Vegetable wastes as a bio-additive for low-salt preservation of raw goat skin: An attempt to reduce salinity in leather manufacture.

Preservation or curing of hides/skins is performed as the primary step of leather processing to conserve them from putrefaction. Normally preservation is carried out using common salt (NaCl), which is discharged in the soak liquor contributing to ~ 70%, of total dissolved solids (TDS) load of entire leather manufacturing. In an attempt to reduce the TDS and chlorides, phyto-based preservation using garlic peel (Allium sativum) and white onion peel (Allium cepa) was carried out. Different concentrations of salt in combination with garlic peel and white onion peel were applied on freshly flayed goat skins based on its green weight and compared to control (40% salt). Sensory evaluation of the preserved skin was done by assessing different parameters like hair slip, putrefaction and odour. Estimation of hydroxyproline (HP) release, moisture content and microbial load were carried out at regular intervals. Skins that remained in good condition for 14 days were further processed into leather and properties were examined which were found comparable to the conventionally cured skins. Hence, this cleaner curing technique helps in reducing the TDS and chlorides in the effluent, thus controlling the pollution caused by tanneries through sustainable leather processing.

Stabilization of collagen through bioconversion: An insight in protein-protein interaction.

Collagen is a natural protein, which is used as a vital biomaterial in tissue engineering. The major concern about native collagen is lack of its thermal stability and weak resistance to proteolytic degradation. In this scenario, the crosslinking compounds used for stabilization of collagen are mostly of chemical nature and exhibit toxicity. The enzyme mediated crosslinking of collagen provides a novel alternative, nontoxic method for stabilization. In this study, aldehyde forming enzyme (AFE) is used in the bioconversion of hydroxylmethyl groups of collagen to formyl groups that results in the formation of peptidyl aldehyde. The resulted peptidyl aldehyde interacts with bipolar ions of basic amino acid residues of collagen. Further interaction leads to the formation of conjugated double bonds (aldol condensation involving the aldehyde group of peptidyl aldehyde) within the collagen. The enzyme modified collagen matrices have shown an increase in the denaturation temperature, when compared with native collagen. Enzyme modified collagen membranes exhibit resistance toward collagenolytic activity. Moreover, they exhibited a nontoxic nature. The catalytic activity of AFE on collagen as a substrate establishes an efficient modification, which enhances the structural stability of collagen. This finds new avenues in the context of protein-protein stabilization and discovers paramount application in tissue engineering.

Preparation and antimicrobial activity of scleraldehyde from Schizophyllum commune.

The present study investigates the antimicrobial activity of oxidized schizophyllan (scleraldehyde) against Gram-positive and Gram-negative bacteria by diffusion and tube dilution analysis. Schizophyllan is a natural polysaccharide produced by fungi of the genus Schizophyllum. Periodate oxidation specifically cleaves the vicinal glycols in scleraldehyde to form their dialdehyde derivatives. The antibacterial activity exhibited by scleraldehyde was defined using various tests such as the disc diffusion assay, minimum inhibitory concentration (MIC) and minimum bactericidal concentration (MBC). MIC and MBC values were found to be in the range of 3.0-8.0 mg/mL. Hence, the present studies establish that the scleraldehyde possesses effective antibacterial properties and can be used as a biopreservative for preservation of raw hides and skins.

Kinetics of leather dyeing pretreated with enzymes: role of acid protease.

In the present investigation, kinetics of dyeing involving pretreatment with acid protease has been presented. Application of acid protease in dyeing process resulted in increased absorption and diffusion of dye into the leather matrix. Enzyme treatment at 1% concentration, 60 min duration and 50 degrees C resulted in maximum of 98% dye exhaustion and increased absorption rate constants. The final exhaustion (C(infinity)) for the best fit of CI Acid Black 194 dye has been 98.5% with K and r2 values from the modified Cegarra-Puente isotherm as 0.1033 and 0.0631. CI Acid Black 194 being a 2:1 metal complex acid dye exhibited higher absorption rate than the acid dye CI Acid Black 210. A reduction in 50% activation energy calculated from Arrhenius equation has been observed in enzyme assisted dyeing process of both the dyes that substantiates enhanced dye absorption. The absorption rate constant calculated with modified Cegarra-Puente equation confirm higher rate constants and faster kinetics for enzyme assisted dyeing process. Enzyme treated leather exhibited richness of color and shade when compared with control. The present study substantiates the essential role of enzyme pretreatment as an eco-friendly leather dyeing process.