Evaluation of Strategies to Produce Highly Porous Cross-Linked Aggregates of Porcine Pancreas Lipase with Magnetic Properties.

The preparation of highly porous magnetic crosslinked aggregates (pm-CLEA) of porcine pancreas lipase (PPL) is reported. Some strategies to improve the volumetric activity of the immobilized biocatalyst were evaluated, such as treatment of PPL with enzyme surface-modifying agents (polyethyleneimine or dodecyl aldehyde), co-aggregation with protein co-feeders (bovine serum albumin and/or soy protein), use of silica magnetic nanoparticles functionalized with amino groups (SMNPs) as separation aid, and starch as pore-making agent. The combination of enzyme surface modification with dodecyl aldehyde, co-aggregation with SMNPs and soy protein, in the presence of 0.

Eucalyptus xylan: An in-house-produced substrate for xylanase evaluation to substitute birchwood xylan.

Over the past decades, most studies with xylanases have used Birchwood xylan as the standard substrate for activity assays. However, recently, Birchwood xylan production was discontinued by major suppliers, creating an important demand for a substitute. Ongoing and future studies require a substrate with characteristics equivalent to the discontinued xylan, in order to enable the comparison of results.

Performance of Different Immobilized Lipases in the Syntheses of Short- and Long-Chain Carboxylic Acid Esters by Esterification Reactions in Organic Media.

Short-chain alkyl esters and sugar esters are widely used in the food, pharmaceutical and cosmetic industries due to their flavor and emulsifying characteristics, respectively. Both compounds can be synthesized via biocatalysis using lipases. This work aims to compare the performance of commercial lipases covalently attached to dry acrylic beads functionalized with oxirane groups (lipases from type B-IMMCALB-T2-350, -IMMAPF-T2-150, and -IMMTLL-T2-150) and a home-made biocatalyst (lipase from adsorbed onto silica coated with octyl groups, named PFL-octyl-silica) in the syntheses of short- and long-chain carboxylic acid esters.

Enhanced saccharification of sugarcane bagasse using soluble cellulase supplemented with immobilized β-glucosidase.

The β-glucosidase (BG) enzyme plays a vital role in the hydrolysis of lignocellulosic biomass. Supplementation of the hydrolysis reaction medium with BG can reduce inhibitory effects, leading to greater conversion. In addition, the inclusion of immobilized BG can be a useful way of increasing enzyme stability and recyclability.

Enhanced production of recombinant thermo-stable lipase in Escherichia coli at high induction temperature.

Thermostable microbial lipases are potential candidates for industrial applications such as specialty organic syntheses as well as hydrolysis of fats and oils. In this work, basic biochemical engineering tools were applied to enhance the production of BTL2 lipase cloned in Escherichia coli BL321 under control of the strong temperature-inducible λP(L) promoter. Initially, surface response analysis was used to assess the influence of growth and induction temperatures on enzyme production, in flask experiments.

Evaluation of immobilized lipases on poly-hydroxybutyrate beads to catalyze biodiesel synthesis.

Five microbial lipase preparations from several sources were immobilized by hydrophobic adsorption on small or large poly-hydroxybutyrate (PHB) beads and the effect of the support particle size on the biocatalyst activity was assessed in the hydrolysis of olive oil, esterification of butyric acid with butanol and transesterification of babassu oil (Orbignya sp.) with ethanol. The catalytic activity of the immobilized lipases in both olive oil hydrolysis and biodiesel synthesis was influenced by the particle size of PHB and lipase source.

Multipoint covalent immobilization of lipase on chitosan hybrid hydrogels: influence of the polyelectrolyte complex type and chemical modification on the catalytic properties of the biocatalysts.

This work aimed at the production of stabilized derivatives of Thermomyces lanuginosus lipase (TLL) by multipoint covalent immobilization of the enzyme on chitosan-based matrices. The resulting biocatalysts were tested for synthesis of biodiesel by ethanolysis of palm oil. Different hydrogels were prepared: chitosan alone and in polyelectrolyte complexes (PEC) with κ-carrageenan, gelatin, alginate, and polyvinyl alcohol (PVA).

Adsorption of components of enzymatic synthesis of ampicillin on different hydrophobic resins.

This work compared the performance of three hydrophobic resins for the adsorption of ampicillin (AMP), D-phenylglycine (PG), D-phenylglycine methyl ester (PGME), and 6- aminopenicillanic acid (6-APA). The influence of pH on adsorption efficiencies was assessed in the range of 4.5-8.