Influence of Environmental Factors on Smallflower Morningglory (Jacquemontia tamnifolia) Germination and Growth

Weed Science ◽  
1987 ◽  
Vol 35 (4) ◽  
pp. 519-523 ◽  
Author(s):  
David R. Shaw ◽  
H. Randy Smith ◽  
A. Wayne Cole ◽  
Charles E. Snipes
Keyword(s):  
Environmental Factors ◽  
Optimum Temperature ◽  
Full Sunlight ◽  
Optimum Ph ◽  
Germination And Growth

The optimum pH for germination of smallflower morningglory (Jacquemontia tamnifolia(L.) Griseb. # IAQTA] seed was 8.0. A scarification time of 25 to 60 s using a drum scarifier with medium grit provided the best germination, and the optimum temperature for germination was 35 to 40C. However, the optimum temperature for growth was 25 to 35C, with reductions in growth occurring above or below this range. Emergence after 14 days was 81 and 49% at planting depths of 1.5 and 10 cm, respectively. Shade levels of 30 to 92% reduced smallflower morningglory growth by 38 to 87% compared to plants grown in full sunlight.

Environmental factors can affect the germination and growth of Parthenium hysterophorus and Rumex crispus

2019 ◽  
Vol 51 (6) ◽  
Author(s):  
Muhammad Azim Khan ◽  
Shaheen Kashmir ◽  
Hafiz Haider Ali ◽  
Bakhtiar Gul ◽  
Ali Raza ◽  
...  
Keyword(s):  
Environmental Factors ◽  
Parthenium Hysterophorus ◽  
Rumex Crispus ◽  
Germination And Growth

Immobilization and Characterization of Tannase and its Haze-removing

2009 ◽  
Vol 15 (6) ◽  
pp. 545-552 ◽  
Author(s):  
Erzheng Su ◽  
Tao Xia ◽  
Liping Gao ◽  
Qianying Dai ◽  
Zhengzhu Zhang
Keyword(s):  
Kinetic Parameter ◽  
High Activity ◽  
Green Tea ◽  
Storage Stability ◽  
Residual Activity ◽  
Black Tea ◽  
Optimum Temperature ◽  
Oolong Tea ◽  
Optimum Ph

Tannase was effectively immobilized on alginate by the method of crosslinking-entrapment-crosslinking with a high activity recovery of 76.6%. The properties of immobilized tannase were investigated. Its optimum temperature was determined to be 35 ° C, decreasing 10 °C compared with that of free enzyme, whereas the optimum pH of 5.0 did not change. The thermal and pH stabilities of immobilized tannase increased to some degree. The kinetic parameter, Km, for immobilized tannase was estimated to be 11.6 × 10-4 mol/L. Fe2+ and Mn2+ could activate the activity of immobilized tannase. The immobilized tannase was also applied to treat the tea beverage to investigate its haze-removing effect. The content of non-estern catechins in green tea, black tea and oolong tea increased by 52.17%, 12.94% and 8.83%, respectively. The content of estern catechins in green tea, oolong tea and black tea decreased by 20.0%, 16.68% and 5.04%, respectively. The anti-sediment effect of green tea infusion treated with immobilized tannase was significantly increased. The storage stability and reusability of the immobilized tannase were improved greatly, with 72.5% activity retention after stored for 42 days and 86.9% residual activity after repeatedly used for 30 times.

scholarly journals Properties of a new fungal b-galactosidase with potential application in the dairy industry

1999 ◽  
Vol 30 (3) ◽  
pp. 265-271 ◽  
Author(s):  
Rubens Cruz ◽  
Vinícius D'Arcádia Cruz ◽  
Juliana Gisele Belote ◽  
Marcelo de Oliveira Khenayfes ◽  
Claudia Dorta ◽  
...  
Keyword(s):  
Hydrolytic Activity ◽  
Industrial Applications ◽  
Transferase Activity ◽  
Optimum Temperature ◽  
Milk Whey ◽  
Beneficial Effects ◽  
Optimum Ph ◽  
Semi Solid ◽  
Good Productivity ◽  
Hydrolysis Of

