l-asparaginase (EC 3.5.1.1) is an enzyme that catalysis mainly the asparagine hydrolysis in l-aspartic acid and ammonium. This enzyme is presented in different organisms, such as microorganisms, vegetal, and some animals, including certain rodent's serum, but not unveiled in humans. It can be used as important chemotherapeutic agent for the treatment of a variety of lymphoproliferative disorders and lymphomas (particularly acute lymphoblastic leukemia (ALL) and Hodgkin's lymphoma), and has been a pivotal agent in chemotherapy protocols from around 30 years. Also, other important application is in food industry, by using the properties of this enzyme to reduce acrylamide levels in commercial fried foods, maintaining their characteristics (color, flavor, texture, security, etc.) Actually, l-asparaginase catalyzes the hydrolysis of l-asparagine, not allowing the reaction of reducing sugars with this aminoacid for the generation of acrylamide. Currently, production of l-asparaginase is mainly based in biotechnological production by using some bacteria. However, industrial production also needs research work aiming to obtain better production yields, as well as novel process by applying different microorganisms to increase the range of applications of the produced enzyme. Within this context, this mini-review presents l-asparaginase applications, production by different microorganisms and some limitations, current investigations, as well as some challenges to be achieved for profitable industrial production.
Polysiloxane-polyvinyl alcohol hybrid matrix was prepared by a sol-gel technique and its capacity to bind porcine pancreatic lipase investigated. The loading of 250 units g −1 support was shown to be effective, resulting in an immobilized lipase with high catalytic activity. Both free and immobilized lipases were characterized by determining the activity profile as a function of pH, temperature, substrate concentration and thermal stability. Application of the immobilized lipase in non-conventional biocatalysis for the synthesis of surfactants and biodiesel was also analyzed. Production of sugar fatty acid esters was found to be dependent on the carbohydrate and the highest molar conversion (50% in 3-4 h of reaction) was achieved for substrates containing fructose and lauric or oleic acids. Biodiesel synthesis from babassu oil and ethanol, propanol or butanol was feasible and regardless of the kind of alcohols, results revealed that the immobilized PPL could efficiently convert triglycerides to fatty acid alkyl esters attaining yields varying from 75 to 95%.
The objective of this work was to produce an immobilized form of lipase from Burkholderia cepacia (lipase PS) with advantageous catalytic properties and stability to be used in the ethanolysis of different feedstocks, mainly babassu oil and tallow beef. For this purpose lipase PS was immobilized on two different non-commercial matrices, such as inorganic matrix (niobium oxide, Nb(2)O(5)) and a hybrid matrix (polysiloxane-polyvinyl alcohol, SiO(2)-PVA) by covalent binding. The properties of free and immobilized enzymes were searched and compared. The best performance regarding all the analyzed parameters (biochemical properties, kinetic constants and thermal stability) were obtained when the lipase was immobilized on SiO(2)-PVA. The superiority of this immobilized system was also confirmed in the transesterification of both feedstocks, attained higher yields and productivities.
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