Enzymes Used in the Food Industry: Friends or Foes?

Rachana Singh , ... Shweta Sachan , in Enzymes in Food Biotechnology, 2019

48.two.v.2 Industrial Applications of Catalase

Catalase has great industrial importance for its applications in the removal of hydrogen peroxide used equally an oxidizing, bleaching, or sterilizing agent ( Arıca et al., 1999; Ertaş et al., 2000). The enzyme can be used in a limited amount in cheese production. It is used in the food manufacture and as well in egg processing, along with other enzymes. Catalase together with glucose oxidase is used in some food preservation, where superoxide dismutase, an antioxidant used in foods, produces H2O2, which is removed by catalase. Glucose oxidase and catalase are often used together in selected foods for preservation.

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General Principles

J.P. Kehrer , ... C.V. Smith , in Comprehensive Toxicology, 2010

1.14.6.1.2 Catalase

Catalase is another dismutase enzyme. It contains a heme moiety at the active site and converts ii hydrogen peroxide molecules to oxygen and water (eqn [28]). This reaction requires the presence of a small-scale corporeality of hydrogen peroxide to demark at the agile site in order to generate catalase compound I, which reacts with a second molecule of hydrogen peroxide. The Thousand m of catalase for H2O2 is in the m mol   fifty−one range, although its 5 max is extremely loftier. Because of the high One thousand m, catalase is most constructive at degrading high concentrations of hydrogen peroxide, such as might be establish in peroxisomes, the subcellular organelle where well-nigh catalase is localized.

(28) H two O 2 + H 2 O 2 → O ii + two H 2 O

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Microbial Enzyme in Food Biotechnology

Poonam Singh , Sanjay Kumar , in Enzymes in Food Biotechnology, 2019

2.four.6 Catalase

Catalase enzymes break downwardly hydrogen peroxide (H 2Oii) to water and oxygen molecules, which protects cells from oxidative damage past reactive oxygen species. Commercial catalases are produced from Aspergillus niger through a solid-state fermentation process (Fiedurek and Gromada, 2000). The major applications of catalase in the nutrient-processing industry include working with other enzymes like glucose oxidase, which is useful in nutrient preservation and egg processing, and sulphydryl oxidase, which under aseptic weather condition, can eliminate the effect of volatile sulphydryl groups, that is, they generate from thermal induction and are responsible for the cooked/off-flavor in ultra-pasteurized milk (Maur, 1996).

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Enzymology of Disturbed Soils

S. Kiss , ... Thou. Drăgan-Bularda , in Developments in Soil Science, 1998

Enzymological research in the Russia

Catalase and invertase activities in the revegetated spoil heaps around the Lebedin strip mine (located in the starooskol iron ore zone inside the Kursk Magnetic Anomaly region) were determined past Sviridova and Panozishvili (1979). The spoil heaps hither were of iii types: sandy, loamy and cretaceous-marly. They were revegetated with spontaneous and introduced grasses or with forest plants (sea buckthorn, black locust, and oleater). Later on 8-10 years the heaps revegetated with grasses were covered with a 1.5-2-cm sod, protecting them confronting erosion. In the 8-10-year-former wood stands the mass of litter reached densities of 0.5-0.nine   t ha-   1. Catalase action was measurable in the soil of all revegetated heaps. This activity, similar respiration (CO2 evolution) and humus accumulation, was more intense under herbaceous vegetation than under forest. Invertase activity was influenced not only by the nature of vegetation simply as well past the nature of spoil heaps. This activity was highest in the rhizosphere of bounding main buckthorn growing on the cretaceous-marly heap.

Zasorina (1985a, b) has studied, enzymologically, the spoil heaps near the Stoilensk iron strip mine (located within the Kursk Magnetic Anomaly region). These spoil heaps are of two types: sandy and cretaceous. The age of natural vegetation growing on heaps varied between 3 and 20 years. Invertase, urease, and catalase activities in the 0-v-cm layer of spoil heaps increased in parallel with the historic period of vegetation. The increase was more pronounced in the sandy spoils than in the cretaceous ones. During the growing flavour, the maximum activity values were registered in midsummer. In both immature and old spoil heaps, later on their revegetation with a mixture of vi grasses and legumes (bromegrass, fescue, wheatgrass, alfalfa, clover, and sainfoin), the enzymatic activities increased 1.5-3 times.

