Nature endowed snakes with a lethal secretion known as venom, which has been fine-tuned over millions of years of evolution. Snakes utilize venom to subdue their prey and to survive in their natural habitat. Venom is known to be a very poisonous mixture, consisting of a variety of molecules, such as carbohydrates, nucleosides, amino acids, lipids, proteins and peptides. Proteins and peptides are the major constituents of the dry weight of snake venoms and are of main interest for scientific investigations as well as for various pharmacological applications. Snake venoms contain enzymatic and non-enzymatic proteins and peptides, which are grouped into different families based on their structure and function. Members of a single family display significant similarities in their primary, secondary and tertiary structures, but in many cases have distinct pharmacological functions and different bioactivities. The functional specificity of peptides belonging to the same family can be attributed to subtle variations in their amino acid sequences. Currently, complementary tools and techniques are utilized to isolate and characterize the peptides, and study their potential applications as molecular probes, and possible templates for drug discovery and design investigations.

BackgroundSnake venom is a source of many pharmacologically important molecules. Agkistrodon bilineatus commonly known as Cantil, is spread over Central America particularly in Mexico and Costa Rica. From the venom of Agkistrodon bilineatus we have isolated and characterised six hypotensive peptides, and two bradykinin inhibitor peptides. The IC-50 value of four synthesized peptides was studied, towards angiotensin converting enzyme, in order to study the structure-function relationship of these peptides.ResultsThe purification of the peptides was carried out by size exclusion chromatography, followed by reverse phase chromatography. Sequences of all peptides were determined applying MALDI-TOF/TOF mass spectrometry. These hypotensive peptides bear homology to bradykinin potentiating peptides and venom vasodilator peptide. The peptide with m/z 1355.53 (M + H)+1, and the corresponding sequence ZQWAQGRAPHPP, we identified for the first time. A precursor protein containing a fragment of this peptide was reported at genome level, (Uniprot ID P68515), in Bothrops insularis venom gland. These proline rich hypotensive peptides or bradykinin potentiating peptides are usually present in the venom of Crotalinae, and exhibit specificity in binding to the C domain of somatic angiotensin converting enzyme. Four of these hypotensive peptides, were selected and synthesized to obtain the required quantity to study their IC50 values in complex with the angiotensin converting enzyme. The peptide with the sequence ZLWPRPQIPP displayed the lowest IC50 value of 0.64 μM. The IC50 value of the peptide ZQWAQGRAPHPP was 3.63 μM.ConclusionThe canonical snake venom BPPs classically display the IPP motif at the C-terminus. Our data suggest that the replacement of the highly conserved hydrophobic isoleucine by histidine does not affect the inhibitory activity, indicating that isoleucine is not mandatory to inhibit the angiotensin converting enzyme. The evaluation of IC 50 values show that the peptide with basic pI value exhibits a lower IC 50 value.

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Aim This work was conducted to produce, purify and characterize biosurfactants from Aspergillus flavus AF612 isolated from citrus fruit. Methods and results Biosurfactant named ‘Uzmaq’ was isolated from A. flavus AF612. The chemical characterization of the biosurfactant was conducted. Biosurfactant Uzmaq produced by A. flavus, was composed of methoxy phenyl oxime glycosides. Two molecular forms of the biosurfactant, Uzmaq‐A and Uzmaq‐B were isolated. Biological properties (antifungal activity) were evaluated. The fractions of the biosurfactant were isolated and their surface properties were analysed. Uzmaq‐A and Uzmaq‐B had critical micelle concentration (CMC) around 170 and 80 mg l−1, and lowered surface tension of water up to 20 and 25 m Nm−1 respectively. The biosurfactants were stable at pH 3–12 and temperature up to 80°C. Growth and biosurfactant production kinetics were also analysed. Conclusion Novel biosurfactant Uzmaq was produced from A. flavus, which was composed of methoxy phenyl oxime glycosides. The surface activity of Uzmaq was better than the maximum values of synthetic chemical surfactants. The biosurfactant showed antifungal activity and self‐assembling properties. Significance and Impact of the Study Aspergillus flavus AF612 can be used for commercial production of Uzmaq that may be employed for controlled drug release applications and bioremediation.

The productivity of major field crops is highly compromised due to weed infestation. Inefficient weed management practices and undue and excessive use of chemical herbicides have drastically contaminated the environment and human health, in addition to resistance development in weed species. Therefore, utilization of allelopathic plants to explore phytochemicals as potent organic alternatives to such chemical herbicides has become indispensable. The current study evaluates the comparative bio-herbicidal potential of methanolic extracts of castor (Ricinus communis), artemisia (Artemisia santolinifolia), wheat (Triticum aestivum), and sorghum (Sorghum bicolor) to suppress growth of major weeds, i.e., wild mustard (Sinapis arvensis), Italian ryegrass (Lolium multiflorum), and carrot grass (Parthenium hysterophorus). The results demonstrated a concentration-dependent effect on weeds’ growth. Overall, in vitro seed germination was reduced from 60 to 100% in response to 5% (w/v) extract concentration. Significant reduction in radicle length, hypocotyl length, and fresh biomass of the weeds was also observed. A strong inhibitory effect was seen in in vivo pot experiments, revealing that application of 10–20% methanolic extracts induced permanent wilting and substantial reduction in the chlorophyll content of weeds along with 20–80% increase in oxidative stress. Artemisia showed the most significant allelopathic effect, on account of highest phenolic and flavonoid contents, followed by castor, wheat, and sorghum, against S. arvensis, L. multiflorum, and P. hysterophorus, respectively. Phytochemical analysis, through high-performance liquid chromatography (HPLC), also exhibited a correlation between extract’s phytotoxicity and their antioxidant potential due to their major constituents (rutin, quercetin, catechin, gallic acid, vanillic acid, syringic acid, ferulic acid, p-hydroxy benzoic acid, p-coumaric acid, and sinapic acid), among the total of 13 identified in methanolic fractions. Comprehensive profiling of allelochemicals with liquid chromatography–mass spectrometry (LC-MS) determined 120, 113, 90, and 50 derivates of phenolic acids, flavonoids, and alkaloids, reported for the first time through this study, demonstrating significant allelopathic potential of the targeted plant fractions, which can be explored further to develop a sustainable bio-herbicidal formulation.

Xylanase was produced by growing Chaetomium thermophile NIBGE in a submerged liquid culture using wheat straw and urea as carbon and nitrogen sources respectively. The xylanase was purified to electrophoretic homogeneity after ammonium sulphate precipitation, anion exchange chromatography by FPLC and gel filtration. The molecular mass of this xylanase BII was 50 kDa. The pH and temperature optima were 6.5 and 70°C respectively. The xylanase BII showed reasonable stability at high pH and 65°C temperature. Some metal ions and EDTA caused little inhibition at low concentrations but complete inhibition was observed at concentrations higher than 2 mM. The K m and V max values with oat spelt xylan as the substrate were found to be 12.5 mg/ml and 83.3 IU/mg protein, respectively. Liberation of reducing sugars from commercial paper pulp samples suggest the feasibility of a biopulping process using this xylanase.

Kunitz-type trypsin inhibitor was first characterized from Enterolobium contortisiliquum (EcTI) (Batista et al., 1996). Plant-based KTIs have shown inhibition of trypsin or chymotrypsin along other serine proteinases such as subtilisin and elastase (Revina et al., 2004; Sumikawa et al., 2006). Some individual KTIs typically have shown more specific activities in comparison to those that inhibit cysteine or aspartic proteinases (Heibges et al., 2003). Kunitz-type trypsin inhibitors are also found in

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