Simultaneous hydrolysis of cheese whey and lactulose production catalyzed by ß-galactosidase from Kluyveromyces lactis NRRL Y1564.

ß-Galactosidase was produced by the yeast Kluyveromyces lactis NRRL Y1564 in cheese whey supplemented with yeast extract under the optimal temperature of 30 °C, delivering an enzymatic activity of 4418.37 U/gcell after 12 h of process. In order to develop more stable biocatalysts, the enzyme produced by fermentation was immobilized on 2.0% w/v chitosan activated with glutaraldehyde, epichlorohydrin or glycidol, producing a highly active and stable biocatalyst capable of hydrolyzing lactose and producing lactulose simultaneously. The biocatalyst obtained by immobilization in chitosan-glutaraldehyde showed high storage stabilities (100% of its activity when stored at 4 °C 105 days). Regarding the milk lactose hydrolysis by both the soluble and the immobilized enzyme, the conversions obtained were 38.0% and 42.8%, respectively. In this study, by using a biocatalyst deriving from enzyme immobilization to chitosan support, a lactulose production of 17.32 g/L was also possible.

Hydrogels based on lignin extracted from cashew apple bagasse and its application in antimicrobial wound dressings.

Hydrogels are versatile materials with a three-dimensional network structure that can retain water and release bioactive compounds. They have found applications in various fields, including agriculture, biomaterial synthesis, and pharmaceuticals. Incorporating natural antimicrobial compounds into hydrogels is a promising approach to developing non-toxic biomedical materials, particularly for wound healing dressings. It was evaluated the extraction and use of cashew apple bagasse lignin (CAB-Lig) due to its healing, anti-inflammatory, and antimicrobial properties for producing a hydrogel-based bandage. The extraction process involved acid and alkali treatments followed by precipitation. The antimicrobial potential of CAB-Lig was evaluated at different concentrations for formulating hydrogels. Hydrogels containing 0.1 % and 3 % lignin showed high swelling and liquid retention abilities. The 3 % lignin hydrogel exhibited effectiveness against Escherichia coli and Staphylococcus aureus. Incorporating CAB-Lig into the hydrogel structure improved its mechanical properties, making it more suitable for application as a bandage. Moreover, the extracted lignin showed low toxicity, indicating its safe use. A bandage was formulated by combining the CAB-Lig-based hydrogel with polyester, which possessed antimicrobial properties and demonstrated biocompatibility (L929 and HaCat cells). The results confirmed the potential of CAB-Lig for synthesizing hydrogels and dressings with antimicrobial properties, offering a sustainable solution for utilizing lignocellulosic biomass.

Bioemulsifier production by Acinetobacter venetianus AMO1502: Potential for bioremediation and environmentally friendly applications.

At the best conditions of the bioprocess (30 °C, pH 7.0, 3.0 g/L NaCl) were obtained 0.66 g/L cell concentration, 3.3 g/L of bioemulsifier, which showed high emulsifying activity (53 % ± 2), reducing the surface tension of the water in 47.2 % (38 mN/m). The polymeric structure of the purified bioemulsifier comprised a carbohydrate backbone composed of hexose-based amino sugars with a monomeric mass of 1099 Da, structurally similar to emulsan. A. venetianus bioemulsifier is non-phytotoxic (GI% > 80 %) against Ocimum basilicum and Brassica oleracea and non-cytotoxic (LC50 5794 mg/L) against Artemia salina, being safe local organisms in comparison to other less eco-friendly synthetic emulsifiers. This bioemulsifier effectively dispersed spilled oil in vitro (C22-C33), reducing oil mass by 12 % (w/w) and dispersing oil in a displacement area of 75 cm2 (23.8 % of the spilled area). Thus, the isolated A. venetianus AMO1502 produced a bioemulsifier potentially applicable for environmentally friendly oil spill remediation.

Polylactic acid production from biotechnological routes: A review.

Polylactic acid (PLA) has been highlighted as an important polymer due to its high potential for applicability in various areas, such as in the chemical, medical, pharmaceutical or biotechnology field. Very recently, studies have reported its use as a basic component for the production of personal protective equipment (PPE) required for the prevention of Sars-Cov-2 contamination, responsible for the cause of coronavirus disease, which is currently a major worldwide sanitary and social problem. PLA is considered a non-toxic, biodegradable and compostable plastic with interesting characteristics from the industrial point of view, and it emerges as a promising product under the concept of "green plastic", since most of the polymers produced currently are petroleum-based, a non-renewable raw material. Biotechnology routes have been mentioned as potential methodologies for the production of this polymer, especially by enzymatic routes, in particular by use of lipases enzymes. The availability of pure lactic acid isomers is a fundamental aspect of the manufacture of PLA with more interesting mechanical and thermal properties. Due to the technological importance that PLA-based polymers are acquiring, as well as their characteristics and applicability in several fields, especially medical, pharmaceutical and biotechnology, this review article sought to gather very recent information regarding the development of research in this area. The main highlight of this study is that it was carried out from a biotechnological point of view, aiming at a totally green bioplastic production, since the obtaining of lactic acid, which will be used as raw material for the PLA synthesis, until the degradation of the polymer obtained by biological routes.

ß-Galactosidase from Kluyveromyces lactis: Characterization, production, immobilization and applications - A review.

A review on the enzyme ß-galactosidase from Kluyveromyces lactis is presented, from the perspective of its structure and mechanisms of action, the main catalyzed reactions, the key factors influencing its activity, and selectivity, as well as the main techniques used for improving the biocatalyst functionality. Particular attention was given to the discussion of hydrolysis, transglycosylation, and galactosylation reactions, which are commonly mediated by this enzyme. In addition, the products generated from these processes were highlighted. Finally, biocatalyst improvement techniques are also discussed, such as enzyme immobilization and protein engineering. On these topics, the most recent immobilization strategies are presented, emphasizing processes that not only allow the recovery of the biocatalyst but also deliver enzymes that show better resistance to high temperatures, chemicals, and inhibitors. In addition, genetic engineering techniques to improve the catalytic properties of the ß-galactosidases were reported. This review gathers information to allow the development of biocatalysts based on the ß-galactosidase enzyme from K. lactis, aiming to improve existing bioprocesses or develop new ones.

The ß-galactosidase immobilization protocol determines its performance as catalysts in the kinetically controlled synthesis of lactulose.

In this paper, 3 different biocatalysts of ß-galactosidase from Kluyveromyces lactis have been prepared by immobilization in chitosan activated with glutaraldehyde (Chi_Glu_Gal), glyoxyl agarose (Aga_Gly_Gal) and agarose coated with polyethylenimine (Aga_PEI_Gal). These biocatalysts have been used to catalyze the synthesis of lactulose from lactose and fructose. Aga-PEI-Gal only produces lactulose at 50 °C, and not at 25 or 37 °C, Aga_Gly_Gal was unable to produce lactulose at any of the assayed temperatures while Chi_Glu_Gal produced lactulose at all assayed temperatures, although a lower yield was obtained at 25 or 37 °C. The pre-incubation of this biocatalyst at 50 °C permitted to obtain similar yields at 25 or 37 °C than at 50 °C. The use of milk whey instead of pure lactose and fructose produced an improvement in the yields using Aga_PEI_Gal and a decrease using Chi_Glu_Gal. The operational stability also depends on the reaction medium and of biocatalyst. This study reveals how enzyme immobilization may greatly alter the performance of ß-galactosidase in a kinetically controlled manner, and how medium composition influences this performance due to the kinetic properties of ß-galactosidase.