On Certain Algebraic Aspects of a Family of Orthogonal Polynomials

[Abstract not available

A new strategy for improvement of tamarind seed based chicken diet after microbial detannification and assessment of its safety aspects

Tamarind seed, an abundant agricultural waste, contains a large amount of naturally occurring anti-nutrient, tannin. This study aimed at evaluating the detannification efficiency of tannase producing Bacillus subtilis PAB2 in comparison with enzymatic and conventional physical techniques, and assessment of its health promoting effect in chicken model. Microbial fermentation resulted in lowering of 80.8% tannin, whereas enzymatic and physical treatment removed only 48 and 28.6%, respectively. To assess the health beneficial effects, experimental schedule for poultry chicken model was designed viz., (T1) commercial food, (T2) T1+tamarind seeds, (T3) T1+enzymatic detannified seeds and (T4) T1+ fermented seeds. It was found that physiological indices of chicken in T4 group improved more than T2, but those were comparable with T1 and T3. The level of total plasma protein, albumin and other haematological parameters also significantly (P<0.05) improved in T4 more than T2. The quantities of small intestinal indicator microbes like Escherichia coli, Clostridium perfringens and Yeast sp. in T4 group increased more than T2. Thus, fermentation led to quality improvement of raw tamarind seed which suggested its employment as an alternative feedstock for poultry chicken

Thermodynamic and kinetic characteristics of an a-amylase from Bacillus licheniformis SKB4

An amylolytic bacterial strain, Bacillus licheniformis SKB4 produced maximum amylase at pH 6.5 at 42 °C, and at late stationary phase (24 h) of growth. Starch and peptone were found the best supporting carbon and nitrogen source with C:N ratio of 1:2 for amylase production. The purified enzyme was non-responsive to most of the metal ions except K+ and Mg++ (1.0 mM). The enzyme was stable and active at pH 6.5. The enzyme showed optimum temperature at 90 °C with 10 min of half life (t½) at 100 °C. The Q10 of the enzyme was 1.0. The thermodynamic principles like activation energy, free energy for substrate binding and transition state of the enzyme were found 31.53, 5.53 and -17.4 KJ/Mol of starch, respectively. The kinetic constant like Vmax, Km, K catand catalytic efficiency (Kcat/Km)for starch were found to be 1.04 μmol mg-1 min-1, 6.2 mg ml-1,2 × 103 S-1 and 3.22 × 102 ml mg-1 S-1,respectively. All these findings suggested that this amylase has unique characteristics for starch hydrolysis in respect to thermostability and kinetic properties