<span style="font-size:15.0pt;mso-bidi-font-family:"Times New Roman";mso-bidi-font-weight: bold" lang="EN-GB">Submerged fermentation and characterization of <span style="font-size:15.0pt;mso-bidi-font-family:"Times New Roman";mso-fareast-language: EN-IN" lang="EN-GB">carboxymethyl cellulase<span style="font-size:15.0pt; mso-bidi-font-family:"Times New Roman";mso-bidi-font-weight:bold" lang="EN-GB"> from a rhizospheric isolate of <i style="mso-bidi-font-style:normal"><span style="font-size:15.0pt;mso-bidi-font-family:"Times New Roman"; mso-fareast-language:EN-IN" lang="EN-GB">Trichoderma</span></i><span style="font-size:15.0pt;mso-bidi-font-family:"Times New Roman";mso-fareast-language: EN-IN" lang="EN-GB"> <i style="mso-bidi-font-style:normal">viride </i><span style="font-size:15.0pt;mso-bidi-font-family:"Times New Roman"; mso-bidi-font-weight:bold" lang="EN-GB">associated with <i>Azadirachta indica</i> </span></span></span></span></span>

Abstract

225-230<span style="font-size:9.0pt;mso-bidi-font-family: " times="" new="" roman""="" lang="EN-GB">Analysis of process parameters influencing the submerged fermentation <span style="font-size:9.0pt;mso-fareast-font-family: E-BZ;mso-bidi-font-family:" times="" new="" roman""="" lang="EN-GB">of carboxymethyl cellulase by Trichoderma viride <span style="font-size:9.0pt;mso-fareast-font-family: E-BZ;mso-bidi-font-family:" times="" new="" roman""="" lang="EN-GB">isolated from <span style="font-size:9.0pt;mso-bidi-font-family: " times="" new="" roman";mso-bidi-font-weight:bold"="" lang="EN-GB">Azadirachta indica rhizosphere<span style="font-size:9.0pt;mso-fareast-font-family:E-BZ;mso-bidi-font-family: " times="" new="" roman""="" lang="EN-GB"> <span style="font-size:9.0pt;mso-bidi-font-family: " times="" new="" roman""="" lang="EN-GB">showed that the highest enzyme yield was obtained with <span style="font-size:9.0pt;mso-fareast-font-family: E-BZ;mso-bidi-font-family:" times="" new="" roman""="" lang="EN-GB">carboxymethyl cellulose and ammonium sulphate as nutritional supplements at an optimum pH, temperature, incubation period and <span style="font-size:9.0pt;mso-fareast-font-family: " ms="" mincho";mso-bidi-font-family:"times="" new="" roman";mso-ansi-language:en-my"="" lang="EN-MY">inoculum volume <span style="font-size:9.0pt;mso-bidi-font-family: " times="" new="" roman""="" lang="EN-GB">of 5.0, 30°C, 72 h and 1% (v/v), respectively. Sodium dodecyl sulphate polyacrylamide gel electrophoresis revealed the apparent molecular weight of the purified enzyme to be 55 kDa. The enzyme exhibited a Vmax value of 83.7 µg/min and Km value of 0.53 mg/ml. Optimal activity of the enzyme at 50<span style="font-size:9.0pt; mso-bidi-font-family:" times="" new="" roman""="" lang="EN-GB">°C and pH 5.0 emphasizes its potential to be utilized in textile industry operations. </span