Aligarh Muslim University

About: Aligarh Muslim University is a education organization based out in Aligarh, Uttar Pradesh, India. It is known for research contribution in the topics: Population & Adsorption. The organization has 8218 authors who have published 16416 publications receiving 289068 citations. The organization is also known as: AMU.

Hydrolysis of milk/whey lactose by β galactosidase: A comparative study of stirred batch process and packed bed reactor prepared with calcium alginate entrapped enzyme

Abstract: Calcium alginate entrapped β galactosidase preparations were used for the hydrolysis of lactose from solution, milk and whey in batch processes as well as in continuous packed bed columns. The efficiency of columns, containing calcium alginate entrapped soluble and crosslinked concanavalin A complex of β galactosidase was examined at various flow rates at room temperature 32 °C, for the continuous hydrolysis of 0.1 M lactose for over 2 months. From the kinetic study the Michaelis constant ( K m ) were found to be 2.51 mM and 5.18 mM for the free and immobilized β galactosidase, respectively. The V max for the soluble enzyme and immobilized preparation was 4.8 × 10 −4 mol/min and 4.2 × 10 −4 mol/min, respectively. Furthermore, we found that entrapped crosslinked Con A–β galactosidase was more efficient in the hydrolysis of lactose present in milk (77%) and whey (86%) in batch processes as compared to the entrapped soluble β galactosidase.

Surface Properties and Mixed Micellization of Cationic Gemini Surfactants with Ethyleneamines

Abstract: Herein, we report the surface properties and mixed micellization of cationic gemini surfactants (butanediyl-1,4-bis(dimethylcetylammonium bromide), pentanediyl-1,5-bis(dimethylcetylammonium bromide), and hexanediyl-1,6-bis(dimethylcetylammonium bromide), respectively referred to as 16-4-16, 16-5-16, and 16-6-16) in the presence of different mole fractions of ethyleneamines (ethylenediamine, diethylenetriamine, triethylenetetramine, and tetraethylenepentamine) at 303 K. The surface properties (critical micelle concentration (CMC), C20 (surfactant concentration required to reduce the surface tension of the solvent by 20 mN·m−1), Γmax (maximum surface excess), Amin (minimum surface area per molecule), and interaction parameter β (for mixed monolayer formation at the aqueous solution/air interface (βσ) and for mixed micelle formation in aqueous medium (βm)) are reported. A synergistic effect has been observed in all instances that were found to be correlated with the chain length of ethyleneamines. The CMC va...

Protein oxidation: an overview of metabolism of sulphur containing amino acid, cysteine.

Abstract: The available data suggest that among cellular constituents, proteins are the major target for oxidation primarily because of their quantity and high rate of interactions with ROS. Proteins are susceptible to ROS modifications of amino acid side chains which alter protein structure. Among the amino acids, Cysteine (Cys) is more prone to oxidation by ROS because of its high nucleophilic property. The reactivity of Cys with ROS is due to the presence of thiol group. In the oxidised form, Cys forms disulfide bond, which are primary covalent cross-link found in proteins, and which stabilize the native conformation of a protein. Indirect evidence suggests that thiol modifications by ROS may be involved in neurodegenerative disorders, but the significance and precise extent of the contributions are poorly understood. Here, we review the role of oxidized Cys in different pathological consequences and its biochemistry may increase the research in the discovery of new therapies. The purpose of this review is to re-examine the role and biochemistry of oxidised Cys residues.