The investigations described by Shcherbakov et al. (1991) were related to the revegetation of the spoil heap in "Berezovyi log" (Broad gorge with birch) at the Lebedin mine. The spoil plots were covered with topsoil (chernozem) redeposited as dry cloth (plots I) or as wet cloth (pumping of soil and water mixtures) (plots Ii). Alfalfa was used for revegetation. In the third year of revegetation, samples were taken from the 0-10-, 10-20-, 20-30-, and 30-twoscore-cm depths of plots I and II and of the zonal soil (typical chernozem) that was not affected by the mining operations. The soil samples were analysed chemically (humus, total N, etc.), enzymologically (urease activity), and microbiologically (respiration, measured as COii evolution, and nitrification capacity). The samples collected from the centre and periphery of plots II were examined separately. The alfalfa yield in plots was also recorded.

All the parameters mentioned above tended to decrease with sampling depth. Urease activeness, respiration, and nitrification chapters gave much higher mean values in plots I than in plots II. At the same time, the mean values in plots I were similar to those obtained in the zonal soil. Consequently, redeposition of topsoil every bit dry material was, from a biological viewpoint, a better method than its redeposition equally wet fabric. Within plots Two no marked differences were observed between the central and peripheric places. It was too established that urease activity and nitrification capacity of plots I and II correlated significantly with the total North content; urease activity correlated with the alfalfa yield, too.

Germanova et al. (1995) adamant urease and catalase activities in the 0-v-cm layer of raw and 5-year-sometime spoil heaps at the Kostomuksha strip atomic number 26 mine located in the northern subzone of the taiga zone (northern Karelia). The adjacent, undisturbed podzolic soil under pino forest served for comparison.

Due to the unfavourable climatic atmospheric condition (number of days without frost: fourscore-ninety per year; medium monthly temperature in July: 14°C; annual amount of precipitations: 600 mm), development of natural vegetation was very poor; microbial numbers and diversity were small and enzyme activities were similarly low in both raw and 5-year-former spoils as compared to values registered in the undisturbed soil. As the beginning step in recultivation, levelling of spoils is recommended to improve their water regime.

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Stability and Stabilization of Biocatalysts

Hyon Joo Lee , ... Immature Je Yoo , in Progress in Biotechnology, 1998

4 SUMMARY

The activity of catalase in h2o-DMF solution (more than than 50% v/v) decreased to x % of the activity of the native catalase. In society to enhance the stability of catalase in the water-DMF solution (50% v/v), we carried out enzymatic reaction at –25 °C. In this case, it was observed that the action of catalase was maintained stable during 300  hours. The stability of catalase in organic media at –25 °C is better than in aqueous solution at 25 °C. Furthermore, though the initial activity of catalase in aqueous solution at 25 °C was higher than at –25 °C, the stability of catalase in aqueous solution at –25 °C was meliorate than at 25 °C. In molecular simulation, it was suggested that the properties of noncovalent forces as well every bit covalent forces were changed at low temperature and the catalase was maintained more than stable past these reasons. To optimize between the stability of enzyme in organic media and operation cost, we performed the enzymatic reaction at 0 °C using sorbitol as an additive. In this case, information technology was found that the activity of catalase in water-DMF solution using sorbitol was higher than that without using sorbitol. Enzymatic reaction at 0 °C using addtive tin exist therefore proposed as an effective stabilizing strategy for enzymatic reaction in organic media.

