comparison of glycolytic and chitinolytic enzyme activities between desert and oasis flies of Phlebotomus papatasi to evaluate potential differences in susceptibility to infection with Leishmania major
stabilization of enzyme against thermal denaturation by intermolecular and intramolecular crosslinking of the surface nucleophilic functional groups with diisocyanate homobifunctional reagents of various lengths. Crosslinking with 1,4-diisocyanatobutane is most effective in enhancing thermostability. Stability is improved dramatically by crosslinking 0.5 mg/ml of protein with 30 micromol/ml of the reagent. Molecular engineering by crosslinking reduces the first-order thermal denaturation constant at 60°C from 1.567 per min for the native enzyme to 0.437 per min for the stabilized enzyme. The best crosslinking treatment increases the activation energy for denaturation from 391 kJ per mol for the native protein to 466 kJ per mol for the stabilized enzyme
cell wall isozyme CIN2 and the abscisic acid antagonism is a potential intervention point for breeding exsertion during or after drought stress at heading
the enzymes invertase, diphosphate-dependent phosphofructokinase and fructose-1,6-bisphosphatase, show distinct activity patterns during development and may affect sugar and acid accumulation and sugar composition of strawberries
increased expression of invertases, among other genes involved in sucrose and starch synthesis and degradation, during clubroot disease caused by the obligate biotrophic protist, Plasmodiophora brassicae
the expression of INVA and INVB from Zymomonas mobilis in Pichia pastoris yields new catalysts with improved catalytic properties, making them suitable candidates for ethanol production from cane molasses
the expression of INVA and INVB from Zymomonas mobilis in Pichia pastoris yields new catalysts with improved catalytic properties, making them suitable candidates for ethanol production from cane molasses
invertase 2 has potential to be applied in food industry since its product, inverted sugar, is used in candies and syrup production, while fructooligosacharides are prebiotics, low calorie and noncariogenic sweeteners
invertase 2 has potential to be applied in food industry since its product, inverted sugar, is used in candies and syrup production, while fructooligosacharides are prebiotics, low calorie and noncariogenic sweeteners
the expression of INVA and INVB from Zymomonas mobilis in Pichia pastoris yields new catalysts with improved catalytic properties, making them suitable candidates for a number of industrial applications
the expression of INVA and INVB from Zymomonas mobilis in Pichia pastoris yields new catalysts with improved catalytic properties, making them suitable candidates for a number of industrial applications
enzymatic sucrose hydrolysis with invertase entrapped into calcium alginate beads is more attractive for industrial use than the acid hydrolysis process
the enzyme is important in industrial production of non-crystallizable invert sugar and soft-centered chocolates, development of methods for identification and determination of the enzyme for industrial use from plants
improved enzyme production by exposure of cells to 0.06 mg/ml N-methyl-N-nitro-N-nitrosoguanidine 0.06 mg/ml for 20 min. The resulting strain NG-5 offers improved extracellular beta-fructofuranidose production of 34 U/ml/min compared to the wild-type strain's 1.15 U/ml/min. A 40fold increase of beta-fructofuranidose activity can be achieved with the process parameters incubation period 48 h, sucrose concentration 5.0 g/l, initial pH of 6.0, inoculum size 2.0% v/v, 16 h old, and urea concentration of 0.2%, w/v
immobilization of invertase on a hydrogel comprised of methacrylic acid and N-vinyl pyrrolidone and ethyleneglycol dimethacrylate, converted to nanogel by an emulsification method and further functionalized by Curtius azide reaction. The values of Vmax, maximum reaction rate, of 0.123 unit/mg, Michaelis constant of 7.429 mol/L and energy of activation of 3.511 kJ/mol for the immobilized invertase are comparable with those of the free invertase at optimum conditions. The covalent immobilization enhances the pH and thermal stability of invertase
immobilization of invertase on a porous silicon layer with appropriate catalytic behavior for the sucrose hydrolysis. The procedure is based on support surface chemical oxidation, silanization, activation with glutaraldehyde and finally covalent bonding of the free enzyme to the functionalized surface. Vmax undergoes a substantial increase of about 30% upon immobilization. The value of Km increases by a factor of 1.53 upon immobilization. The initial activity is still preserved up to 28 days while the free enzyme undergoes a 26% loss of activity after the same period
immobilization of invertase on polyurethane rigid adhesive foam for application in an enzymatic bioreactor. The kinetic parameters are Km 46.5 mM for immobilized invertase versus 61.2 mM for free invertase. The immobilized invertase derivative maintains 50.1% of initial activity, i.e. 69.17 U/g support, for 8 months. The bioreactor shows the best production of inverted sugar syrup using up-flow rate of 0.48 l/h with average conversion of 10.64%/h at a feeding rate of 104 /h
production of high levels of cell extract and extracellular invertases when grown under submerged fermentation and solid-state fermentation, using agroindustrial products or residues as substrates, mainly soy bran and wheat bran, at 40°C for 72 h and 96 h, respectively. Addition of glucose or fructose in submerged fermentation inhibits enzyme production, while the addition of 1% (w/v) peptone as organic nitrogen source enhances the production by 3.7fold. 1% (w/v) (NH4)2HPO4 inhibits enzyme production around 80%