streptomyces sp. B-PNG23 (Azzeddine et al 2013) and similar to that observed for Bacillus subtilis LFS3 (Rawat and Tewari 2012) and Gracilibacillus sp. SK1 (Yu and Li 2015).…”

Section: Characterization Of Purified Endoglucanasesupporting

confidence: 84%

Production, purification, characterization and usage of a detergent additive of endoglucanase from isolated halotolerant Amycolatopsis cihanbeyliensis mutated strain Mut43

Adıgüzel

Tunçer

2017

Biocatalysis and Biotransformation

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The Amycolatopsis cihanbeyliensis Mut43, which is obtained by UV radiation, exhibited endoglucanase activity of 5.21 U/mL, which was $2.3-fold higher than that of the wild strain (2.04 U/mL). The highest enzyme activity was obtained after 3 days of incubation at 32 C, pH 7.0, 150 rpm, and 6% NaCl in a liquid medium containing 1.5% (w/v) wheat straw (0.25 mm of particle size) and 0.6% (w/v) yeast extract. Enzyme activity was eluted as a single peak (gel filtration chromatography), and Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) analysis of the corresponding peak revealed a molar mass of 30 kDa. Zymogram analysis confirmed the presence of a single active endoglucanase component. The enzyme was purified to $21-fold, and the mean overall yield was $6%. The purified endoglucanase was active up to 80 C and showed a half-life of 214 min at 60 C in the absence of substrate at pH 8.0. The apparent K m value for the purified endoglucanase was 0.70 mg/mL, while the V max value was 6.20 Units/lg. Endoglucanase activity was reduced (25%) by treatment with 30 U of proteinase K/mg. The addition of Mg þ2 and Ca þ2 (5 mM) enhanced endoglucanase activity. Additionally, endoglucanase activity in the presence of 5 mM SDS or organic solvents was 75 and 50% of maximum activity, respectively. The high levels of enzyme production from A. cihanbeyliensis Mut43 achieved under batch conditions, coupled with the temperature stability, activity over a broad pH range, relatively high stability (70-80%) in the presence of industrial laundry detergents and storage halflives of 45 days at þ4 C and 75 days at À20 C signify the suitability of this enzyme for industrial applications as detergent additive. ARTICLE HISTORY

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Section: Characterization Of Purified Endoglucanasesupporting

confidence: 84%

Production, purification, characterization and usage of a detergent additive of endoglucanase from isolated halotolerant Amycolatopsis cihanbeyliensis mutated strain Mut43

Adıgüzel

Tunçer

2017

Biocatalysis and Biotransformation

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“…In support of these results the highest cellulase activity of Streptomyces sp. B-PNG23 was observed at 28 °C (Azzeddine et al 2013).…”

Section: Optimization Of Culture Conditions For Production Of Cellulasementioning

confidence: 97%

culture conditions for production of cellulase by Aspergillus tubingensis KY615746 using rice straw waste

El-Nahrawy

Metwally

El-Kodoos

et al. 2017

EBSS

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TWENTY isolates of cellulase producing fungi were isolated from six samples of rotted rice straw which collected from different localities in El-Gharbia Governorate (Basyion), Kafrelsheikh Governorate (Sakha) and El-Dakahlia Governorate (El-Mansoura). On the basis of hydrolysis zone surrounding the colonies, an efficient fungus isolate (F7) for highest cellulolytic activity were chosen. According to morphological and biochemical characteristics as well as 18S rRNA sequence indicated that the isolate belonged to Aspergillus tubingensis KY615746. Effect of culture conditions for production of cellulase enzyme by A. tubingensis were investigated under Submerged Fermentation (SMF) and Solid State Fermentation (SSF) techniques. The optimum conditions for cellulase production by A. tubingensis were the best inoculum size was found to be 3%, pH 4, temperature 30 °C and incubation period 6th day where the reducing sugars attained (0.675, 0.728, 0.731 and 0.913 mg ml -1 ) with maximum activity (0.050, 0.055, 0.053 and 0.063 U ml -1 ), respectively for SMF conditions.On the other hand, the maximum cellulase activity under SSF technique with moisture level 10g : 30ml were (0.16 Ug -), incubation period 9 th day, inoculum size 4 ml:10g, pH 5 and temperature 30 °C where the reducing sugars were (1.412, 1.532, 1.551 and 1.521 mg g -1 ) with maximum activity (0.20, 0.22, 0.23 and 0.23 Ug -1 ), respectively. Based on the results, it may be concluded that rice straw waste can be a potential substrate for produce cellulase by SSF technique.

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“…The optimum temperature of the A. geliboluensis endoglucanase was higher than some other endoglucanases obtained from Streptomyces sp. B-PNG23 (Bettache et al 2013), Bacillus subtilis (Asha and Sakthivel 2014), and Bacillus mycoides S122C (Balasubramanian et al 2012). Some researchers have also recently reported that endoglucanases showed maximum activity at 60 °C and above 60 °C (Saratale et al 2012;Dipasquale et al 2014).…”

Section: Characterization Of Endoxylanase and Endoglucanasementioning

confidence: 97%

“…B-PNG23 (Bettache et al 2013) secreted high amounts of enzyme when the yeast extract was used in the medium. The suitable incubation temperature for endoxylanase and endoglucanase production from A. geliboluensis was determined.…”

Section: Optimization Of Endoglucanase and Endoxylanase Productionmentioning

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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Optimization and partial characterization of endoglucanase produced by Streptomyces sp. B-PNG23

Cited by 26 publications

References 30 publications

Production, purification, characterization and usage of a detergent additive of endoglucanase from isolated halotolerant Amycolatopsis cihanbeyliensis mutated strain Mut43

Production, purification, characterization and usage of a detergent additive of endoglucanase from isolated halotolerant Amycolatopsis cihanbeyliensis mutated strain Mut43

culture conditions for production of cellulase by Aspergillus tubingensis KY615746 using rice straw waste

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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