Proteases are one of the largest groups of hydrolytic enzymes constituting about 60% of total worldwide sales of industrial enzymes due to their wide applications in detergent, leather, textile, food and pharmaceutical industry. Microbial proteases have been preferred over animal and plant proteases because of their fundamental features and ease in production. Bacillus infantis SKS1, an alkaline protease producing bacteria has been isolated from garden soil of north India and identified using morphological, biochemical and molecular methods. 16S rDNA sequence amplified using universal primers has 99% sequence identity with corresponding gene sequence of Bacillus infantis strain FM 34 and Bacillus sp. Beige. The bacterial culture and its 16S rDNA gene sequence have been deposited to Microbial Culture Collection (Pune, India) with accession number MCC 3035 and GenBank with accession number KR092197 respectively. The partially purified extract of Bacillus infantis SKS1 was thermostable and active in presence of Mg 2+ , acetyl acetone and laundry detergents implicating its application in industry. Production of these enzymes using this strain was maximized by optimization of various parameters including temperature, pH, media components and other growth conditions. Our results show that fructose and dextrose serve as the best carbon sources for production of these enzymes, highlighting the use of this strain for enzyme production utilizing relatively inexpensive substrates like beet molasses and corn steep liquor. Additionally, this strain showed maximum production of enzymes at 40˚C similar to bacterial species used for commercial production of alkaline proteases. Characterization of alkaline proteases from this strain of Bacillus infantis and optimization of parameters for its production would help in understanding its industrial application and large-scale production.

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In this study, simultaneous saccharification and fermentation (SSF) was employed to produce ethanol from 1% sodium hydroxide-treated rice straw in a thermostatically controlled glass reactor using 20 FPU gds⁻¹ cellulase, 50 IU gds⁻¹ β-glucosidase, 15 IU gds⁻¹ pectinase and a newly isolated thermotolerant Pichia kudriavzevii HOP-1 strain. Scanning electron micrograph images showed that the size of the P. kudriavzevii cells ranged from 2.48 to 6.93 μm in diameter while the shape of the cells varied from oval, ellipsoidal to elongate. Pichia kudriavzevii cells showed extensive pseudohyphae formation after 5 days of growth and could assimilate sugars like glucose, sucrose, galactose, fructose, and mannose but the cells could not assimilate xylose, arabinose, cellobiose, raffinose, or trehalose. In addition, the yeast cells could tolerate up to 40% glucose and 5% NaCl concentrations but their growth was inhibited at 1% acetic acid and 0.01% cyclohexamide concentrations. Pichia kudriavzevii produced about 35 and 200% more ethanol than the conventional Saccharomyces cerevisiae cells at 40 and 45°C, respectively. About 94% glucan in alkali-treated rice straw was converted to glucose through enzymatic hydrolysis within 36 h. Ethanol concentration of 24.25 g l⁻¹ corresponding to 82% theoretical yield on glucan basis and ethanol productivity of 1.10 g l⁻¹ h⁻¹ achieved using P. kudriavzevii during SSF hold promise for scale-up studies. An insignificant amount of glycerol and no xylitol was produced during SSF. To the best of our knowledge, this is the first study reporting ethanol production from any lignocellulosic biomass using P. kudriavzevii.

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This study reports the purification and characterization of β-glucosidase from a newly isolated thermophilic fungus, Melanocarpus sp. Microbial Type Culture Collection (MTCC) 3922. The molecular weight of βglucosidase was determined to be ~ 92 and 102 kDa with SDS PAGE and gel filtration, respectively, and pI of ~ 4.1. It was optimally active at 60ºC and pH 6.0, though was stable at 50ºC and pH 5.0-6.0. The presence of *Corresponding author DTT, mercaptoethanol and metal ions such as Na + , K + , Ca 2+ , Mg 2+ and Zn 2+ positively influenced the activity of β-glucosidase but the activity was inhibited in the presence of CuSO 4. β-Glucosidase recognized pNP-βglucopyranoside (pNPG) as the preferred substrate, and showed very low affinity for pNP-β-D-cellobioside. K m and V max for the hydrolysis of pNPG by β-glucosidase was calculated as 3.3 mM and 43.68 µmolmin-1 mg