OBJECTIVETo study the effect of light intensity on physiological and biochemical characteristics of Chrysanthemum morifolium at the vegetative stage.

METHODThe dynamic response of physiological and biochemical indexes of Ch. morifolium were measured under different treatments (100%, 80%, 60%, 40% and 20% of the full sunlight) at the vegetative stage.

RESULTThe physiological and biochemical indexes of Ch. morifolium showed dynamic changes with the progress of growth and the increase of the treatment time. The soluble sugar content decreased when the light intensity reduced, and had a significant positive correlation with the light intensity. Soluble protein content rose firstly and fell later, malondialdehyde content increased, superoxide dismutase and catalase activity decreased initially and increased afterwards.

CONCLUSIONProper shading benefits the nitrogen accumulation of Ch. morifolium at the vegetative stage, and reduces the strength of stress condition. The suitable light environment for growth of Ch. morifolium at the vegetative stage is about 80%-60% of full sunlight and the optimum treatment time is 20-40 days.

Catalase ; metabolism ; Chrysanthemum ; physiology ; Light ; Lipid Peroxidation ; Superoxide Dismutase ; metabolism

Catalases are well studied enzymes that play critical roles in protecting cells against the toxic effects of hydrogen peroxide. The ubiquity of the enzyme and the availability of substrates made heme catalases the focus of many biochemical and molecular biology studies over 100 years. In human, this has been implicated in various physiological and pathological conditions. Advancement in proteomics revealed many of novel and previously unknown features of this mysterious enzyme, but some functional aspects are yet to be explained. Along with discussion on future research area, this mini-review compile the information available on the structure, function and mechanism of action of human catalase.
Catalase ; chemistry ; metabolism ; physiology ; Heme ; chemistry ; Humans ; Hydrogen Peroxide ; metabolism

Catalase is widely used in the food, medical, and textile industries. It possesses exceptional properties including high catalytic efficiency, high specificity, and environmental friendliness. Free catalase cannot be recycled and reused in industry, resulting in a costly industrial biotransformation process if catalase is used as a core ingredient. Developing a simple, mild, cost-effective, and environmentally friendly approach to immobilize catalase is anticipated to improve its utilization efficiency and enzymatic performance. In this study, the catalase KatA derived from Bacillus subtilis 168 was expressed in Escherichia coli. Following separation and purification, the purified enzyme was prepared as an immobilized enzyme in the form of enzyme-inorganic hybrid nanoflowers, and the enzymatic properties were investigated. The results indicated that the purified KatA was obtained through a three-step procedure that included ethanol precipitation, DEAE anion exchange chromatography, and hydrophobic chromatography. Then, by optimizing the process parameters, a novel KatA/Ca₃(PO₄)₂ hybrid nanoflower was developed. The optimum reaction temperature of the free KatA was determined to be 35 ℃, the optimum reaction temperature of KatA/Ca₃(PO₄)₂ hybrid nanoflowers was 30-35 ℃, and the optimum reaction pH of both was 11.0. The free KatA and KatA/Ca₃(PO₄)₂ hybrid nanoflowers exhibited excellent stability at pH 4.0-11.0 and 25-50 ℃. The KatA/Ca₃(PO₄)₂ hybrid nanoflowers demonstrated increased storage stability than that of the free KatA, maintaining 82% of the original enzymatic activity after 14 d of storage at 4 ℃, whereas the free KatA has only 50% of the original enzymatic activity. In addition, after 5 catalytic reactions, the nanoflower still maintained 55% of its initial enzymatic activity, indicating that it has good operational stability. The K_m of the free KatA to the substrate hydrogen peroxide was (8.80±0.42) mmol/L, and the k_cat/K_m was (13 151.53± 299.19) L/(mmol·s). The K_m of the KatA/Ca₃(PO₄)₂ hybrid nanoflowers was (32.75±2.96) mmol/L, and the k_cat/K_m was (4 550.67±107.51) L/(mmol·s). Compared to the free KatA, the affinity of KatA/Ca₃(PO₄)₂ hybrid nanoflowers to the substrate hydrogen peroxide was decreased, and the catalytic efficiency was also decreased. In summary, this study developed KatA/Ca₃(PO₄)₂ hybrid nanoflowers using Ca²⁺ as a self-assembly inducer, which enhanced the enzymatic properties and will facilitate the environmentally friendly preparation and widespread application of immobilized catalase.
Catalase ; Nanostructures/chemistry* ; Hydrogen Peroxide/metabolism* ; Enzymes, Immobilized/chemistry* ; Catalysis

