Hardwood kraft pulp fibre oxidation using acidic hydrogen peroxide

2021 ◽  
Vol 0 (0) ◽  
Author(s):  
Axel Martinsson ◽  
Merima Hasani ◽  
Hans Theliander
Keyword(s):  
Hydrogen Peroxide ◽  
Reaction Times ◽  
Compositional Analysis ◽  
Accessible Surface Area ◽  
Carbonyl Groups ◽  
Cold Caustic Extraction ◽  
Cross Links ◽  
Acidic Conditions ◽  
Hardwood Pulp ◽  
Accessible Surface

Abstract Gaining insight into the oxidation of hardwood kraft fibres using hydrogen peroxide at mildly acidic conditions was the main aim of this study. The oxidized hardwood pulp had an increased number of carbonyl groups and, when formed into sheets, an enhanced durability in water was seen due to the formation of cross-links, known as hemiacetals. The carbonyl groups formed were found to be mainly ketones with the exception of the case with longer reaction times (60–90 minutes) at 85 °C, where aldehydes were detected. Through compositional analysis it was found that mainly xylan was oxidized, likely due to the higher amount of xylan close to the surface of the fibre wall. The influence of xylan on the oxidation process was investigated using cold caustic extraction (CCE) performed prior to oxidation. When the CCE pulp was oxidized, there was an increased rate of introduced carbonyl groups and degradation was more pronounced. This is likely due to the accessible surface area being increased, caused by the formation of pores when the lower molecular weight xylan was being extracted during CCE.

scholarly journals Modification of softwood kraft pulp fibres using hydrogen peroxide at acidic conditions

Cellulose ◽  
2020 ◽  
Vol 27 (12) ◽  
pp. 7191-7202
Author(s):  
Axel Martinsson ◽  
Merima Hasani ◽  
Antje Potthast ◽  
Hans Theliander
Keyword(s):  
Hydrogen Peroxide ◽  
Residence Time ◽  
Kraft Pulp ◽  
Hydroxyl Groups ◽  
Carbonyl Groups ◽  
Wet Strength ◽  
Covalent Bonds ◽  
Softwood Kraft Pulp ◽  
Pulp Fibres ◽  
Acidic Conditions

Abstract The aim of this work was to provide softwood kraft pulp fibres with new functionalities by the introduction of carbonyl groups. Carbonyl groups are known to affect properties such as wet strength through the formation of covalent bonds, i.e. hemiacetals. The method developed involves oxidation using hydrogen peroxide at mildly acidic conditions. It was found that the carbonyl group content increased with both increasing temperature and residence time when oxidized at acidic conditions. The number of carboxylic groups, however, remained approximately constant. There was virtually no increase in carbonyl groups when oxidation was performed at alkaline conditions. The maximum increase in carbonyl groups was found at a residence time of 90 min, a reaction temperature of 85 °C and a pH of 4. These conditions resulted in an increase in carbonyl groups from 30 to 122 µmol/g. When formed into a sheet, the pulp oxidized at acidic conditions proved to maintain its structural integrity at aqueous conditions. This indicates the formation of hemiacetal bonds between the introduced carbonyl groups and the hydroxyl groups on the carbohydrate chains. Thus, a possible application for the method could be fibre modification during the final bleaching stage of softwood kraft pulp, where the wet strength of the pulp could be increased.

Bleaching optimization at WestRock mill in Covington, Virginia

TAPPI Journal ◽  
2016 ◽  
Vol 15 (9) ◽  
pp. 581-586 ◽  
Author(s):  
RICARDO B. SANTOS ◽  
PETER W. HART ◽  
DOUGLAS C. PRYKE ◽  
JOHN VANDERHEIDE
Keyword(s):  
Hydrogen Peroxide ◽  
Sodium Hydroxide ◽  
Chlorine Dioxide ◽  
Capital Expenditures ◽  
Equipment Repair ◽  
Optimization Program ◽  
Hardwood Pulp ◽  
Improved Performance

The WestRock mill in Covington, VA, USA, initiated a long term diagnostic and optimization program for all three of its bleaching lines. Benchmarking studies were used to help identify optimization opportunities. Capital expenditures for mixing improvement, filtrate changes, equipment repair, other equipment changes, and species changes were outside the scope of this work. This focus of this paper is the B line, producing southern hardwood pulp in a D(EP)DD sequence at 88% GE brightness. The benchmarking study and optimization work identified the following opportunities for improved performance: nonoptimal addition of caustic and hydrogen peroxide to the (EP) stage, carryover of D0 filtrate to the (EP) stage, and carryover of (EP) filtrate to the D1 stage. As a result of actions the mill undertook to address these opportunities, D0 kappa factor decreased about 5%, sodium hydroxide consumption in the (EP) stage decreased about 35%, chlorine dioxide consumption in the D1 stage decreased about 25%, and overall bleaching cost decreased about 15%.

