A. K. Saran on Modernity, Indian Tradition and Sociology in India

Abstract

The presence of complexity in the electronic structure of strongly correlated electron system NdCoO3 (NCO) have sparked interest in the investigation of its physical properties. Here, we study the the Seebeck coefficient (α) of NCO by using the combined experimental and DFT+U based methods. The experimentally measured α is found to be ∼ 444 µV /K at 300 K, which decreases to 109.8 µV /K at 600 K. In order to understand the measured α, we have calculated the PDOS and band structure of the NCO. Furthermore, the calculated occupancy of 6.4 for Co 3d orbitals and presence of large unoccupied O 2p states indicate the covalent nature of the bonding. Apart from this, the maximum effective mass is found to be 36.75 (28.13) for the spin-up (dn) channel in conduction band indicates the n-type behaviour of the compound in contrast to our experimentally observed p-type behaviour. While, the calculated α at the temperature-dependent chemical potential (µ) at 300 K shows the p-type behaviour of the compound. Fairly good agreement is seen between the calculated and measured values of α at U f f = 5.5 eV and U dd = 2.7 eV. The maximum power factor (PF) is found to be 47.6 (114.4) × 10 14 µW K −2 cm −1 s −1 at 1100 K, which corresponds to p (n)-type doping of ∼ 1.4 (0.7) × 10 21 cm −3 . This study suggests the importance of strong on-site electron correlation in understanding the thermoelectric property of the compound.

Strawberry Protease as a Laundry Detergent Additive Candidate: Immobilization, Compatibility Study with Detergent Ingredients, and Washing Performance Test

“…It was reported that while the enzyme considerably retained its activity in the presence of Triton-X 100 and Tween-80, it almost completely lost its activity in the presence of SDS. [43] Strawberry protease appears to be more stable than both enzymes in the presence of surfactants. A study by Mahakhan et al examined the stability of B. gibsonii 6BS15-4 alkaline protease in the presence of oxidizing agents and found that this enzyme gave similar results to strawberry protease in the presence of NaBO 3 , but was much more stable in the presence of hydrogen peroxide.…”

“…It was reported that the crude protease remained stable in the presence of Perwoll after 1 h of incubation at 30 °C, and apparent losses occurred in the presence of Persil and Ariel. [41] The stability of protease enzymes purified from two separate plant sources, Phalaris minor seeds [42] and Artocarpus heterophyllus seeds, [43] in the presence of various surfactants, was examined. The effect of Triton-X100, SDS, Tween-20, and Tween-80 surfactants on Phalaris minor seed protease activity at different concentration levels (0.1%, 0.5%, and 1%) was tested.…”