Fe (III) modified collagen fibers were used to immobilize catalase through the cross-linking of glutaraldehyde. The loading amount of catalase on the supporting matrix was 16.7 mg/g, and 35% enzymatic activity was remained. A series of experiments were conducted on free and immobilized catalase in order to investigate their optimal pH and temperature, and the thermal, storage and operation stability. Results suggest that the free and immobilized catalase prefer similar pH and temperature condition, which were pH 7.0 and 25 degrees C. It should be noted that the thermal stability of catalase was considerably improved after immobilization owing to the fact that the enzyme kept 30% of relative activity after incubation at 75 degrees C for 5 h. On the contrary, the free catalase was completely inactive. As for the storage stability, the immobilized catalase kept 88% of relative activity after stored at room temperature for 12 days while the free one was completely inactive under the same conditions. Moreover, the immobilized catalase preserved 57% of relative activity after being reused 26 times, exhibiting excellent operation stability. Consequently, this investigation suggests that collagen fiber can be used as excellent supporting matrix for the immobilization of catalase, and it is potential to be used for the immobilization of similar enzymes.
Catalase ; chemistry ; metabolism ; Collagen ; chemistry ; metabolism ; Enzymes, Immobilized ; chemistry ; metabolism ; Ferric Compounds ; chemistry

OBJECTIVETo study the growth state and physiological changes of Epimedium wushanense under different light conditions (100%, 80%, 60%, 40%, 20%), and investigate its adaptation mechanism to shade environment so that it can provide theoretical basis for cultivation and production.

METHODThe growth index, the content of photosynthetic pigments, proline content, MDA content, soluble sugar content, soluble protein content and antioxidant enzymy activity of E. wushanense under different shade conditions were measured.

RESULTExcept for length/width, the other form index of E. wushanense changed significantly. The E. wushanense grew well between light intensity 80%-40%, besides, the biomass above the earth was relatively high. The chlorophyll a, chlorophyll b, total chlorophyll content and carotenoids cotent were enhanced after shaded, the values of chlorophyll a\chlorophyll b increased between light intensity 100% -60% and reduced between light intensity 60% -20%. The proline and MDA content decreased after shading, the soluble sugar and soluble protein content increased respectively between light intensity 100% -60%, 100% -40% and reduced respectively between light intensity 60% -20%, 40% -20%. The SOD activity, CAT activity decreased after shading, and the POD activity, APX activity reduced between light intensity 60% -40%, raised under 20% treatment.

CONCLUSION80% 40% irradiance treatment was favorable to the growth of E. wushanense.

Catalase ; metabolism ; Epimedium ; chemistry ; physiology ; Light ; Peroxidase ; metabolism ; Superoxide Dismutase ; metabolism

OBJECTIVEThe studies were carried out on the physiologic characteristics of Panax notoginseng seeds during the after--ripening process in order to understand the seed's biochemical and physiological changes and lay the foundation for the germplasm conversation and breeding research of P. notoginseng seeds.

METHODDynamic changes of storage material contents, respiratory rate and protective enzymatic activity were determined by normal biochemical and physiological measuring methods.

RESULTThe respiratory rate increased continuously during the stratification process, the contents of starch, soluble protein, crude fat decreased and the content of water-soluble saccharide increased with the embryo development, activities of CAT, POD and SOD increased with the raise of MDA content.

CONCLUSIONP. notoginseng seed's biochemical and physiological changes interacted with its embryo morphological changes to complete its after-ripening development.

Catalase ; metabolism ; Oxygen Consumption ; Panax notoginseng ; chemistry ; physiology ; Seeds ; growth & development ; Superoxide Dismutase ; metabolism

OBJECTIVE: To observe the effect of astaxanthin (ASTA) on the activities of superoxide dismutase (SOD), catalase (CAT) and glutathione peroxidase (GSH-Px) in suspended leukocyte-depleted red blood cells stored for transfusion. METHODS: The suspended leukocyte-depleted red blood cells were randomly divided into group A, B, C and D. The ASTA was added into preservation solution of suspended leukocyte-depleted red blood cells of group B, C and D with the final concentration 5, 10 and 20 μmol/L, respectively, while DMSO was added into cells of group A in the same volume. After 7, 14, 28 and 42 days of storage, the reactive oxygen species (ROS) content in red blood cells was detected by fluorescence microplate reader, malondialdehyde (MDA) content was detected by thiobarbituric acid (TBA) method, activity of SOD was detected by xanthine oxidase method, the activity of CAT was detected by visible light method, and activity of GSH-Px was detected by colorimetry. RESULTS: After 7, 14, 28 and 42 days of storage, the contents of ROS and MDA in suspended red blood cells of group B, C and D were significantly lower(P<0.05), while the activities of SOD and GSH-Px were higher than those of group A(P<0.05); and CAT activity in cells treated by ASTA was significantly higher at 28 and 42 days of storage in comparison with that of group A(P<0.05). There were positive correlations between the ROS, MDA content in suspended red blood cells of group A, B, C, D and storage time(P<0.01), while negative correlation between SOD, CAT, GSH-Px activity and storage time(P<0.01). CONCLUSION ASTA can decrease the oxidative stress level and peroxide damage degree by increasing the antioxidant enzyme activities in suspended leukocyte-depleted red blood cells during storage.
Antioxidants ; Catalase/metabolism* ; Erythrocytes ; Leukocytes ; Oxidative Stress ; Superoxide Dismutase/metabolism* ; Xanthophylls