<FONT FACE="Symbol">b</font>-Galactosidase or <FONT FACE="Symbol">b</font>-D-galactoside-galactohydrolase (EC. 3.2.1.23) is an important enzyme industrially used for the hydrolysis of lactose from milk and milk whey for several applications. Lately, the importance of this enzyme was enhanced by its galactosyltransferase activity, which is responsible for the synthesis of transgalactosylated oligosaccharides (TOS) that act as functional foods, with several beneficial effects on consumers. Penicillium simplicissimum, a strain isolated from soil, when grown in semi-solid medium showed good productivity of <FONT FACE="Symbol">b</font>-galactosidase with galactosyltransferase activity. The optimum pH for hydrolysis was in the 4.04.6 range and the optimum pH for galactosyltransferase activity was in the 6.07.0 range. The optimum temperature for hydrolysis and transferase activity was 55-60°C and 50°C, respectively, and the enzyme showed high thermostability for the hydrolytic activity. The enzyme showed a potential for several industrial applications such as removal of 67% of the lactose from milk and 84% of the lactose from milk whey when incubated at their original pH (4.5 and 6.34, respectively) under optimum temperature conditions. When incubated with a 40% lactose solution in 150 mM McIlvaine buffer, pH 4.5, at 55°C the enzyme converted 86.5% of the lactose to its component monosaccharides. When incubated with a 60% lactose solution in the same buffer but at pH 6.5 and 50°C, the enzyme can synthetize up to 30.5% TOS, with 39.5% lactose and 30% monosaccharides remaining in the preparation.

scholarly journals Characterization of Biosynthetic Enzymes for Ectoine as a Compatible Solute in a Moderately Halophilic Eubacterium, Halomonas elongata

1999 ◽  
Vol 181 (1) ◽  
pp. 91-99 ◽  
Author(s):  
Hisayo Ono ◽  
Kazuhisa Sawada ◽  
Nonpanga Khunajakr ◽  
Tao Tao ◽  
Mihoko Yamamoto ◽  
...  
Keyword(s):  
Molecular Mass ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Gel Filtration ◽  
Apparent Molecular Mass ◽  
Optimum Temperature ◽  
Sds Page ◽  
Halomonas Elongata ◽  
Optimum Ph

ABSTRACT 1,4,5,6-Tetrahydro-2-methyl-4-pyrimidinecarboxylic acid (ectoine) is an excellent osmoprotectant. The biosynthetic pathway of ectoine from aspartic β-semialdehyde (ASA), in Halomonas elongata, was elucidated by purification and characterization of each enzyme involved. 2,4-Diaminobutyrate (DABA) aminotransferase catalyzed reversively the first step of the pathway, conversion of ASA to DABA by transamination with l-glutamate. This enzyme required pyridoxal 5′-phosphate and potassium ions for its activity and stability. The gel filtration estimated an apparent molecular mass of 260 kDa, whereas molecular mass measured by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) was 44 kDa. This enzyme exhibited an optimum pH of 8.6 and an optimum temperature of 25°C and had Km s of 9.1 mM forl-glutamate and 4.5 mM for dl-ASA. DABA acetyltransferase catalyzed acetylation of DABA to γ-N-acetyl-α,γ-diaminobutyric acid (ADABA) with acetyl coenzyme A and exhibited an optimum pH of 8.2 and an optimum temperature of 20°C in the presence of 0.4 M NaCl. The molecular mass was 45 kDa by gel filtration. Ectoine synthase catalyzed circularization of ADABA to ectoine and exhibited an optimum pH of 8.5 to 9.0 and an optimum temperature of 15°C in the presence of 0.5 M NaCl. This enzyme had an apparent molecular mass of 19 kDa by SDS-PAGE and a Km of 8.4 mM in the presence of 0.77 M NaCl. DABA acetyltransferase and ectoine synthase were stabilized in the presence of NaCl (>2 M) and DABA (100 mM) at temperatures below 30°C.