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Application of Microbial Enzymes in the Dairy Industry

Emad A. Abada , in Enzymes in Food Biotechnology, 2019

5.5 Catalase

The enzyme catalase could be utilized in a special application in club to produce cheese. In the case of producing some types of cheeses like Swiss, hydrogen peroxide, a potent oxidizer that is toxic to cells, is used in the country of pasteurization. It is used to retain natural milk enzymes that are useful for the finished production and flavor development of the cheese ( Perin et al., 2017). Fifty-fifty though the high-level heat of pasteurization could break down these enzymes, residues of hydrogen peroxide in the milk prevent the bacterial cultures that are needed for the bodily cheese production, so all traces of it must be removed. There are many resources used to get catalase enzymes like bovine livers or microbial sources. To alter hydrogen peroxide into water, also as molecular oxygen, catalase enzymes are added (Fig. 5.3).

Fig. 5.3

Fig. 5.3. Protein construction of catalase.

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Respiratory Toxicology

One thousand.V. Fanucchi , in Comprehensive Toxicology, 2010

viii.11.2.1.1(ii) Catalase

Like GPx, catalase accelerates the combination of two hydrogen peroxide molecules to produce water and oxygen. Catalase activity steadily increases during both the fetal and postnatal periods of lung development in humans ( McElroy et al. 1992) and in all experimental animals studied, including republic of guinea pigs, rats, and mice ( Table 2 ) (Chen and Frank 1993; Harman et al. 1990; Hayashibe et al. 1990; Sosenko and Frank 1989; Tanswell and Freeman 1984). In contrast to GPx, though, mRNA expression during this time is consistent with the increase in activity (Chen and Frank 1993). In humans, catalase activity increases 3.five-fold between 10 weeks of gestation and 3 months postnatal age, unlike SOD and GPx, which remain abiding throughout human being lung development (McElroy et al. 1992). The increase in catalase activeness during the late gestational period has been suggested past McElroy et al. (1992) to be linked to maturation of the surfactant system and has been correlated temporally to increases in lung dipalmitoylphosphatidylcholine (DPPC) content.

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Biology, genetic aspects and oxidative stress response of actinobacteria and strategies for bioremediation of toxic metals

Himadri Tanaya Behera , ... Lopamudra Ray , in Microbial Biodegradation and Bioremediation (Second Edition), 2022

9.3.v.2 CatR

Two specific types of catalases are produced by S. coelicolor; (one) CatA and CatB; and (2) CatC (catalase-peroxidase). CatA is necessary for constructive mycelium growth and Hydrogen peroxide induces the CatA expression, and Osmotic stress induces the CatB expression protecting the cell from the stress. Though the role of the catalase-peroxidase (CatC) has not been properly reported, it is temporarily expressed at the later stage of the exponential phase and initial stage of the stationary phase (Hahn et al., 2000).

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Microplastic Effects in Mullus surmuletus: Ingestion and Induction of Detoxification Systems

C. Alomar , ... S. Deudero , in Fate and Impact of Microplastics in Marine Ecosystems, 2017

Further on, antioxidant enzymes—catalase and superoxide dismutase—and the detoxification enzyme glutathione s-transferase (GST) activities and malondialdehyde (MDA) levels as a marking of lipid peroxidation were adamant in a subset of 40 samples of M. surmuletus with microplastics (n=20) and without microplastics (due north=20). No significant differences were reported in the antioxidant enzymes activities and in MDA between both groups. The activity of GST was significantly increased in Thousand. surmuletus containing microplastics (p<0.05), suggesting that the presence of microplastics activates the detoxification mechanisms.

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Cobalt

S.C. Gad , in Encyclopedia of Toxicology (Third Edition), 2014

Mechanism of Toxicity

Cobalt most ofttimes depresses the activity of enzymes, including catalase, amino levulinic acid synthetase, and P-450, enzymes involved in cellular respiration. The Krebs citric acid bike can be blocked by cobalt resulting in the inhibition of cellular free energy production. Cobalt tin replace zinc in a number of zinc-required enzymes such as alcohol dehydrogenase. Cobalt can as well heighten the kinetics of some enzymes, such as heme oxidase in the liver. Cobalt interferes with and depresses iodine metabolism, resulting in reduced thyroid action. Reduced thyroid activity tin lead to goiter.

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