Invertase Related terms: Fructose, Glucose, Enzymes, Genes, Proteins, Invertases (B-d-fructofuranosidase) are present in multiple forms in most plant tissues, and there are numerous studies describing these enzyme entities (for Enzymes review on early literature see Avigad, 1982; apRees, 1984; Hawker, 1985). ‘Sugars, Sucrose From: Plant Biochemistry, 1997 a View all Topics > wh, Download as PDF QQ Setalert © About this page Carbohydrate Metabolism RIN. Chibbar, .. M. Baga, in Reference Module in Food Science, 2016 Sucrose Invertase and SS are the two enzymes capable of cleaving sucrose present in plants. invertases catalyze the irreversible hydrolysis of sucrose to free glucose and fructose. Based on optimum pH of their activity, invertases, are grouped into acidic (optimum pH 4.0-5.5) and alkaline/neutral types (optimum pH 7.0-8.0). Acidic invertases are mainly found in cytosol and occasionally in cell walls, whereas alkaline/neutral types are abundant in vacuoles and cell walls. Alkaline/neutral invertases have recently been reported in chloroplasts and mitochondria. Alkaline invertases are sucrose-specific, while neutral invertase from carrot can also mediate raffinose and stachyose hydrolyses. The cell wall invertases hydrolyze the incoming translocated sucrose into glucose and fructose molecules. SucS catalyzes the reversible reaction converting sucrose and UDP to fructose and UDP-glucose. Fructose is available for respiration and the UDP-glucose can enter the hexose phosphate pool for further metabolic processes. $5, compart mentalized in the cytosol, is the main enzyme that degrades sucrose in starch storage organs such as developing seeds or in rapidly growing tissues that are converting sucrose to cell wall structural polysaccharides. In slow-growing and mature cells, invertase is the major enzyme hydrolyzing sucrose, which provides substrates for respiration. , Purchase book Enzymes Used in the Food Industry: Friends or Foes? Rachana Singh, .. Shweta Sachan, in Enzymes in Food Biotechnology, 201948.2.10 Invertase Invertase is S-bD-fructo-furanosidase isolated from S. cerevisiae and other microorganisms. Hydrolysis from rerted sugar is one of invertase’s sucrose to fructose and glucose is catalyzed by this enzyme. The production of numerous applications. Due to its sweetening effects, which are more than sucrose, it has great industrial significance and has good prospects for its use in biotechnology. Invertase is more active at temperatures between 40 and 60°C and pH ranging from 3 to 5. Microorganisms such as filamentous fungi are good producers of invertase with potential use in various industries. Soares et al. (2012) cultivated the filamentous fungus Rhizopus sp. in a wheat bran medium and obtained invertase. Another potential invertase-producing fungus is Aspergillus casiellus. it was inoculated in a soybean meal medium and after 72 h its crude extract was isolated. As most invertases used in the industry are produced by yeasts, the search for high yielding fungi is a requisite. , Purchase book Plant-Derived Enzymes: A Treasure for Food Biotechnology ‘Anju Meshramy, ... Nidhi Srivastava, in Enzymes in Food Biotechnology, 2019 28.2.6 Invertase EC Numbs 3.21126 Source: Phloem of higher plants Used in: Food Molecular weight: 205 kDa Substrate: Sucrose Product: Glucose and fructose Invertase occurs both inside and outside the cell It is produced by the submerged controlled aerobic fermentation of a nontoxigenic, nonpathogenic strain of Saccharomyces cerevisiae, extracted after washing and autolysis (Uma et al,, 2010). Other names include glucosucrase, Saccharase, beta-h-fructosidase, beta-fructosidase, sucrase, invertin, fructo-sylinvertase, maxinvert L 1000, acid invertase, and alkaline invertase. The systematic name is beta- fructofuranosidase. The enzyme has a broad range of industrial applications such as the production of confectionaries with liquid contents, as in the case of some chewing gums. It also facilitates the formation of ethanol from cane molasses. However, the use of invertase is very limited because another enzyme, glucose isomerase, can help in the conversion of glucose to fructose at a cheaper cost (Uma et al., 2010). For taste and health reasons, the food industry requires highly purified invertase for use. Its also used in the preparation of digestive aid tablets, chocolates, infant food formulas, the assimilation of fortified wines ete. (Christopher and kumbalwar, 2015) (Fig. 28.10) , Purchase bookCarbohydrate Metabolism: Storage Carbohydrates G. Avigad, P.M. Dey, in Plant Biochemistry, 1997 (ii) Metabolic role of invertase Invertase isoenzymes are potentially to be found in all compartments which may contain sucrose as a metabolite whether as a transient or a stored molecule. In the cytosol, sucrose synthase provides an important alternative to invertase action and sometimes even becomes the dominant obligatory route of sucrose cleavage. The degree of expression of each of the invertase isoenzymes can show large variation according to the physiological and developmental stage of the particular organ exarnined and may vary in different species of plants. The molecular basis for the