J. Raghava Rao

Recouping the wastewater: a way forward for cleaner leather processing

Abstract Leather processing employs copious amounts of water. This leads to the generation of enormous amounts of liquid effluent. The high effluent volume requires huge investments for effluent treatment plants in order to meet the required specification for the discharge of liquid effluents to various water bodies. Increasingly therefore, water use minimization in leather processing assumes greater significance due to increased treatment costs. End-of-pipe treatment methods alone do not meet the requirements and hence, in-plant control measures are gaining importance. The new era of cleaner technology has begun in leather processing. Pre-tanning and tanning operations contribute about 57% of the water consumption in leather processing and the washings about 35%. The proper adoption of integrated cleaner technologies provides a viable solution to the conservation of water in leather processing. This paper presents an integrated approach for water use minimization through recycling and optimization in leather processing. The integrated approach provides considerable reduction in the use of process water.

Cleaner chrome tanning — emerging options

Abstract More than 90% of global leather production of 18 billion sq. ft is through chrome-tanning process currently. The conventional methods employed for tanning lead to significant material loss and serious environmental concern. The current chrome management options like high exhaustion tannage, chrome recycling and recovery–reuse methods, though offer improvements, do not provide comprehensive solutions. Two new options viz. closed loop aluminium–chrome combination tanning and two-stage tanning have now been developed and field-tested. These options add economic and environmental benefits to chrome tanning through modifications in process methodologies.

An improved product-process for cleaner chrome tanning in leather processing

Abstract Severe restrictions imposed by the pollution control authorities on the disposal of chromium, total dissolved solids and chlorides in tannery effluents have forced the tanners to look for low-waste, high exhaust chrome tanning salts. An improved chrome syntan with more than 90% uptake of chrome has been developed. The new product serves both as tanning and retanning agent and can be applied directly to delimed pelts thus eliminating the conventional pickling stage in the leather processing. This modified process helps to reduce the chemical oxygen demand (COD), total dissolved solids (TDS) and chlorides in the spent tan liquor by 51, 81 and 99%, respectively. The product offers full, soft leathers having shrinkage temperature comparable to conventional chrome tanned skins. Since the developed product is highly reactive, it saves time and reduces the water requirement when compared to the conventional chrome tanning method. Thus the novel product/process developed not only has advantages in reducing pollution loads but also seems to be techno-economically viable.

Molecular mechanics and dynamics studies on the interaction of gallic acid with collagen-like peptides

Abstract Molecular modelling approaches have been used to understand the interaction of collagen-like peptides with gallic acid, which mimic vegetable tanning processes involved in protein stabilization. Several interaction sites have been identified and the binding energies of the complexes have been calculated. The calculated binding energies for various geometries are in the range 6–13 kcal/mol. It is found that some complexes exhibit hydrogen bonding, and electrostatic interaction plays a dominant role in the stabilization of the peptide by gallic acid. The π-OH type of interaction is also observed in the peptide stabilization. Molecular dynamics (MD) simulation for 600 ps revealed the possibility of hydrogen bonding between the collagen-like peptide and gallic acid.

Effect of ionic liquids on the different hierarchical order of type I collagen.

The effect of ionic liquids (ILs) on proteins has been gaining huge interest due to easy tunability of cation and anion for generating the desired effect. This study explores the effect of alkyl imidazolium chloride ILs on collagen at molecular, inter-fibrillar and skin matrix level. Circular dichroic studies reveal that at the molecular level, the secondary structure of collagen was not affected by imidazolium ILs and there was no change in thermal stability as well. However, collagen at the inter-fibrillar level behaved differently. With increase in concentration of ILs, remarkable decrease in thermal stability of rat tail tendon (RTT) collagen fibers with marginal swelling effect was seen. SEM micrographs of skin matrix treated with IL show opening up of pores. This kind of exquisite behavior of ILs at different hierarchal order of collagen indicates that ILs are endowed with potential lyotropic action, which can be judiciously employed for biomedical applications.

