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Batch enzymatic hydrolysis processes require post-treatments to obtain a glucose syrup free of nonhydrolyzed materials and enzymes. An alternative process is the membrane process, which does not require the addition of chemicals. When membrane and enzymatic hydrolysis processes are combined, the resulting process is known as the in situ product recovery (ISPR) process. The present ISPR process studies focus on the efficiencies of enzymatic hydrolysis with continuous feeding of substrate and/or enzymes. However, little attention has been paid to the enzyme immobilization effect, which can be generated using membranes in conjunction with enzymatic hydrolysis during the production process. Temperature and pH affect the efficiency of glucose syrup production during the enzymatic hydrolysis and membrane processes. In this study, a response surface methodology is used to achieve maximum glucose syrup production without a continuous feed of substrate and/or enzymes. This study also focuses on the evaluation of the membranes as an enzyme membrane reactor. The membrane system operates with submerged membranes of hollow fiber in polyvinylidene fluoride with pure wheat starch in discontinuous diafiltration mode. Results indicated that the maximum glucose production is 73.6 ± 4.3 gglucoseL–1at 61.5 °C and pH 4.8. Besides, the fouling layer in the membranes act as a reactor. This reactor contributes to greater stability and resistance to sudden changes in operating variables. The reactor also has the potential to be reused, thus reducing costs associated with new membranes and enzymes.

Glucose-6-phosphate dehydrogenase (G6PD; EC 1.1.1.49) deficiency is a common genetic abnormality affecting an estimated 400 million people worldwide. Clinical and biochemical analyses have identified many variants exhibiting a range of phenotypes, which have been well characterized from the hematological point of view. However, until now, their precise molecular basis has remained unknown. We have cloned and sequenced seven mutant G6PD alleles. In the nondeficient polymorphic African variant G6PD A we have found a single point mutation. The other six mutants investigated were all associated with enzyme deficiency. In one of the commonest, G6PD Mediterranean, which is associated with favism among other clinical manifestations, a single amino acid replacement was found (serine----phenylalanine): it must be responsible for the decreased stability and the reduced catalytic efficiency of this enzyme. Single point mutations were also found in G6PD Metaponto (Southern Italy) and in G6PD Ilesha (Nigeria), which are asymptomatic, and in G6PD Chatham, which was observed in an Indian boy with neonatal jaundice. In G6PD "Matera," which is now known to be the same as G6PD A-, two separate point mutations were found, one of which is the same as in G6PD A. In G6PD Santiago, a de novo mutation (glycine----arginine) is associated with severe chronic hemolytic anemia. The mutations observed show a striking predominance of C----T transitions, with CG doublets involved in four of seven cases. Thus, diverse point mutations may account largely for the phenotypic heterogeneity of G6PD deficiency.

This study deals with an experimental investigation into the trans-esterification behavior of two biocatalysts produced by different immobilization techniques of the same lipase from Pseudomonas cepacia. Biocatalysts catalyzed trans-esterification of commercial frying oil. It was verified that no enzyme leaching occurs and stepwise addition of ethanol is needed to improve the process performance. When stoichiometric ethanol has been added completely at the beginning of the reaction, percent mass fraction of esters reached 33% after 9 h and 52% after 30 h. Instead, when ethanol has been added in steps, ester production gradually increased at any time. Moreover, different amounts of biocatalyst were added to the reaction system and it was found that it is not necessary to add more than 3% of biocatalyst with respect to the oil mass to avoid inhibition. The immobilization method influences the reaction progress and the intermediate-glyceride profiles were analyzed. Results showed that the two biocatalysts have the same affinity towards triglycerides, but the covalently immobilized lipase (epobond P. cepacia) has a lower affinity towards diglycerides and monoglycerides and, in general, a lower activity than the absorbed lipase (lipo P. cepacia).

Thermal performance and stability over time are key parameters for the characterization and application of PCMs in the building sector. Generally, inorganic PCMs are dispersions of hydrated salts and additives in water that counteract phase segregation phenomena and subcooling. Traditional methods or in "house" methods can be used for evaluating thermal properties, while stability can be estimated over time by using optical techniques. By considering this double approach, in this work thermal and structural analyses of Glauber salt based composite PCMs are conducted by means of non-conventional equipment: T-history method (thermal analysis) and Turbiscan (stability analysis). Three samples with the same composition (Glauber salt with additives) were prepared by using different sonication times and their thermal performances were compared by testing both the thermal cycling and the thermal properties. The stability of the mixtures was verified by the identification of destabilization phenomena, the evaluation of the migration velocities of particles and the estimation of variation of particle size.