Invertase properties

Cell wall properties of transgenic tobacco plants that express a yeast derived acid invertase in their vacuole... 

Planteose is an exception to the general behavior of the raffinose oligosaccharides in that it is stable against the action of yeast invertase.22 29 This property, shared also by melezitose,45 is explained by the lack of an unsubstituted /3-D-fructofuranoside group. The resistance to invertase action can be utilized in the preparative separation of planteose from sucrose.29... 

Van den Ende, W. and Van Laere, A., Purification and properties of an invertase with sucrose sucrose fructosyl transferase (SST) activity from the roots of Cichorium intybus L., New Phytol., 123, 31-37, 1993. 

Both fructooligosaccharide synthesis and sucrose hydrolysis are catalyzed by most of the fructosyltransferases and 3-fmctofuranosidases (invertases) in the presence of sucrose. The transferase hydrolase raho, which determines the maximum yield of fructooligosaccharide, depends basically on two parameters the concentra-hon of sucrose and the intrinsic enzyme properties, that is its ability to bind the nucleophile (to which a fructose is transferred) and to exclude H2O from the acceptor binding site [11]. 

Forccd flow mode. Invertase, an enzyme, can be chemically immobilized to the surfaces of ceramic membrane pores by the technique of covalent bonding of silane-glutaraldehyde [Nakajima et al., 1989b]. The substrate (reactant), during the sucrose conversion process, enters the membrane reactor in a crossflow mode. Under suction from the other side of the membrane, the substrate flows into the enzyme-immobilized membrane pores where the bioconversion takes place. Both the product and the unreacted substrate indiscriminately pass through the membrane pores. Thus, no permselective properties are utilized in this case. The primary purpose of the membrane is to provide a well-engineered catalytic path for the reactant, sucrose. 

Properties White, crystalline powder sweet taste. D 1.465, mp (anhydrous) 118-119C, bp decomposes at about 130C, optical rotation +104.5 degrees. Soluble in water very slightly soluble in alcohol. Split by invertase to mehbiose and saccharose. Combustible. 

Stefuca V, Gemeiner P, Kurillova L, Danielsson B, Bales V (1990) Application of the enzyme thermistor to the direct estimation of intrinsic kinetics using the saccharose-immobilized invertase system. Enzyme Microb Technol 12 830 - 835 Stefuca V, Welwardova A, Gemeiner P, Jakubova A (1994) Application of enzyme flow microcalorimetry to the study of microkinetic properties of immobilized biocatalyst. Biotech-nolTech 8 497-502... 

Fig. 6. Investigation of kinetic properties of immobilized invertase by flow microcalorimetry in the circulation mode. Initial sucrose concentration 51 mM, invertase immobilization by biospecific binding on concanavalin A-bead cellulose was prepared by binding on concana-valin A linked to chlorotriazine-activated cellulose, a Raw experimental thermometric data b data after conversion by the procedure indicated in Fig. 4. Concentrations were determined spectrophotometrically (open symbols) and by transformation of thermometric data explained in Section 5 (closed symbols) [32]...

This approach was used for the study of the kinetic properties of invertase immobilized on the cellulose bead surface [27,30,33]. In the following example the kinetic model described for invertase was used [34]... 

The significance of Eq. (28) is that the thermometric data can be used for evaluation of the kinetic parameters Km and K , and, thus, for rapid determination of the kinetic properties of IMB preparations. This had been performed in the previous work by investigating the kinetic properties of immobilized invertase [27]. Typical kinetic data from this study are presented in Fig. 7. In this... 

Fig. 8. Flow microcalorimetric investigation of kinetic properties of invertase bound to Eupergit C activated by concanavalin A. The line corresponds to calculated data. The model involving high substrate conversion was used and parameters were estimated by nonlinear regression Vm= 1950 mM min-1, Km= 3420 mM, K = 246 mM, P = 2.7 K (unpubl. results)...

The last equation was used in several papers studying the kinetic properties of invertase, where substrate inhibition was evaluated in terms of the inhibition parameter K [27,30,31]. 

B. R., Dai, S., and Woodward, J., "Properties of carbohydrate-metabolizing enz5mies immobilized in sol-gel beads stabilization of invertase and -glucosidase by Blue Dextran", (2002) Bioteehnol. Lett. 24 783-790. 

CHEMICAL PROPERTIES stable in air stable under ordinary conditions of use and storage hazardous polymerization will not occur hydrolyzes to glucose and fructose by dilute acids and by invertase, a yeast enzyme optical rotation falls and is negative upon completion of hydrolysis does not reduce Fehling s solution (consists of two solutions, one of copper sulfate, the other of alkaline tartrate), forms an osazone, or show mutarotation fermentable, but resists bacterial decomposition when in high concentrations. FP (NA) LFL/UFL (NA) AT (NA) MEC (45g/cm ). 

The enhancement of enzyme yields by carbohydrate esters (Table 3) may be due, in part, to their surfactant properties. This is certainly true of sucrose monopalmitate, which has been found to increase yields, not only of invertase, but of many other enzymes listed in Table 4. Both Tween 80 and sucrose monopalmitate are nonionic surfactants relatively nontoxic to the organisms tested. At first, it was believed that only this type of surfactant possessed the stimulating effect. Later sodium oleate proved superior to Tween 80 for producing cellulase by some fungi. The anionic surfactants tend to be more toxic than the nonionics. The cationic agents, which are even more toxic, have not been found useful in this work. 

Chen JP, Wang HY (1998) Improved properties of bilirubin oxidase by entrapment in alginate-silicate sol-gel matrix. Biotechnol Tech 12(ll) 851-853 Chen Y, Kang ET, Neoh KG et al. (2000) Covalent immobilization of invertase onto the surface-modified polyaniline from graft copolymeiization with acrylic acid. Eur Polym J 36(10) 2095-2103... 

The properties of 3-D-fructofuranosidase (invertase) of Saccharomyces cerevisiae, and of the modified enzyme after removal of about 90% of the carbohydrate residues, have been found to differ considerably, not only in stability but also in their capacity to be renatured following inactivation by guanidinium chloride. The covalently bound carbohydrate of yeast 3-D-fructo-... 

Docolomansky, P., Breier, A., Gemeiner, P., and Ziegelhoifer, A., Screening of binding properties of con-A immobilized on bead cellulose by flow microcalorimetry using invertase and anti-con-A antibody as reporting systems. Anal. Lett., 1995, vol. 28, no. 15, pp. 2585-2594. 

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