Molecular Dynamics Investigations on the Effect of D Amino Acid Substitution in a Triple-Helix Structure and the Stability of Collagen

Studies on the structure and stability of peptides and proteins during l-->d configurational change are certainly important for the designing of peptides with new biological activity and protein engineering. The l-->d amino acid (d AA) changes have been observed in aged proteins such as collagen. Hence, in this study, an attempt has been made to explore the effect of the replacement of l amino acid (l AA) in the model collagen-like peptides with d AA and the origin of structural stability (destability) has been traced using the molecular dynamics (MD) method employing the AMBER force field. Our results reveal that the substitution of d AA produces a large local disruption to the triple-helical structure. Formation of a kink (bulge) at the site of substitution is observed from the detailed analysis of MD trajectory. However, this local perturbation of kinked helix changes the direction of the helices and affects the relative orientation of the respective AA residues for helix-helix interaction, enough to affect the overall stability of the model collagen-like peptide. The destabilization energy per d Ala substitution is 7.87 kcal/mol, which is similar to the value for the Gly-->Ala mutation in collagen. Since the Gly-->Ala mutation is involved in genetic disorders such as osteogenesis imperfecta (OI), the l-->d configurational change may produce a similar effect on collagen.

A potential new commercial method for processing leather to reduce environmental impact

IntroductionCurrent leather processing method involves dehairing and fibre opening employing lime and sulphide, which results in higher negative impact on the environment due to its uncleanness. This method of dehairing and fibre-opening process accounts for nearly 70–80% biochemical oxygen demand and chemical oxygen demand (COD) in tannery wastewater and also the generation of H2S gas.Materials and methodsHence, an attempt has been made to reduce the environmental impact of the leather processing through a biochemical approach, employing proteolytic enzyme and sodium metasilicate for performing the above process more cleanly.Results and discussionThe developed process exhibits significant reduction in environmental parametres such as COD and total solid loads by 55% and 25%, respectively. This method completely avoids the formation of lime sludge.ConclusionThe functional properties of the leathers are also on par with conventionally processed leathers. Further, the process seems to be commercially viable.

Electrostatic Forces Mediated by Choline Dihydrogen Phosphate Stabilize Collagen

Cross-linkers aid in improving biostability of collagen via different mechanisms. Choline dihydrogen phosphate (cDHP), a biocompatible ionic liquid, has been reported as a potential cross-linker for collagen. However, its mechanism is yet unclear. This study explores the effect of cDHP on the physicochemical stability of collagen and nature of its interaction. Dielectric behavior of collagen-cDHP composites signifies that cDHP enhances intermolecular forces. This was demonstrated by an increase in cross-linked groups and high denaturation temperature of collagen-cDHP composites. XRD measurements reveal minor conformational change in helices. Molecular modeling studies illustrate that the force existing between collagen and cDHP is electrostatic in nature. Herein, it is postulated that dihydrogen phosphate anion attaches to cationic functional groups of collagen, resulting in closer vicinity of various side chains of collagen, forming physical and chemical cross-links within collagen, contributing to its structural stability. Our study suggests that dihydrogen phosphate anions can be employed for developing a new class of biocompatible cross-linkers.

Role of Preferential Ions of Ammonium Ionic Liquid in Destabilization of Collagen

Ions play a key role in the destabilization of collagen. This study explores the effect of diethyl methyl ammonium methane sulfonate (AMS), an ionic liquid (IL), on different hierarchical orderings of collagen, namely, at the molecular and fibrillar levels. The rheological behavior and secondary structural changes reveal changes in the hydrogen-bonding environment of collagen, leading to alterations in the triple helical structure of collagen. An increase in the concentration of AMS resulted in swelling of rat-tail tendon fibers, and also, decreased thermal stability signifies that ions are obliged to destabilize collagen at the fibrillar level. Molecular modeling studies confirm that anions are judiciously held responsible for structural deformities in collagen, whereas cations have a tenuous effect. Thus, the preferential role of ions present in an ammonium IL has been elucidated in this study.

Density functional theory calculations on dipeptide–gallic acid interaction

Abstract In the present investigation, an attempt has been made to study the interaction of dipeptides with gallic acid, using Becke3 parameter Lee Yang Parr (B3LYP) method employing 3-21G*, 6-31G* and 6-31+G* basis sets. The interaction energies of the dipeptide–gallic acid complexes are in the range of −5 to −18 kcal/mol depending on the mode of intermolecular complexation. Calculated molecular electrostatic potential (MESP) for the various intermolecular complexes revealed the electrostatic nature of the interaction. Qualitative estimations based on chemical hardness and chemical potential demonstrated fractional electron transfer from dipeptide to gallic acid.