regulatory patterns of invertase activity is little understood. A description of several selected number of studies which illustrate a role for invertase in overall carbohydrate fluxes is presented in the following examples. In the ripening fruits of strains of cultivated tomatoes, sucrose accumulates because of a very low ability to produce acid invertase, whereas other strains which are strong acid invertase producers accumulate glucose and fructose (Miron & Schaffer, 1991; Yelle et al, 1991; Stommel, 1992; Klann et al., 1993). It has been suggested that when sucrose accumulates in fruit with diminished vacuolar invertase, its level is dominantly determined by a striking increase in the activity of SPS (Dali et al, 1992). Sucrose synthase activity is the major reaction responsible for sucrose utilization in these senescent fruit. Tomato hybrids which incorporated the acid invertase genes produce the enzyme both in the apoplast and in the vacuole and accumulate hexoses rather than sucrose. In a related experiment, introduction of the cDNA of acid invertase in the antisense direction into an invertase-producing tomato, resulted in a significant increase of sucrose accumulation (Ohyama et al, 1995). In the tomato, similar to other plants, mechanical wounding or fungal infection strongly induced increased expression of acid invertase (Sturm & Chrispeels, 1990; Benhamou et al, 191; Ohyama et al, 1995). The physiological value of this phenomenon is not clear, but it may be related to the profound changes elicited under such conditions by the oligosaccharine regulators. Transgenic tobacco plants which express yeast invertase were used to evaluate the relative role of different subcellular compartments in relation to sucrose metabolism. These transformed plants were of stunted growth, had distinct morphological changes in the leaves, a reduced rate of photosynthesis and increased respiration. ‘Compared to the normal non-transformed plants, accumulation of starch, sucrose and reducing hexoses had greatly increased in the illuminated leaves. Starch levels did not diminish even after a prolonged dark period indicating deficiencies in its mobilization into sucrose and in sugar transport. Some variation in the distribution and level of accumulated sugars was noticed depending on whether the inserted yeast invertase was localized in the cell wall, the cytosol or vacuolar compartments (Stitt et a, 1990; Sonnewald et al, 1991, Heineke et al, 1994a,b). Similar to the creation of transgenic tobacco plants, yeast invertase has been expressed in transformed potato plant (Heineke et al, 1992). In this case there was a large accumulation of glucose and fructose and elimination of sucrose from the apoplast in the leaves. Consequently, the osmolarity of the cell sap was elevated, tubers which were smaller in size and number contained higher levels of monosaccharide and less starch, all of which reflected the decreased level of sucrose that was available for transport. It is interesting that in the mature and stored excised and stored potato tubers, there was a sharp decline in the activity of sucrose synthase, and acid invertase activity was retained as the dominating catalyst responsible for sucrose cleavage (Ross & Davies, 1992). This suggests that the presence of sucrose itself contributes to the regulation of both sucrose synthase and invertase{gene expression. in another experiment (Zrenner ef ai. 14¥9), tubers of transgenic potato piants wnicn expressea antisense RINA for sucrose synthase had low levels of this enzyme, but expressed a large increase of both alkaline and acid invertase activity resulting in high concentrations of glucose and fructose. These ‘antisense’ tubers also had accumulated a low level of starch suggesting that sucrose synthase activity is a key determinant in regulating carbohydrate sink strength in the tubers. The indispensable need for invertase to allow normal tissue development is seen in the seed miniature-1 (mn) mutant of maize. The homozygote of this mutant lost the ability to produce invertase in the basal endosperm cells, resulting in an inability to sustain normal development of kernels after pollination (Miller & Chourey, 1992). This finding supports the concept that endosperm invertase constitutes a key rate-limiting regulatory step which provide hexoses for the biosynthesis of sucrose and starch in the developing kernel (Dochlert & Felker, 1987), ‘An evaluation of the role of invertase in leaves (Huber, 1989) concluded that high activity of vacuolar invertase in such species as soybean and tobacco prevents sucrose accumulation within the vacuole. The hexoses produced are metabolically re-utilized in the cytoplasm, including some cycling back into sucrose synthesis. In comparison, other plants, such as pea, broad bean and spinach have a very low level of acid invertase. Consequently, accumulation of sucrose in the leaves is significant. In a starchless mutant of Nicotiana, more carbon is partitioned into sucrose during photosynthesis to levels which exceed the capacity for its export from the leaves. This sucrose is hydrolyzed by the vacuolar invertase, resulting in a 5-10-fold increase of free