Carla Roberta Matte

Development of active biofilms of quinoa (Chenopodium quinoa W.) starch containing gold nanoparticles and evaluation of antimicrobial activity.

Active biofilms of quinoa (Chenopodium quinoa, W.) starch were prepared by incorporating gold nanoparticles stabilised by an ionic silsesquioxane that contains the 1,4-diazoniabicyclo[2.2.2]octane chloride group. The biofilms were characterised and their antimicrobial activity was evaluated against Escherichiacoli and Staphylococcusaureus. The presence of gold nanoparticles produces an improvement in the mechanical, optical and morphological properties, maintaining the thermal and barrier properties unchanged when compared to the standard biofilm. The active biofilms exhibited strong antibacterial activity against food-borne pathogens with inhibition percentages of 99% against E. coli and 98% against S. aureus. These quinoa starch biofilms containing gold nanoparticles are very promising to be used as active food packaging for the maintenance of food safety and extension of the shelf life of packaged foods.

Silver Nanoparticle Thin Films Deposited on Glass Surface Using an Ionic Silsesquioxane as Stabilizer and as Crosslinking Agent

Thin films containing silver nanoparticles homogeneously dispersed, with narrow size distribution below 10 nm, were synthesized on flat glass surface, by using an ionic silsesquioxane as stabilizer and crosslinking agent. The films can be prepared without previous functionalization of substrate surfaces and without addition of other components. The films were heat treated up to 200 oC and characterized by ultraviolet-visible, transmission electron microscopy, atomic force microscopy, thermogravimetric analysis and ellipsometry. The films were thermally stable when heated up to 200 oC, presenting the same thickness, and maintaining both optical and morphological properties of silver nanoparticles. The antibacterial activity of the films, containing the silver nanoparticles, was evaluated against Staphylococcus aureus by using the film applicator coating method, showing an excellent performance even after the third cycle of sterilization.

Physical-Chemical Properties of the Support Immobead 150 Before and After the Immobilization Process of Lipase

We carried out the physico-chemical characterization of Immobead 150, a hydrophobic support for the immobilization of lipases. Thermomyces lanuginosus lipase (TLL) was immobilized on Immobead 150 by multipoint covalent attachment (ImmTLL) and the morphological, textural, structural, thermal, and physico-chemical properties of the support, before and after enzyme immobilization, were investigated. Immobead 150 presents approximately 1,000 μmol of epoxy groups per gram of support, a high hydrophobicity, and good thermal stability. The spherical particles of Immobead 150 present average diameters of 155 μm, specific surface areas of 137 m g and pore volumes of 0.37 cm g, showing pores in the region of the micro and meso sizes. The immobilization process of TLL (150 mg g) caused a decrease of the specific area and pore volumes, to 63 m g and 0.25 cm g, respectively, as a result of coating of the support surface by the enzyme molecule. However, the immobilization process did not affect the morphology of the support. The obtained biocatalyst was effective for the syntheses of fatty acid ethyl esters (biodiesel), and of aroma esters, showing yields of 68 and 70%, respectively, similar to commercial preparations used as controls.

Effects of immobilization, pH and reaction time in the modulation of α-, β- or γ-cyclodextrins production by cyclodextrin glycosyltransferase: Batch and continuous process

This study reports the immobilization of a β-CGTase on glutaraldehyde pre-activated silica and its use to production of cyclodextrins in batch and continuous reactions. We were able to modulate the cyclodextrin production (α-, β- and γ-CD) by immobilization and changing the reaction conditions. In batch reactions, the immobilized enzyme reached to maximum productions of 4.9mgmL-1 of α-CD, 3.6mgmL-1 of β-CD and 3.5mgmL-1 of γ-CD at different conditions of temperature, pH and reaction time. In continuous reactor, varying the residence time and pH it was possible to produce at pH 4.0 and 141min of residence time preferentially γ-CD (0.75 and 3.36mgmL-1 of α- and γ-CD, respectively), or at pH 8.0 and 4.81min α- and β-CDs (3.44 and 3.51mgmL-1).

Enzymatic synthesis of ethyl esters from waste oil using mixtures of lipases in a plug-flow packed-bed continuous reactor

This work describes the continuous synthesis of ethyl esters via enzymatic catalysis on a packed‐bed continuous reactor, using mixtures of immobilized lipases (combi‐lipases) of Candida antarctica (CALB), Thermomyces lanuginosus (TLL), and Rhizomucor miehei (RML). The influence of the addition of glass beads to the reactor bed, evaluation of the use of different solvents, and flow rate on reaction conditions was studied. All experiments were conducted using the best combination of lipases according to the fatty acid composition of the waste oil (combi‐lipase composition: 40% of TLL, 35% of CALB, and 25% of RML) and soybean oil (combi‐lipase composition: 22.5% of TLL, 50% of CALB, and 27.5% of RML). The best general reaction conditions were found to be using tert‐butanol as solvent, and the flow rate of 0.08 mL min−1. The combi‐lipase reactors operating at steady state for over 30 days (720 h), kept conversion yields of ∼50%, with average productivity of 1.94 gethyl esters gsubstrate−1 h−1, regardless of the type of oil in use.