Publisher Correction: Purification, Biochemical Characterization, and Facile Immobilization of Laccase from Sphingobacterium ksn-11 and its Application in Transformation of Diclofenac.

The original version of this article unfortunately contained a mistake in the equation under "Immobilized Laccase Activity and its Storage Stability" section.

Purification, Biochemical Characterization, and Facile Immobilization of Laccase from Sphingobacterium ksn-11 and its Application in Transformation of Diclofenac.

An extracellular laccase enzyme secreted from Sphingobacterium ksn-11 was purified to electrophoretic homogeneity, showing a molecular weight of 90 kDa. The purified enzyme was monomeric in nature confirmed by sodium dodecyl gel electrophoresis. The optimum temperature and pH were found to be 40 °C and 4.

Imidacloprid impedes mitochondrial function and induces oxidative stress in cotton bollworm, Helicoverpa armigera larvae (Hubner: Noctuidae).

Neonicotinoids have high agonistic affinity to insect nicotinic acetylcholine receptors (nAChR) and are frequently used as insecticides against most devastating lepidopteran insect pests. Imidacloprid influenced dose-dependent decline in the state III and IV respiration, respiration control index (RCI), and P/O ratios, in vitro and in vivo. The bioassay indicated its LD value to be 531.

Evaluation of flubendiamide-induced mitochondrial dysfunction and metabolic changes in Helicoverpa armigera (Hubner).

Phthalic acid diamide insecticides are the most effective insecticides used against most of the lepidopteran pests including Helicoverpa armigera, a polyphagous pest posing threat to several crops worldwide. The present studies were undertaken to understand different target sites and their interaction with insect ryanodine receptors (RyR). Bioassays indicated that flubendiamide inhibited the larval growth in dose-dependent manner with LD value of 0.

Modulation of P-glycoprotein ATPase of Helicoverpa armigera by cholesterol: effects on ATPase activity and interaction of insecticides.

Purified P-glycoprotein ATPase from Helicoverpa armigera (Ha-Pgp), reconstituted in proteoliposomes composed of phospholipids and cholesterol, shows higher ATPase activity in the presence of cholesterol than in its absence. The Ha-Pgp ATPase activity was increased 30-40% with cholesterol. The KM for ATP was found to be 1 and 0.

Modulatory effects of natural curcuminoids on P-glycoprotein ATPase of insecticide-resistant pest Helicoverpa armigera (Lepidopetera: Noctüidae).

Three major curcuminoids (I, II and III) were purified from turmeric and tested for their ability to modulate the function of P-glycoprotein ATPase of the insecticide-resistant pest Helicoverpa armigera (Ha-Pgp). The curcumin mixture inhibited the activity of Ha-Pgp ATPase by 80-90% at 100 μM concentration. Along with curcuminoids I, II and III, it inhibited the verapamil- and ethylparaoxon-stimulated Ha-Pgp ATPase activity.

Purification and characterization of extreme alkaline, thermostable keratinase, and keratin disulfide reductase produced by Bacillus halodurans PPKS-2.

Two alkaline keratinases-I and II secreted by Bacillus halodurans PPKS-2 were purified and characterized. Both the keratinases were purified using ammonium sulfate, DEAE-Sephadex followed by Sephadex G-200 column chromatography. The purification was 21.

P-glycoprotein ATPase from the resistant pest, Helicoverpa armigera: purification, characterization and effect of various insecticides on its transport function.

Helicoverpa armigera is a major pest of agricultural crops and has developed resistance to various insecticides. A P-glycoprotein (Pgp) with ATPase activity likely to be involved in insecticide resistance was purified and characterized from insecticide-resistant H. armigera.

Production of keratinase by free and immobilized cells of Bacillus halodurans strain PPKS-2: partial characterization and its application in feather degradation and dehairing of the goat skin.

An extremely alkaliphilic bacterial strain, Bacillus sp. PPKS-2, was isolated from rice mill effluents and screened for the production of extracellular keratinase. The maximum production of keratinase occurred after 48 h in shaking culture at pH 11.

Differential elicitation of proteases and protease inhibitors in two different genotypes of chickpea (Cicer arietinum) by salicylic acid and spermine.

Elicitation of proteases and protease inhibitors (PIs) by salicylic acid (SA) and spermine (Spm) was investigated in roots and shoots of two different genotypes of chickpea cultivars ICCV10 and L550, which were resistant and susceptible to wilt disease, respectively. SA and Spm were found to suppress the elicitation of proteases in the resistant cv, whereas they induce it in susceptible cv. Elicitation of new trypsin and chymotrypsin inhibitors was observed in the roots and shoots of resistant cv treated with SA and Spm.

Stimulatory effect of insecticides on partially purified P-glycoprotein ATPase from the resistant pest Helicoverpa armigera.

A P-glycoprotein-like protein (Ha-Pgp) was detected in a membrane preparation from the insecticide-resistant pest Helicoverpa armigera (Lepidoptera: Noctüidae) using C219 antibodies that are directed towards an epitope in the nucleotide-binding domains. This protein was partially purified and found to be a glycoprotein displaying ATPase activity. SDS-PAGE confirmed that a high molecular mass glycoprotein (150 kDa) was overexpressed in resistant pests, but was not detected in susceptible pests.