María Luján Ferreira

Bio: María Luján Ferreira is an academic researcher from Universidad Nacional del Sur. The author has contributed to research in topics: Lipase & Candida antarctica. The author has an hindex of 32, co-authored 145 publications receiving 3071 citations. Previous affiliations of María Luján Ferreira include National Scientific and Technical Research Council.

PLA nano- and microparticles for drug delivery: an overview of the methods of preparation.

Abstract: The controlled release of medicaments remains the most convenient way of drug delivery. Therefore, a wide variety of reports can be found in the open literature dealing with drug delivery systems. In particular, the use of nano- and microparticles devices has received special attention during the past two decades. PLA and its copolymers with GA and/or PEG appear as the preferred substrates to fabricate these devices. The methods of fabrication of these particles will be reviewed in this article, describing in detail the experimental variables associated with each one with regard to the influence of them on the performance of the particles as drug carriers. An analysis of the relationship between the method of preparation and the kind of drug to encapsulate is also included. Furthermore, certain issues involved in the addition of other monomeric substrates than lactic acid to the particles formulation as well as novel devices, other than nano- and microparticles, will be discussed in the present work considering the published literature available.

Burkholderia cepacia lipase: A versatile catalyst in synthesis reactions

Abstract: The lipase from Burkholderia cepacia, formerly known as Pseudomonas cepacia lipase, is a commercial enzyme in both soluble and immobilized forms widely recognized for its thermal resistance and tolerance to a large number of solvents and short-chain alcohols. The main applications of this lipase are in transesterification reactions and in the synthesis of drugs (because of the properties mentioned above). This review intends to show the features of this enzyme and some of the most relevant aspects of its use in different synthesis reactions. Also, different immobilization techniques together with the effect of various compounds on lipase activity are presented. This lipase shows important advantages over other lipases, especially in reaction media including solvents or reactions involving short-chain alcohols.

Catalytic Transformation of Lignin for the Production of Chemicals and Fuels

Abstract: and Fuels Changzhi Li,† Xiaochen Zhao,† Aiqin Wang,† George W. Huber,†,‡ and Tao Zhang*,† †State Key Laborotary of Catalysis, iChEM (Collaborative Innovation Center of Chemistry for Energy Materials), Dalian Institute of Chemical Physics, Chinese Academy of Sciences, Dalian 116023, China ‡Department of Chemical and Biological Engineering, University of WisconsinMadison, Madison, Wisconsin 53706, United States

Organocatalytic ring-opening polymerization.

Abstract: Modern synthetic methods have revolutionized polymer chemistry through the development of new and powerful strategies for the controlled synthesis of complex polymer architectures. 1-5 Many of these developments were spawned by new classes of transition metal catalysts for the synthesis of new polyolefin microstructures, 5 the design of highly efficient families of “living” polymerization strategies for the synthesis of block, graft, and star polymers, 6-12 controlled methods for the synthesis of dendritic macromolecules, 3,13,14

An overview of technologies for immobilization of enzymes and surface analysis techniques for immobilized enzymes

Abstract: The current demands of sustainable green methodologies have increased the use of enzymatic technology in industrial processes. Employment of enzyme as biocatalysts offers the benefits of mild reaction conditions, biodegradability and catalytic efficiency. The harsh conditions of industrial processes, however, increase propensity of enzyme destabilization, shortening their industrial lifespan. Consequently, the technology of enzyme immobilization provides an effective means to circumvent these concerns by enhancing enzyme catalytic properties and also simplify downstream processing and improve operational stability. There are several techniques used to immobilize the enzymes onto supports which range from reversible physical adsorption and ionic linkages, to the irreversible stable covalent bonds. Such techniques produce immobilized enzymes of varying stability due to changes in the surface microenvironment and degree of multipoint attachment. Hence, it is mandatory to obtain information about the structure of the enzyme protein following interaction with the support surface as well as interactions of the enzymes with other proteins. Characterization technologies at the nanoscale level to study enzymes immobilized on surfaces are crucial to obtain valuable qualitative and quantitative information, including morphological visualization of the immobilized enzymes. These technologies are pertinent to assess efficacy of an immobilization technique and development of future enzyme immobilization strategies.