Enzyme Kinetics
Mostrando 13-24 de 1004 artigos, teses e dissertações.
-
13. Additives on in vitro ruminal fermentation characteristics of rice straw
ABSTRACT The objective of this study was to evaluate the effects of mineral and protein-energy (MPES), exogenous fibrolytic enzyme supplements (ES), combination of MPES + ES, and straw without supplement (WS) on digestibility, fermentation kinetic parameters, cumulative gas production, methane, CO2 production, and volatile fatty acid concentration of rice st
R. Bras. Zootec.. Publicado em: 2017-03
-
14. Characterisation of iunH gene knockout strain from Mycobacterium tuberculosis
BACKGROUND Tuberculosis (TB) is an infectious disease caused mainly by the bacillus Mycobacterium tuberculosis. The better understanding of important metabolic pathways from M. tuberculosis can contribute to the development of novel therapeutic and prophylactic strategies to combat TB. Nucleoside hydrolase (MtIAGU-NH), encoded by iunH gene (Rv3393), is an
Mem. Inst. Oswaldo Cruz. Publicado em: 2017-03
-
15. A broad pH range and processive chitinase from a metagenome library
Chitinases are hydrolases that degrade chitin, a polymer of N-acetylglucosamine linked β(1-4) present in the exoskeleton of crustaceans, insects, nematodes and fungal cell walls. A metagenome fosmid library from a wastewater-contaminated soil was functionally screened for chitinase activity leading to the isolation and identification of a chitinase gene nam
Braz J Med Biol Res. Publicado em: 05/01/2017
-
16. Applications of Plackett–Burman and Central Composite Design for the Optimization of Novel Brevundimonas diminuta KT277492 Chitinase Production, Investigation of its Antifungal Activity
ABSTRACT Biological control strategy which can damage chitin, a vital component of pathogenic fungi and arthropods promises a safe solution for many fungal problems. And it’s more favorable than chemicals which increase health risks and environmental problems. Thus, the chitinase producers appear potential candidates of biological control of pathogenic fun
Braz. arch. biol. technol.. Publicado em: 31/10/2016
-
17. Cholinesterases Inhibition by Novel cis- and trans-3-Arylaminocyclohexyl N,N-Dimethylcarbamates: Biological Evaluation and Molecular Modeling
The present study describes the synthesis, assessment of the anticholinesterase activity and the inhibition type of novel cis- and trans-3-arylaminocyclohexyl N,N-dimethylcarbamates. In vitro inhibition assay by Ellman's method with human blood samples showed that carbamates were selective for butyrylcholinesterase (BuChE) with compound concentration that in
J. Braz. Chem. Soc.. Publicado em: 2016-09
-
18. Thermal inactivation kinetics of partially purified mango pectin methylesterase
Abstract Kinetic parameters of thermal inactivation of pectin methylesterase (PME) in a partially purified mango enzyme extract were determined. The PME of mango partially purified by salting out showed different patterns of thermal inactivation, indicating the presence of a thermostable fraction at 70 °C and a thermolabile fraction at lower temperatures. T
Food Sci. Technol. Publicado em: 30/06/2016
-
19. Double mutation of Saccharomyces cerevisiae for enhanced β-D-fructofuranosidase fructohydrolase productivity and application of growth kinetics for parametric significance analysis
Abstract The kinetics of an extracellular β-D-fructofuranosidase fructohydrolase production by Saccharomyces cerevisiae in a chemically defined medium, i.e., sucrose peptone agar yeast extract at pH 6, was investigated. The wild-type was treated with a chemical mutagen, methyl methane sulfonate. Among the six mutants isolated, methyl methane sulfonate-V was
Braz. J. Microbiol.. Publicado em: 2016-03
-
20. EFFECTIVE ALKALINE PEROXIDE OXIDATION PRETREATMENT OF SHEA TREE SAWDUST FOR THE PRODUCTION OF BIOFUELS: KINETICS OF DELIGNIFICATION AND ENZYMATIC CONVERSION TO SUGAR AND SUBSEQUENT PRODUCTION OF ETHANOL BY FERMENTATION USING Saccharomyces cerevisiae
Abstract Shea tree sawdust delignification kinetic data during alkaline peroxide pretreatment were investigated at temperatures of 120 °C, 135 °C, and 150 °C. The activation energy during delignification was 76.4 kJ/mol and the Arrhenius constant was calculated as 8.4 x 106 per min. The reducing sugar yield for the treated to the untreated biomass was abo
Braz. J. Chem. Eng.. Publicado em: 2016-03
-
21. ALCALOIDES ACRIDÔNICOS INIBEM CATEPSINA L E V
Cathepsins represent a class of enzymes that has the primary function of randomly degrading proteins in the lysosomes, although are also involved in different pathologies. The aim of this paper was to evaluate the capacity of acridone alkaloids isolated from Swinglea glutinosa (Rutaceae) to inhibit cathepsin L in vitro . The IC50 values found were in the 0.8
Quím. Nova. Publicado em: 2016-01
-
22. Partial Purification and Characterization of β-glucosidase fromMonascus sanguineus
The aim of the present work was to study the production and characterization of β-glucosidase from Monascus sanguineus. Agro-waste residues were screened to obtain the maximum yield of enzyme. Jack fruit seed was the best substrate for enzyme production. Studies on the optimization of pH and temperature showed acidic pH favorable for enzymatic activity, whe
Braz. arch. biol. technol.. Publicado em: 14/10/2014
-
23. Kinetics Study of Extracellular Detergent Stable Alkaline Protease from Rhizopus oryzae
In this study, extracellular alkaline protease was produced from Rhizopus oryzae in submerged fermentation using dairy waste (whey) as a substrate. Fermentation kinetics was studied and various parameters were optimized. The strain produced maximum protease at initial medium pH of 6.0 medium depth of 26 mm, inoculum size of 2% at incubation temperature of 35
Braz. arch. biol. technol.. Publicado em: 29/08/2014
-
24. A new approach to evaluate immobilization of β-galactosidase on Eupergit® C: structural, kinetic, and thermal characterization
This study aimed to evaluate β-galactosidase immobilization. For this purpose, the ionic strength of the buffer, reaction time, amount of the immobilization support, and pH were evaluated by a central composite design. Assay 8, which consisted of 1.5 mol L-1 phosphate buffer (pH 7.5) and a reaction time of 2 h, produced the maximum yield. Eupergit® C (400
Quím. Nova. Publicado em: 2014-06