hexose accumulation (Huber & Hanson, 1992). oh, Purchase book CARBOHYDRATE METABOLISM RN. Chibbar, ... RL. Khandelwal, in Encyclopedia of Grain Science, 2004 Sucrose Invertase and SS are the two enzymes capable of cleaving sucrose present in plants. Invertases catalyze the irreversible hydrolysis of sucrose to free glucose and fructose. Invertases are present in the cytosol, vacuole, and in the cell walls. The cytosolic invertase is an alkaline type, active at pH 7.5, whereas the vacuolar and cell-wall invertases are acidic enzymes active at pH 5 or lower. The cell-wall invertases hydrolyze the incoming translocated sucrose into glucose and fructose molecules for conversion into storage carbohydrates. SS catalyzes the reversible reaction converting sucrose and UDP to fructose and UDP-glucose. Fructose is available for respiration and the UDP-glucose can enter the hexose-phosphate pool for further metabolic processes. SS, compartmentalized in the cytosol, is the main enzyme that degrades sucrose in starch-storage organs such as developing seeds or in rapidly growing tissues that are converting sucrose to cell-wall structural polysaccharides. In slow growing and mature cells, invertase is the major enzyme hydrolyzing sucrose and provides substrates for respiration. 4, Purchase bookThe Plant Invertases: Physiology, Biochemistry and Molecular Biology Z. Tymowska-Lalanne, M. Kreis, in Advances in Botanical Research, 1998 | INTRODUCTION Plant invertases (-D-fructofuranosidase EC 3.2.1.26) constitute a family of enzymes that hydrolyse sucrose into glucose and fructose. Three types of invertase, namely cell-wall, vacuolar and cytoplasmic, have been purified from a number of species and characterized at the biochemical level. Plant invertases, implicated in source/sink relationships, phloem loading and unloading, growth and other developmental processes, play important biological functions. However, the physiological roles of the individual members of the invertase family are not yet established and many questions remain to be elucidated. Recently, molecular approaches allowed the cloning of invertase genes and their cDNAs. Specific gene probes were used to carry out an investigation on the regulation of expression of individual members of this gene family during plant growth and development. Each of the 3 types of invertases is probably specified by several genes. For example, in carrot it exists at least 3 genes encoding cell-wall invertases and 2 genes encoding vacuolar invertases (Unger et al, 1994; Sturm et al., 1995). The activity of plant invertases can be modulated by organ- and developmental-specific gene expression and by various internal and external factors acting at the level of gene expression and/or prot activity. The existence of several invertase genes and the complex regulation of their expression and of enzyme activity, confers to plants a great flexibility in their carbohydrate metabolism. In this review, we describe the current knowledge about plant invertases from a biochemical and molecular point of view. ch, Purchase book Magnetic separation of nanobiostructured systems for innovation of biocatalytic processes in food industry ‘Anna llyina .. Cristébal N. Aguilar-Gonzélez, in Novel Approaches of Nanotechnology in Food, 2016 5.1.3 Invertases Invertase, also known as B-d-fructofuranosidefructohydrolase, B-fructofuranosidase, sucrase, saccharase. This enzyme catalyzes the hydrolysis of sucrose and related glycosides. It is commercially important due to its use for the hydrolysis of sucrose and is widely employed in food and beverage industries. Invertase is utilized to manufacture artificial honey, plasticizing agents, applied in cosmetics, pharmaceutical, and paper industries as well as in biosensor for sucrose detection (Kotwal and Shankar, 2009; Kulshrestha et al., 2013). In order to improve the recovering of invertase and to evaluate its stability and activity, Uzun et al. (2010) synthesized polyamidoamine (PAMAM) dendrimer on the surface of magnetite nanoparticles to enhance an invertase immobilization. It is important to mention that the quantity of immobilized enzymes on the (PAMAM) dendrimer-magnetite nanoparticles was up to 2.5 times higher in comparison with the magnetite nanoparticles ‘modified only with amino silane. The use of a surface-hyperbranched nanoparticles allows to anchor moreenzyme molecules onto the particle surface. Although the invertase affinity to sucrose decreased after immobilization, the stability of the immobilized enzyme toward pH (enzyme activity from 3.0 to 9.0), temperature, and storage was enhanced. ws, Purchase book Stability and Stabilization of Biocatalysts S. Bielecki, RI. Somiari, in Progress in Biotechnology, 1998 2 INTRODUCTION Invertase (B-fructofuranosidase, EC 3.2.1.26) is easily obtainable and exhibits transferase activity so can be exploited for synthesis of fructooligosaccharides using sucrose as the donor and acceptor of the transferred glycoside. But the transferase activity of this enzyme in aqueous media is typically low because water is the preferred acceptor [1]. Although it is known that the transglycosylating activity of glycosyl hydrolase may be