The well-known detrimental effects of cadmium (Cd) on plants are chloroplast destruction, photosynthetic pigment inhibition, imbalance of essential plant nutrients, and membrane damage. Jasmonic acid (JA) is an alleviator against different stresses such as salinity and drought. However, the functional attributes of JA in plants such as the interactive effects of JA application and Cd on rapeseed in response to heavy metal stress remain unclear. JA at 50 µmol/L was observed in literature to have senescence effects in plants. In the present study, 25 µmol/L JA is observed to be a "stress ameliorating molecule" by improving the tolerance of rapeseed plants to Cd toxicity. JA reduces the Cd uptake in the leaves, thereby reducing membrane damage and malondialdehyde content and increasing the essential nutrient uptake. Furthermore, JA shields the chloroplast against the damaging effects of Cd, thereby increasing gas exchange and photosynthetic pigments. Moreover, JA modulates the antioxidant enzyme activity to strengthen the internal defense system. Our results demonstrate the function of JA in alleviating Cd toxicity and its underlying mechanism. Moreover, JA attenuates the damage of Cd to plants. This study enriches our knowledge regarding the use of and protection provided by JA in Cd stress.
Brassica napus/metabolism* ; Cadmium/toxicity* ; Catalase/metabolism* ; Cyclopentanes/pharmacology* ; Oxylipins/pharmacology* ; Photosynthesis ; Plant Leaves/metabolism* ; Superoxide Dismutase/metabolism*

OBJECTIVETo construct the adenovirus vector containing recombinant human catalase (CAT) and to express the recombinant gene in vitro.

METHODSTotal RNA was extracted from human leukocytes and full-length human CAT cDNA was obtained with RT-PCR method. The CAT gene was cloned into pcDNA3.1(+) vector and pcDNA3.1(+)CAT was constructed. The positive clones were confirmed by the restriction enzyme digestion and gene sequencing. The CAT gene was cloned into the entry vector pENTR1A, and pENTR1A-CAT vector was constructed. By LR reaction pENTR1A-CAT and pAd/CMV/V5-DEST was recombined in vitro, and the recombinant adenovirus pAd/CMV/V5-DEST-CAT was obtained. The positive pAd/CMV/V5-DEST-CAT was confirmed by sequencing and transfected into 293A cells with Pac I linearization and Lipofectamine 2 000, and the recombinant virus particles were packaged and amplified in the cells. The expression of CAT protein and CAT enzyme activities of the recombinant virus were determined by Western blot and 240 nm UV absorption methods.

RESULTHigh expression of recombinant adenovirus was obtained and the expressed human catalase had high enzyme activity.

CONCLUSIONAd/CMV/V5-DEST-CAT vector containing human catalase gene has been constructed successfully; and the expressed enzyme in 293A cells has high activity.

Adenoviridae ; genetics ; Catalase ; genetics ; metabolism ; Cell Line ; Genetic Vectors ; Humans ; Transfection

The effect of growth and fermentation conditions on the production of catalase by T. aurantiacus WSH 03-01 was investigated in shaking flasks. Catalase activity reached 1594 u/mL when the culture was grown on a complex carbon source containing 20 g/L dextrin and 1% (V/V) ethanol, which was 23% higher than the sum produced on 20 g/L dextrin and 1% (V/V) ethanol, respectively. It was concluded that dextrin might act as a major carbon source in the complex, while ethanol was rather a stimulator than a carbon source. The stimulation effect of ethanol on catalase production was postulated to be two aspects; catalase-dependent alcohol metabolism is activated by acute alcohol, thus more catalase need to be synthesized for that use, named direct induction. As for indirect induction, which may result from little amount of H2O2 generation in process of NADH regeneration in respiratory chain. Peptone was shown to be a favorable nitrogen source for catalase production and its optimum concentration was found to be 10 g/L. Catalase production by T. aurantiacus WSH 03-01 was further improved by optimizing the initial pH, volume of medium in flasks as well as the concentration of external H2O2. Under the optimum culture conditions, the activity of catalase reached 2762 u/mL, which was nearly 6.8 times higher than that of the initiate conditions. Furthermore, the potential application of this novel catalase in the treatment of textile bleaching effluents was evaluated. Thermo-and alkaline stability of this catalase was compared with the commercial available catalases produced from bovine and Aspergillus niger. The crude enzyme from T. aurantiacus WSH 03-01 showed stronger stabilities at (70 degrees C, 80 degrees C, 90 degrees C) and (pH 9.0, pH 10.0, pH 11.0) than the other two types of catalases, indicating a great application potential in the clean production process of textile industry.
Catalase ; metabolism ; Culture Media ; Ethanol ; metabolism ; Fermentation ; Hot Temperature ; Hydrogen-Ion Concentration ; Peptones ; metabolism ; Textile Industry ; Thermoascus ; enzymology ; growth & development