Application of the ESMACS Binding Free Energy Protocol to a Highly Varied Ligand Dataset: Lactate Dehydogenase A

2019 ◽  
Author(s):  
David Wright ◽  
Fouad Husseini ◽  
Shunzhou Wan ◽  
Christophe Meyer ◽  
Herman Van Vlijmen ◽  
...  
Keyword(s):  
Free Energy ◽  
Surface Area ◽  
Binding Free Energy ◽  
Normal Mode Analysis ◽  
Binding Mode ◽  
Accessible Surface Area ◽  
Solvent Accessible Surface Area ◽  
Mode Analysis ◽  
Energy Calculation ◽  
Accessible Surface

<div>Here, we evaluate the performance of our range of ensemble simulation based binding free energy calculation protocols, called ESMACS (enhanced sampling of molecular dynamics with approximation of continuum solvent) for use in fragment based drug design scenarios. ESMACS is designed to generate reproducible binding affinity predictions from the widely used molecular mechanics Poisson-Boltzmann surface area (MMPBSA) approach. We study ligands designed to target two binding pockets in the lactate dehydogenase A target protein, which vary in size, charge and binding mode. When comparing to experimental results, we obtain excellent statistical rankings across this highly diverse set of ligands. In addition, we investigate three approaches to account for entropic contributions not captured by standard MMPBSA calculations: (1) normal mode analysis, (2) weighted solvent accessible surface area (WSAS) and (3) variational entropy. </div>

scholarly journals An automated protocol for modelling peptide substrates to proteases

2020 ◽  
Vol 21 (1) ◽  
Author(s):  
Rodrigo Ochoa ◽  
Mikhail Magnitov ◽  
Roman A. Laskowski ◽  
Pilar Cossio ◽  
Janet M. Thornton
Keyword(s):  
Substrate Recognition ◽  
Accessible Surface Area ◽  
Conformational Sampling ◽  
Structural Determinants ◽  
Peptide Substrates ◽  
The Family ◽  
Protease Substrate ◽  
Peptide Complexes ◽  
Accessible Surface ◽  
Automated Protocol

Abstract Background Proteases are key drivers in many biological processes, in part due to their specificity towards their substrates. However, depending on the family and molecular function, they can also display substrate promiscuity which can also be essential. Databases compiling specificity matrices derived from experimental assays have provided valuable insights into protease substrate recognition. Despite this, there are still gaps in our knowledge of the structural determinants. Here, we compile a set of protease crystal structures with bound peptide-like ligands to create a protocol for modelling substrates bound to protease structures, and for studying observables associated to the binding recognition. Results As an application, we modelled a subset of protease–peptide complexes for which experimental cleavage data are available to compare with informational entropies obtained from protease–specificity matrices. The modelled complexes were subjected to conformational sampling using the Backrub method in Rosetta, and multiple observables from the simulations were calculated and compared per peptide position. We found that some of the calculated structural observables, such as the relative accessible surface area and the interaction energy, can help characterize a protease’s substrate recognition, giving insights for the potential prediction of novel substrates by combining additional approaches. Conclusion Overall, our approach provides a repository of protease structures with annotated data, and an open source computational protocol to reproduce the modelling and dynamic analysis of the protease–peptide complexes.

scholarly journals PAMAM dendrimer: a pH-controlled nanosponge

2017 ◽  
Vol 95 (9) ◽  
pp. 991-998 ◽  
Author(s):  
Prabal K. Maiti
Keyword(s):  
Accessible Surface Area ◽  
Pamam Dendrimer ◽  
Low Ph ◽  
Dynamics Simulation ◽  
Solvent Accessible Surface Area ◽  
Water Molecules ◽  
Accessible Volume ◽  
Accessible Surface ◽  
Solvent Accessible Surface ◽  
Ph Controlled

Using fully atomistic molecular dynamics simulation that are several hundred nanoseconds long, we demonstrate the pH-controlled sponge action of PAMAM dendrimer. We show how at varying pH levels, the PAMAM dendrimer acts as a wet sponge; at neutral or low pH levels, the dendrimer expands noticeably and the interior of the dendrimer opens up to host several hundreds to thousands of water molecules depending on the generation number. Increasing the pH (i.e., going from low pH to high pH) leads to the collapse of the dendrimer size, thereby expelling the inner water, which mimics the ‘sponge’ action. As the dendrimer size swells up at a neutral pH or low pH due to the electrostatic repulsion between the primary and tertiary amines that are protonated at this pH, there is dramatic increase in the available solvent accessible surface area (SASA), as well as solvent accessible volume (SAV).

PUTRACER: A NOVEL METHOD FOR IDENTIFICATION OF CONTINUOUS-DOMAINS IN MULTI-DOMAIN PROTEINS

2013 ◽  
Vol 11 (01) ◽  
pp. 1340012 ◽  
Author(s):  
SEYED SHAHRIAR ARAB ◽  
MOHAMMADBAGHER PARSA GHARAMALEKI ◽  
ZAIDDODINE PASHANDI ◽  
REZVAN MOBASSERI
Keyword(s):  
Protein Structures ◽  
Three Dimensional ◽  
Accessible Surface Area ◽  
Computer Assisted ◽  
Correct Assignment ◽  
Critical Boundary ◽  
Novel Method ◽  
Accessible Surface ◽  
A Chain

Computer assisted assignment of protein domains is considered as an important issue in structural bioinformatics. The exponential increase in the number of known three dimensional protein structures and the significant role of proteins in biology, medicine and pharmacology illustrate the necessity of a reliable method to automatically detect structural domains as protein units. For this aim, we have developed a program based on the accessible surface area (ASA) and the hydrogen bonds energy in protein backbone (HBE). PUTracer (Protein Unit Tracer) is built on the features of a fast top-down approach to cut a chain into its domains (contiguous domains) with minimal change in ASA as well as HBE. Performance of the program was assessed by a comprehensive benchmark dataset of 124 protein chains, which is based on agreement among experts (e.g. CATH, SCOP) and was expanded to include structures with different types of domain combinations. Equal number of domains and at least 90% agreement in critical boundary accuracy were considered as correct assignment conditions. PUTracer assigned domains correctly in 81.45% of protein chains. Although low critical boundary accuracy in 18.55% of protein chains leads to the incorrect assignments, adjusting the scales causes to improve the performance up to 89.5%. We discuss here the success or failure of adjusting the scales with provided evidences. Availability: PUTracer is available at http://bioinf.modares.ac.ir/software/PUTracer/

Sign in / Sign up

Export Citation Format

Share Document