Glucoamylase isoform (GAII) purified from a thermophilic fungus Scytalidium thermophilum 15.8 with biotechnological potential

Scytalidium thermophilum 15.8 produced two extracellular glucoamylases. Using a DEAE-Cellulose chromatographic column glucoamylases form II (GAII) was separated and purified from glucoamylases form I (GAI) that was previously purified and characterised (Cereia et al., 2000) when the filtrate of the culture medium was applied to a DEAE-Cellulose chromatographic column. GAII bound to the DEAECellulose and was eluted with a NaCl gradient, while GAI did not bind to the resin. GAII presentedelectrophoretic homogeneity in 6% denaturing and non-denaturing PAGE, separately, with a molecular mass of 83 kDa, after the second round DEAE-Cellulose purification step. The enzyme pI was 7.2.Optima pH and activity temperature were 5.5 and 55ºC respectively for starch and maltose as substrates, with a termostability of 2.5 min at 60ºC. Enzymatic activities were activated by 1 mM Na+, Mn2+ and Mg2+ or 10 mM NH4+, Ba2+ and Mg2+. The carbohydrate content was 10%. The kinetic parameters Km and Vmax with starch and maltose as substrate were 0.2 and 1.5 mg/ml, and 22.3 and 4.39 U/mg of protein, respectively. The amino acid sequence of GAII had 92% homology with theglucoamylase of Humicola grisea var. thermoidea after 13 cycles. Generally, GAII had different properties compared with GAI (Cereia et al., 2000)

model predictive control tools for evolutionary plants

The analysis and design of control system configurations for automated production systems is generally a challenging problem, in particular given the increasing number of automation devices and the amount of information to be managed. This problem becomes even more complex when the production system is characterized by a fast evolutionary behaviour in terms of tasks to be executed, production volumes, changing priorities, and available resources. Thus, the control solution needs to be optimized on the basis of key performance indicators like flow production, service level, job tardiness, peak of the absorbed electrical power and the total energy consumed by the plant. This paper proposes a prototype control platform based on Model Predictive Control (MPC) that is able to impress to the production system the desired functional behaviour. The platform is structured according to a two-level control architecture. At the lower layer, distributed MPC algorithms control the pieces of equipment in the production system. At the higher layer an MPC coordinator manages the lower level controllers, by taking full advantage of the most recent advances in hybrid control theory, dynamic programming, mixed‐integer optimization, and game theory. The MPC-based control platform will be presented and then applied to the case of a pilot production plant

Different covalent immobilizations modulate lipase activities of Hypocrea pseudokoningii

This article belongs to the Special Issue Lipases and Lipases Modification.Enzyme immobilization can promote several advantages for their industrial application. In this work, a lipase from Hypocrea pseudokoningii was efficiently linked to four chemical supports: agarose activated with cyanogen bromide (CNBr), glyoxyl-agarose (GX), MANAE-agarose activated with glutaraldehyde (GA) and GA-crosslinked with glutaraldehyde. Results showed a more stable lipase with both the GA-crosslinked and GA derivatives, compared to the control (CNBr), at 50 °C, 60 °C and 70 °C. Moreover, all derivatives were stabilized when incubated with organic solvents at 50%, such as ethanol, methanol, n-propanol and cyclohexane. Furthermore, lipase was highly activated (4-fold) in the presence of cyclohexane. GA-crosslinked and GA derivatives were more stable than the CNBr one in the presence of organic solvents. All derivatives were able to hydrolyze sardine, açaí (Euterpe oleracea), cotton seed and grape seed oils. However, during the hydrolysis of sardine oil, GX derivative showed to be 2.3-fold more selectivity (eicosapentaenoic acid (EPA)/docosahexaenoic acid (DHA) ratio) than the control. Additionally, the types of immobilization interfered with the lipase enantiomeric preference. Unlike the control, the other three derivatives preferably hydrolyzed the R-isomer of 2-hydroxy-4-phenylbutanoic acid ethyl ester and the S-isomer of 1-phenylethanol acetate racemic mixtures. On the other hand, GX and CNBr derivatives preferably hydrolyzed the S-isomer of butyryl-2-phenylacetic acid racemic mixture while the GA and GA-crosslink derivatives preferably hydrolyzed the R-isomer. However, all derivatives, including the control, preferably hydrolyzed the methyl mandelate S-isomer. Moreover, the derivatives could be used for eight consecutive cycles retaining more than 50% of their residual activity. This work shows the importance of immobilization as a tool to increase the lipase stability to temperature and organic solvents, thus enabling the possibility of their application at large scale processes.This work was supported by grants from Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP, process No. 2013/50892-5; 2010/52322-3), Conselho de Desenvolvimento Científico e Tecnológico (CNPq process No. 406838/2013-5; 563260/2010-6). This project is also part of the National Institute of Science and Technology of the Bioethanol (No. 574002/2008-1), CNPq—Ciência sem Fronteira (No. 242775/2012-8). JAJ and MLTMP are Research Fellows of CNPq. MGP and ACV are supported by CNPq. FDAF was recipient of a FAPESP Fellowship.Peer reviewe