Immobilization of lipase on woolen fabrics: Enhanced effectiveness in stain removal

Abstract

The aim of this research was to examine the effectiveness of an enzyme in enhancing the cleaning effectiveness of woolen fabric without addition of any detergent. As a model enzyme, lipase from Pseudomonas fluoresces was immobilized onto a woolen cloth using a unique protocol that involved: chlorination of the wool, adsorbing a polyethyleneimine (PEI) spacer, adsorbing, and cross-linking with glutaraldehyde (GA) followed by adsorption of the lipase. It was determined that for this protocol, the immobilized activity was dependent on the GA solution pH and not on its concentration. The cloth exhibited excellent oily stain removal ability: after being stained with olive oil and stored for 1 day in air at room temperature, the oily stain could be easily removed by 0.05 M pH 8.5 Tris buffer without any detergent addition. This enhanced cleaning was stable also over a period of one month. The activity of the cloth (based on activity assay) dropped considerably over just 15 days storage in air. This therefore likely indicates that the enhanced cleaning seen over an extended storage period may not require as high an enzyme activity. The activity of the immobilized lipase was also very stable when stored under near ideal conditions: when the immobilized cloth was stored in 0.05 M Tris buffer (pH 8.5) for more than 80 days in a refrigerator, more than 80% of the lipase activity remained. Overall, results indicate that this immobilization protocol is a promising step towards producing a woolen fabric with enhanced cleaning properties.

Luffa cylindrica sponges as a thermally and chemically stable support for Aspergillus niger lipase

“…This technique increases the operational and storage stability of enzymes and the thermal and chemical stability of the immobilized biocatalysts. Most importantly, however, the binding of enzymes to a solid support generates heterogeneous biocatalysts which can be more easily separated from the reaction system . Compounds of both organic and inorganic origin may play the role of support in the enzyme immobilization process, and their selection is usually determined by the application of the biocatalyst systems …”

Recent advances on sources and industrial applications of lipases

“…Also, lipase from P. fluoresces when immobilized onto a woolen cloth has exhibited excellent oil stain removal ability. The immobilization procedure has a unique protocol involving chlorination of the wool, adsorbing a polyethyleneimine spacer, adsorbing, and cross‐linking with glutaraldehyde followed by adsorption of the lipase …”

“…Other factors relevant to enhance the commercial potential of enzymes include proper selection of supports during application, and suitable downstream processing and purification strategies during production of lipases. A range of support materials including both organic and inorganic compounds can be used for lipase immobilization in which fabrics have the advantages, such as availability in bulk, low‐pressure drop, and mature processing technologies . Among the numerous materials reported on enzyme immobilization, nanomaterials are gaining increasing attention due to their enhanced surface area, reduced mass transfer resistance, and effective enzyme loading.…”

APPLICABILITY OF WOOL COVALENT BONDED Bacillus circulans 25 CELLS FOR MILK-CLOTTING ENZYME PRODUCTION BY BATCH, REPEATED BATCH AND CONTINUOUS PROCESS

“…The surface of untreated wool is quite hydrophobic, cell immobilization onto this surface can then be achieved by using glutaraldehyde (GA) as a cross-linking agent due to its fast reaction and low toxicity. The most widely accepted theory on the GA cross-linking mechanism is that the aldehyde groups in GA react with the lysine residues in the protein through a Schiff base reaction (An et al, 2014). Repeated batch fermentation is considered useful technology for enhancing the productivity due to the reduction in fermentation time and removal of the inoculum preparation step (Reddy et al, 2016).…”