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

Abstract

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

Biochemical characterization of a novel thermo‐halo‐tolerant GH5 endoglucanase from a thermal spring metagenome

“…The activity of Cel M was noted to be considerably tolerant to the commercial detergents procured from the local market, for example, Surf Excel, Tide, Ariel, Wheel, and Patanjali, displaying about 50% relative activity in the presence of these detergent samples (Figure 6b). The data on detergent compatibility of Cel M endorse its potential utility in the industrial applications that employ detergents (Adıgüzel & Tunçer, 2017).…”

Functional Analysis of a Highly Active β-Glucanase from Bispora sp. MEY-1 Using Its C-terminally Truncated Mutant

“…In the animal feed industry, the enzymes are used as supplements to enhance feed digestibility and conversion, to eliminate antinutritional factors, and to reduce environmental pollution problems, such as sticky droppings. , In the brewing industry, glucanases are added to reduce the turbidity and viscosity of brewer mash, as well as to produce high-quality brewer malt . In laundry detergents, β-glucanases are used to remove β-glucan stains . This broad application spectrum promotes the research and development of β-glucanases with high catalytic activity to decrease the quantity of enzyme used, increase their utilization efficiency, and reduce the cost.…”

“…7 In laundry detergents, β-glucanases are used to remove βglucan stains. 8 This broad application spectrum promotes the research and development of β-glucanases with high catalytic activity to decrease the quantity of enzyme used, increase their utilization efficiency, and reduce the cost.…”