We isolated a mutant that produced higher levels of curdlan than the wild strain Agrobacterium sp. ATCC 31750 by chemical mutagenesis using N-methyl-N-nitro-nitrosoguanidine. The mutant strain produced 66 g/L of curdlan in 120 h with a yield of (0.88) while, the wild strain produced 41 g/L in 120 h with a yield of (0.62) in a stirred bioreactor. The mutant could not produce curdlan when the pH was shifted from 7.0 to 5.5 after nitrogen depletion as followed for wild strain. In contrast, pH optimum for cell growth and curdlan production for mutant was found to be 7.0. We optimized the downstream processing of curdlan by varying different volumes of NaOH and HCl for extraction and precipitation of curdlan. The molecular weight of the purified curdlan from the wild and mutant strain was 6.6 × 105 Da and 5.8 × 105 Da respectively. The monosaccharide analyses confirm that curdlan from both wild and mutant strain contains only glucose units. From the NMR and FTIR data, it has been confirmed that curdlan was exclusively composed of β (1 → 3)-D-glucan residues.
The effect of salt, pH, and temperature stress on the cellular level of antioxidant enzymes, catalase and superoxide dismutase (SOD) and glycerol-3-phosphate dehydrogenase (G3PDH) was studied in Debaryomyces nepalensis NCYC 3413, a halotolerant yeast. The catalase activity increased in different phases, while SOD and G3PDH activities declined in late stationary phase. A significant increase in SOD activity was observed under different stress as compared to control. Salt and temperature stress enhanced the catalase activity where as it was suppressed by pH stress. G3PDH level increased with salt stress, however, no significant change was observed under pH and temperature stress. The observations recorded in this investigation suggested that D. nepalensis has an efficient protective mechanism of antioxidant enzymes and G3PDH against salt, pH, and temperature stresses.
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