The current study was performed to optimize three different industrial textile effluent biodegradation potentials of a brown rot fungus, Piptoporus betulinus IEBL-3, to reduce environmental pollution. The Response Surface Methodology under the Box Bhenken Design was used for the optimization steps. Three ligninolytic enzymes named lignin peroxidase, manganese peroxidase and laccase were also studied during the biodegradation process. The biodegradation rate of the 3 industrial effluents varied between 67 and 76% at the initially optimized conditions. There was a 10%, 7% and 9% increase in the biodegradation of Mujahid textile (MT), Five Star textile (FST) and Sitara textile (ST) effluent, respectively, after the addition of various additional carbon and nitrogen sources in different ratios. The biological treatment decreases the Biological Oxygen Demand and Chemical Oxygen Demand values of the effluents well below the WHO-recommended values for the industrial effluents. The HPLC monitoring of the effluent’s biodegradation showed the appearance of new peaks, some of which may correspond to secondary amines. Study of ligninolytic enzymes during the biodegradation process confirmed their role in the biodegradation process, with lignin peroxidase having highest activity among the others. These findings suggest that P. betulinus is a potential fungus for the biodegradation of the dyes and effluents and can be a suitable candidate for this process.

Streptomyces species have been exploited widely as microbial cell factories, especially for antibiotic production. However, their potential for alpha-amylase production has not been extensively studied. This study reports the isolation, molecular identification, and optimization of the physiological conditions for alpha-amylase production from Streptomyces sp., isolated from soil in Kotli Azad Kashmir. The maximum growth of Streptomyces MI-1 was observed at a neutral pH and a temperature of 35 °C. An amylase activity of 1.15 IU/mL was observed when 4% starch was added to the nutrient medium. During the submerged state fermentation, the maximum amylase activity of 2.136 IU/mL/min was observed after 144 h of incubation. The characterization of bacterial amylase revealed an optimum temperature of 40 °C, and its optimum pH was 7.0. Furthermore, during the study, examining the effect of different metal ions found that Mg2+ and Ca2+ ions had a positive effect, while Cu2+ and Fe2+ ions had an inhibitory effect compared to the control. This preliminary study provides basal line information for the discovery of novel microbes from the unexplored natural resources for amylase production, which will be used for many purposes.

Ligninolytic enzymes are employed for the production of second-generation biofuel to minimize fuel crisis. Additionally, they play a crucial role in global carbon cycle and a variety of applications in food, agriculture, paper and textile industries. On a large scale production of ligninolytic enzymes, microorganisms can be cultured on lignocellulosic wastes. In the present study, proximate analysis including acid detergent lignin (ADL), acid detergent cellulose (ADC), acid detergent fi ber (ADF) and acid insoluble ash (AIA) were performed for Platanus orientalis (chinar), Bauhinia variegata (orchid tree), Pinus roxburghii (chir pine), wheat straw and wheat husk. Platanus orientalis was selected as substrate because of higher lignin contents for the production of ligninolytic enzymes by Aspergillus flavus. Solid State Fermentation was used and Response Surface Methodology was employed for optimizing various parameters and enzymes production. Maximum production was achieved at temperature 32°C, fermentation period 120 hours, pH 4.5, inoculums size 3.5 mL, substrate mesh size 80 mm, substrate size 7 g. Maximum purifi cation of laccase, manganese peroxidase (MnP) and lignin peroxidase (LiP) was achieved with 50%, 60% and 40% ammonium sulfate respectively and it was enhanced by gel filtration chromatography. Characterization of enzymes shows that Laccase has 35°C optimum temperature, 4.5 pH, 0.289 mM Km and 227.27 μM/ml Vmax. Manganese peroxidase has 30°C optimum temperature, 5.5 pH, 0.538 mM Km and 203.08 μM/ml Vmax. Lignin peroxidase has 30°C optimum temperature, 3 pH, 2 mM Km and 2000 µM/ml Vmax. Protein concentrations found in crude extracts and partially purified enzymes are respectively: laccase 1.78 and 0.71 mg/ml, MnP 1.59 and 0.68 mg/ml. LiP, 1.70 and 0.69 mg/ml.