Photo-catalysis of red wine stains using titanium dioxide sol-gel coatings on wool fabrics

This paper investigated the use of titanium dioxide sol-gel coatings to photo-catalyse red wine stains on wool fabrics. Coatings were produced by the hydrolysis and condensation of titanium butoxide (Ti(OC4H9)4) on the surface of wool fabrics after pad application. Coatings were partially converted to the anatase form of titanium dioxide by prolonged immersion in boiling water. The coating presence was confirmed using scanning electron microscopy, UVspectrophotometry and atomic force microscopy. Coated samples were measured for photo-catalytic activity by degrading red wine stains from the surface of the coated fabric. The level of photocatalysis was determined for each of the coating systems after 168 hours. Red wine stains were photo-catalysed and level of staining was reduced from the UV exposed surface of the coated wool fabric.<br />

Molecular characterization and enzymatic hydrolysis of flavanoid extracted from citrus waste

The citrus fruit processing industry generates substantial quantities of waste rich in phenolic substances, which is a valuable natural source of polyphenols (flavonoids) such as naringin and its disposal is becoming a major problem. In the US alone, the juice processing of oranges and grapefruit generates over 5 Mt of citrus waste every year. In the case of India, about 2.15 Mt of citrus peel out of 6.28 Mt of citrus fruits are produced yearly from citrus juice processing. In case of Australia, about 15-40% of citrus peel waste is generated by processing of citrus fruit (0.85 Mt). Thus Isolation of functional compounds (mostly flavanoids) and their further processing can be of interest to the food and pharmaceutical industry. This peel is rich in naringin and may be used for rhamnose production by utilizing &alpha;-L-rhamnosidase (EC 3.2.1.40), an enzyme that catalyzes the cleavage of terminal rhamnosyl groups from naringin to yield prunin and rhamnose. We recently purified recombinant &alpha;-L-rhamnosidase from E. coli cells using immobilized metal-chelate affinity chromatography (IMAC) and used it for naringin hydrolysis. The purified enzyme established hydrolysis of naringin extracted from citrus peel and thus endorses its industrial applicability for producing rhamnose. Infrared (IR) spectroscopy confirmed molecular characteristics of naringin extracted from citrus peel waste.<br />

Enzymatic synthesis of isopropyl myristate using immobilized lipase from Bacillus cereus MTCC 8372

A purified alkaline thermo-tolerant bacterial lipase from Bacillus cereus MTCC 8372 was immobilized on a <i>Poly</i> (MAc- <i>co</i> -DMA- <i>cl</i> -MBAm) hydrogel. The hydrogel showed approximately 94% binding capacity for lipase. The immobilized lipase (2.36 IU) was used to achieve esterification of myristic acid and isopropanol in <i>n</i> -heptane at 65 &deg;C under continuous shaking. The myristic acid and isopropanol when used at a concentration of 100 mM each in n -heptane resulted in formation of isopropyl myristate (66.0 &plusmn; 0.3 mM) in 15 h. The reaction temperature below or higher than 65&deg;C markedly reduced the formation of isopropyl myristate. Addition of a molecular sieve (3 &Aring; &times; 1.5 mm) to the reaction mixture drastically reduced the ester formation. The hydrogel bound lipase when repetitively used to perform esterification under optimized conditions resulted in 38.0 &plusmn; 0.2 mM isopropyl myristate after the 3 ^rd cycle of esterification.<br />

Microbial lipases : at the interface of aqueous and non-aqueous media: a review

In recent times, biotechnological applications of <b>microbial lipases</b> in synthesis of many organic molecules have rapidly increased in <b>non-aqueous media</b>. <b>Microbial lipases</b> are the working horses' in biocatalysis and have been extensively studied when their exceptionally high stability in <b>non-aqueous media</b> has been discovered. Stability of lipases in organic solvents makes them commercially feasibile in the enzymatic esterification reactions. Their stability is affected by temperature, reaction medium, water concentration and by the biocatalyst's preparation. An optimization process for ester synthesis from pilot scale to industrial scale in the reaction medium is discussed. The water released during the esterification process can be controlled over a wide range and has a profound effect on the activity of the <b>lipases</b>. Approaches to <b>lipase</b> catalysis like protein engineering, directed evolution and metagenome approach were studied. This review reports the recent development in the field of <b>non-aqueous microbial lipase</b> catalysis and factors controlling the esterification/transesterification processes in organic <b>media</b>.

Molecular aspects of boundary lubrication by human lubricin : effect of disulfide bonds and enzymatic digestion

Lubricin (LUB) is a glycoprotein of the synovial cavity of human articular joints, where it serves as an antiadhesive, boundary lubricant, and regulating factor for the cartilage surface. It has been proposed that these properties are related to the presence of a long, extended, heavily glycosylated and highly hydrated mucinous domain in the central part of the LUB molecule. In this work, we show that LUB has a contour length of 220 &plusmn; 30 nm and a persistence length of &le;10 nm. LUB molecules aggregate in oligomers where the protein extremities are linked by disulfide bonds. We have studied the effect of proteolytic digestion by chymotrypsin and removal of the disulfide bonds, both of which mainly affect the N&minus; and C&minus; terminals of the protein, on the adsorption, normal forces, friction (lubrication) forces, and wear of LUB layers adsorbed on smooth, negatively charged mica surfaces, where the protein naturally forms lubricating polymer brush-like layers. After in situ digestion, the surface coverage was drastically reduced, the normal forces were altered, and both the coefficient of friction and the wear were dramatically increased (the COF increased to &mu; = 1.1&minus;1.9), indicating that the mucinous domain was removed from the surface. Removal of disulfide bonds did not change the surface coverage or the overall features of the normal forces; however, we find an increase in the friction coefficient from &mu; = 0.02&minus;0.04 to &mu; = 0.13&minus;1.17 in the pressure regime below 6 atm, which we attribute to a higher affinity of the protein terminals for the surface. The necessary condition for LUB to be a good lubricant is that the protein be adsorbed to the surface via its terminals, leaving the central mucin domain free to form a low-friction, surface-protecting layer. Our results suggest that this &ldquo;end-anchoring&rdquo; has to be strong enough to impart the layer a sufficient resistance to shear, but without excessively restricting the conformational freedom of the adsorbed proteins.<br />