Biochemical and thermodynamic characterization of de novo synthesized β-amylase from fenugreek.

β-Amylase has been de novo synthesized from germinating fenugreek seeds. Enzyme has been isolated and purified from 36 h germinated seeds with 226-fold purification and specific activity of 763 U/mg. Homogeneity of the purified β-amylase has been confirmed with size-exclusion chromatography, SDS-PAGE and MALDI MS/MS analysis.

Exploration of Phytochemicals Found in sp. and their Antiretroviral Activities.

The human immunodeficiency virus (HIV) infects cells of the immune system and destroys their function. Approximately, 2 million people die every year from HIV as reported by the World Health Organization. HIV/AIDS is difficult to treat as the virus continuously develops resistance to drugs being developed.

Cadamba: A miraculous tree having enormous pharmacological implications.

The Cadamba is one of the important medicinal plants belonging to the Rubiaceae family. It is crucially significant as it has the largest number of phytochemicals and secondary metabolites (viz., cadambagenic acid, cadamine, quinovic acid, β-sitosterol, cadambine, etc.

Response surface analysis of nano-ureases from Canavalia ensiformis and Cajanus cajan.

Ureases isolated from leguminous sources, Canavalia ensiformis and Cajanus cajan were immobilized onto gold nanoparticles (nano-ureases). Optimization of the urease immobilization was carried using response surface methodology based on Central Composite Design. Immobilization efficiency of nano-urease from C.

Insights into pH-induced conformational transition of β-galactosidase from Pisum sativum leading to its multimerization.

Although β-galactosidases are physiologically a very important enzyme and have may therapeutics applications, very little is known about the stability and the folding aspects of the enzyme. We have used β-galactosidase from Pisum sativum (PsBGAL) as model system to investigate stability, folding, and function relationship of β-galactosidases. PsBGAL is a vacuolar protein which has a tendency to multimerize at acidic pH with protein concentration ≥100 μg mL⁻¹ and dissociates into its subunits above neutral pH.

Lactose nano-probe optimized using response surface methodology.

A lactose nano-probe has been developed by immobilization of PsBGAL onto gold nanoparticles (AuNps). It is helpful for severe lactose intolerants for quality check of lactose hydrolyzed milk and estimation of hidden lactose present in variety of food products. Optimization of PsBGAL immobilization onto AuNps using spacer arm (cysteamine-glutaraldehyde) was carried out by response surface methodology (Box-Behnken design).

A beta-galactosidase from pea seeds (PsBGAL): purification, stabilization, catalytic energetics, conformational heterogeneity, and its significance.

A basic glycosylated beta-galactosidase (PsBGAL) has been purified from pea seeds by 910-fold with a specific activity of 77.33 mumoL min(-1) mg(-1) protein. The purified enzyme is an electrophoretically homogeneous protein consisting of a single protein band with an apparent M(r) of 55 kDa, while the deglycosylated enzyme has a M(r) of 54.

Optimal immobilization of beta-galactosidase from Pea (PsBGAL) onto Sephadex and chitosan beads using response surface methodology and its applications.

Response surface methodology (RSM) and centre composite design (CCD) were used to optimize immobilization of beta-galactosidase (BGAL) from Pisum sativum onto two matrices: Sephadex G-75 and chitosan beads. The immobilization efficiency of 75.66% and 75.

Stabilization of beta-galactosidase (from peas) by immobilization onto amberlite MB-150 beads and its application in lactose hydrolysis.

The soluble PsBGAL (from Pisum sativum ) is extremely unstable with loss of over 80% in enzyme activity within 24 h at 4 degrees C when the protein concentration was lower than 0.1 mg/mL. Enzyme immobilization onto Amberlite MB-150 beads (diameter = 5 microm) greatly stabilized the enzyme preparation, with almost no loss for 12 months at room temperature (27 degrees C).