scholarly journals Immobilization of Isolated Lipase From Moldy Copra(Aspergillus Oryzae)

2011 ◽  
Vol 8 (2) ◽  
pp. 896-902
Author(s):  
Seniwati Dali ◽  
A. B. D. Rauf Patong ◽  
M. Noor Jalaluddin ◽  
Pirman ◽  
Baharuddin Hamzah
Keyword(s):  
Thermal Stability ◽  
Aspergillus Oryzae ◽  
Immobilized Lipase ◽  
Optimum Temperature ◽  
Adsorption Method ◽  
Ph Optimum ◽  
Optimum Ph ◽  
Recovery Technique ◽  
Free Lipase

Enzyme immobilization is a recovery technique that has been studied in several years, using support as a media to help enzyme dissolutions to the reaction substrate. Immobilization method used in this study was adsorption method, using specific lipase fromAspergillus oryzae. Lipase was partially purified from the culture supernatant ofAspergillus oryzae. Enzyme was immobilized by adsorbed on silica gel. Studies on free and immobilized lipase systems for determination of optimum pH, optimum temperature, thermal stability and reusability were carried out. The results showed that free lipase had optimum pH 8,2 and optimum temperature 35 °C while the immobilized lipase had optimum 8,2 and optimum temperature 45 °C. The thermal stability of the immobilized lipase, relative to that of the free lipase, was markedly increased. The immobilized lipase can be reused for at least six times.

scholarly journals Preparation of Cross-Linked Enzyme Aggregates (CLEAs) of an Inulosucrase Mutant for the Enzymatic Synthesis of Inulin-Type Fructooligosaccharides

Catalysts ◽  
2019 ◽  
Vol 9 (8) ◽  
pp. 641 ◽  
Author(s):  
Thanapon Charoenwongpaiboon ◽  
Rath Pichyangkura ◽  
Robert A. Field ◽  
Manchumas Hengsakul Prousoontorn
Keyword(s):  
Enzymatic Synthesis ◽  
Biochemical Characterization ◽  
Lactobacillus Reuteri ◽  
Soluble Enzyme ◽  
Optimum Temperature ◽  
Optimum Conditions ◽  
Product Specificity ◽  
Product Characterization ◽  
Optimum Ph ◽  
Probiotic Activity

Fructooligosaccharides are well-known carbohydrate molecules that exhibit good probiotic activity and are widely used as sweeteners. Inulin-type fructooligosaccharides (IFOs) can be synthesized from sucrose using inulosucrase. In this study, cross-linked enzyme aggregates (CLEAs) of Lactobacillus reuteri 121 inulosucrase (R483A-LrInu) were prepared and used as a biocatalyst for IFOs production. Under optimum conditions, R483A-LrInu CLEAs retained 42% of original inulosucrase activity. Biochemical characterization demonstrated that the optimum pH of inulosucrase changed from 5 to 4 after immobilization, while the optimum temperature was unchanged. Furthermore, the pH stability and thermostability of the R483A-LrInu CLEAs was significantly improved. IFOs product characterization indicated that the product specificity of the enzyme was impacted by CLEA generation, producing a narrower range of IFOs than the soluble enzyme. In addition, the R483A-LrInu CLEAs showed operational stability in the batch synthesis of IFOs.

