Mapping of patents on bioemulsifier and biosurfactant: A review

91-115Biosurfactant (BS) and bioemulsifier (BE) molecules have both hydrophilic and hydrophobic moieties that partition preferentially at the interface between fluid phases with different degrees of polarity and hydrogen bonding such as oil/water or air/water interfaces. Such characteristics enable excellent detergency, emulsifying, foaming and dispersing traits. Their low toxicity and environmental friendly nature and range of potential industrial applications in the oil, bioremediation, health care and food processing industries make them a highly sought after group of chemical compounds. Several patents have been issued on BE and BS produced by Acinetobacter spp., Bacillus spp., Pseudomonas spp. and sophorolipid producing yeasts like Candida spp. This review presents the result of a scan and mapping effort for 255 patents granted on these compounds worldwide highlighting the types of microorganisms, molecules produced, production process and their potential industrial applications

Insight into the effect of inhibitor resistant S130G mutant on physico-chemical properties of SHV type beta-lactamase: a molecular dynamics study.

Bacterial resistance is a serious threat to human health. The production of β-lactamase, which inactivates β-lactams is most common cause of resistance to the β-lactam antibiotics. The Class A enzymes are most frequently encountered among the four β-lactamases in the clinic isolates. Mutations in class A β-lactamases play a crucial role in substrate and inhibitor specificity. SHV and TEM type are known to be most common class A β-lactamases. In the present study, we have analyzed the effect of inhibitor resistant S130G point mutation of SHV type Class-A β-lactamase using molecular dynamics and other in silico approaches. Our study involved the use of different in silico methods to investigate the affect of S130G point mutation on the major physico-chemical properties of SHV type class A β-lactamase. We have used molecular dynamics approach to compare the dynamic behaviour of native and S130G mutant form of SHV β-lactamase by analyzing different properties like root mean square deviation (RMSD), H-bond, Radius of gyration (Rg) and RMS fluctuation of mutation. The results clearly suggest notable loss in the stability of S130G mutant that may further lead to decrease in substrate specificity of SHV. Molecular docking further indicates that S130G mutation decreases the binding affinity of all the three inhibitors in clinical practice

Solvent accessible surface area of native and S130G mutant of SHV β-lactamases.

<p>Native is shown in black; S130G mutant form of SHV type β-lactamase is shown in red.</p

RMSF of the backbone atoms of native and mutant SHV β-lactamase vs. time at 300 K.

<p>Native is shown in black; S130G point mutant form of SHV β-lactamases is shown in red.</p

Physico-chemical features of native and S130G mutant SHV studied.

<p>Physico-chemical features of native and S130G mutant SHV studied.</p

Binding efficacy of clavulanic against SHV S130G mutant at different time intervals and the active site residues involved in the binding.

<p>Binding efficacy of clavulanic against SHV S130G mutant at different time intervals and the active site residues involved in the binding.</p

Potential energy (kJ/mol) of native and mutant type SHV β-lactamases.

<p>Native is shown in black; S130G mutant form of SHV β-lactamases is shown in red.</p

Time evolution of the secondary structure elements of S130G mutant of SHV at 300 K.

<p>The color scale at the bottom represents the DSSP classification of each secondary structure element.</p

Binding mode of clavulanic acid with active site residues of SHV wt at different time intervals (a) binding of ca at 0 ns (b) binding of ca at 2 ns (c) binding of ca at 5 ns (d) binding of ca at 10 ns.

<p>Binding mode of clavulanic acid with active site residues of SHV wt at different time intervals (a) binding of ca at 0 ns (b) binding of ca at 2 ns (c) binding of ca at 5 ns (d) binding of ca at 10 ns.</p