Correlation between total phenolic and flavonoid contents and biological activities of 12 ethanolic extracts of Iranian propolis.

Propolis is a resinous substance produced by honey bees that is very popular as a natural remedy in traditional medicine. The current research is the first study on the biological properties of ethanolic extracts of propolis (EEP) from several different regions (12) of Iran. Total phenolic and flavonoid contents (TPC and TFC) of Iranian EEPs were variable between 26.

Effects of synonymous mutations on kinetic properties and structure of firefly luciferase: Molecular dynamics simulation, molecular docking, RNA folding, and experimental study.

Although synonymous mutations have long been thought to lack striking results, a growing body of research shows these mutations have highly variable effects. In this study, the impact of synonymous mutations in the development of thermostable luciferase was investigated using a combination of experimental and theoretical approaches. Using bioinformatics analysis, the codon usage features in the Lampyridae family's luciferases were studied and four synonymous mutations of Arg in luciferase were created.

Modeling and optimization of radish root extract drying as peroxidase source using spouted bed dryer.

The main advantages of the dried enzymes are the lower cost of storage and longer time of preservation for industrial applications. In this study, the spouted bed dryer was utilized for drying the garden radish (Raphanus sativus L.) root extract as a cost-effective source of the peroxidase enzyme.

Immobilization of Lepidium draba peroxidase on a novel Zn-MOF nanostructure.

In the present study, ultrasound irradiation was utilized to synthesize a novel zinc metal-organic framework (MOF). Scanning electron microscopic images, exhibited homogenous morphology with a nano-sized distribution of the Zn-MOF structure as also confirmed by X-ray diffraction patterns. Following, physical immobilization of Lepidium draba peroxidase (LDP) were optimized on the Zn-MOF in phosphate buffer (50 mM, pH 6.

Upregulation of pluripotent long noncoding RNA ES3 in HER2-positive breast cancer.

Breast cancer is the second most common cancer and estimates to be responsible for 20% of all cancer patients. Breast cancer has several subtypes including luminal A, luminal B, normal breast-like, basal-like, and human epidermal growth factor receptor 2 (HER2)-enriched. HER2-positive breast cancer cells have higher HER2 expression than other breast cancer subtypes.

Improvement of kinetic properties and thermostability of recombinant Lepidium draba peroxidase (LDP) upon exposed to osmolytes.

In this study, effects of different concentrations of glycine and D-sorbitol were analyzed on the activity and thermostability of recombinant Lepidium draba peroxidase (LDP). Based on the results, activity of the enzyme increased in the presence of various concentrations of these osmolytes. Maximum activity was detected for the enzyme in the presence of 300 mM glycine and 600 mM sorbitol.

Optimization of in vitro refolding conditions of recombinant Lepidium draba peroxidase using design of experiments.

The main objective of this study was to optimize the in vitro refolding conditions of the recombinant Lepidium draba peroxidase (LDP). Initially, the effects of various factors were investigated on LDP refolding yield using one-factor-at-a-time (OFAT) method. Based on the OFAT results, optimum concentrations for LDP refolding were 2 M urea, 2 mM CaCl, 0.

Heterologous Expression, Purification and Characterization of a Peroxidase Isolated from Lepidium draba.

Peroxidase is one of the most widely used enzymes in biotechnology and medicine. In the current study, cDNA encoding peroxidase from Lepidium draba (LDP) was cloned and expressed in Escherichia coli BL21 (DE3) cells in the form of inclusion bodies (IBs). To achieve purified active enzyme, IBs were solubilized before being purified and refolded.

In silico locating the immune-reactive segments of Lepidium draba peroxidase and designing a less immune-reactive enzyme derivative.

Peroxidases have broad applications in industry, environmental as well as pharmaceutical and diagnosis. Recently applicability of peroxidases in cancer therapy was mentioned. In the present study, a horseradish peroxidase homologue from Lepidium draba was subjected to in silico analyzes aiming at identifying and locating immune-reactive regions.

Implication of Arg213 and Arg337 on the kinetic and structural stability of firefly luciferase.

Possible roles of two different Arginine (Arg; R) 213 and 337 on kinetic and structural stability of Photinus pyralis luciferase have been investigated using thermal and chemical denaturation studies. This enzyme is highly sensitive to protease digestion and temperature, which limits its fieldability, particularly for in vivo imaging. In order to generate more stable luciferases against trypsin digestion, site-directed mutagenesis was conducted to block two representative tryptic sites on the surface of N-terminal domain, via substitution of Arg213 and Arg337 by methionine (Met; M) and glutamine (Gln; Q), respectively [A.

Design and characterization of novel trypsin-resistant firefly luciferases by site-directed mutagenesis.

Firefly luciferase (EC.1.13.

Critical role of Glu175 on stability and folding of bacterial luciferase: stopped-flow fluorescence study.

Bacterial luciferase is a heterodimeric enzyme, which catalyzes the light emission reaction, utilizing reduced FMN (FMNH2), a long chain aliphatic aldehyde and O(2), to produce green-blue light. This enzyme can be readily classed as slow or fast decay based on their rate of luminescence decay in a single turnover. Mutation of Glu175 in alpha subunit to Gly converted slow decay Xenorhabdus Luminescence luciferase to fast decay one.

Implication of a critical residue (Glu175) in structure and function of bacterial luciferase.

Structural properties of a bacterial luciferase mutant, evolved by random mutagenesis, have been investigated. Bacterial luciferases (LuxAB) can be readily classed as slow or fast decay luciferases based on their rates of luminescence decay in a single turnover assay. By random mutagenesis, one of the mutants generated by a single mutation on LuxA at position 175 (E175G) resulted in the "slow decay" Xenorhabdus luminescens luciferase was converted into a luciferase with a significantly more rapid decay rate [Hosseinkhani, S.