KINETIC STUDIES ON ACID PHOSPHATASE IN TRIBOLIUM CONFUSUM DUVAL

1964 ◽  
Vol 42 (12) ◽  
pp. 1769-1775 ◽  
Author(s):  
K. D. Chaudhary ◽  
S. Moorjani ◽  
A. Lemonde
Keyword(s):  
Kinetic Studies ◽  
Final Concentration ◽  
Tribolium Confusum ◽  
Metallic Ions ◽  
Optimal Conditions ◽  
Optimum Temperature ◽  
Apparent Effect ◽  
Michaelis Constant ◽  
Optimum Ph ◽  
Zero Order Reaction

The biochemical characteristics of acid phosphomonoesterase in Tribolium confusum homogenate have been determined. Zero-order reaction occurs for 30 minutes, with 10−3 M final concentration of phenyl phosphate at an optimum pH of 6.4. Michaelis constant (Km) under the optimal conditions is 6.34 × 10−3 M. Maximum enzyme activity is obtained at 40 °C, and the activation energy (ΔE) is 13,000 cal/mole, within the limits of optimum temperature. Inorganic phosphate inhibits competitively and Ki value is 3.45 × 10−3 M. Partial inhibition by fluoride is shown. Apparent effect of metallic ions also has been demonstrated.Comparison of these results with those reported in the literature for several other species of insects, as well as with those in certain mammalian systems, has been discussed.

scholarly journals NANOPARTICLE BASED BIOSENSOR FOR PENICILLIN QUANTIFICATION IN PHARMACEUTICALS

2019 ◽  
pp. 102-107
Author(s):  
EMINE KARAKUS ◽  
CISEM TURAN
Keyword(s):  
Response Time ◽  
Zno Nanoparticles ◽  
Pharmaceutical Preparation ◽  
Zno Nanorods ◽  
Zno Nanorod ◽  
Buffer Concentration ◽  
Optimum Temperature ◽  
Short Response Time ◽  
Biosensor System ◽  
Optimum Ph

Objective: The objective of this study was to develop a new biosensor system based on nanoparticle to determine penicillin in pharmaceuticals. Methods: The characterization and optimization of the potentiometric penicillin biosensor (PB) were prepared by using synthesized surface-dependent and surface-independent ZnO nanoparticles named ZnO nanorods and chitosan were carried out. It was preferred ZnO nanorod because of its electrical, optical, physical and photocatalyst properties, biocompatibility and non-toxicity in the construction of the penicillin biosensor. Results: The operating range was obtained as 10-1-10-3M, the optimum buffer concentration was 10 mmol, optimum pH was 7.4 and the optimum temperature was 25 °C for the PB. The PB has advantages in terms of short response time, long enough shelf life, cheap, and easy elaborate. Conclusion: Whether the biosensor can be used to determine penicillin and accurately measure penicillin, the amount of penicillin in a commercial pharmaceutical preparation named Alfoxil was successfully made by using our prepared penicillin biosensor.

scholarly journals Arsenite-Oxidizing Hydrogenobaculum Strain Isolated from an Acid-Sulfate-Chloride Geothermal Spring in Yellowstone National Park

2004 ◽  
Vol 70 (3) ◽  
pp. 1865-1868 ◽  
Author(s):  
Jessica Donahoe-Christiansen ◽  
Seth D'Imperio ◽  
Colin R. Jackson ◽  
William P. Inskeep ◽  
Timothy R. McDermott
Keyword(s):  
Yellowstone National Park ◽  
National Park ◽  
Microbial Populations ◽  
Optimum Temperature ◽  
Arsenite Oxidation ◽  
Geothermal Spring ◽  
Saturation Kinetics ◽  
Optimum Ph ◽  
Obligate Chemolithoautotroph ◽  
Sole Energy

ABSTRACT An arsenite-oxidizing Hydrogenobaculum strain was isolated from a geothermal spring in Yellowstone National Park, Wyo., that was previously shown to contain microbial populations engaged in arsenite oxidation. The isolate was sensitive to both arsenite and arsenate and behaved as an obligate chemolithoautotroph that used H2 as its sole energy source and had an optimum temperature of 55 to 60�C and an optimum pH of 3.0. The arsenite oxidation in this organism displayed saturation kinetics and was strongly inhibited by H2S.

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