Results 131 to 140 of about 2,670 (168)

Pectinesterase in New Zealand grapefruit juice

Journal of the Science of Food and Agriculture, 1976
AbstractSamples of juice from both early and later season New Zealand grapefruit have been analysed for the presence of three enzymes that have been reported in some overseas citrus varieties. While both early and late season juice contained pectinesterase, neither polygalacturonase nor ascorbic acid oxidase was detected in juice extracted from early ...
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Capillary Electrophoresis Analysis of Orange Juice Pectinesterases

Journal of Agricultural and Food Chemistry, 2000
Pectinesterase (PE) was extracted from orange juice and pulp with 1 M NaCl, desalted, and separated using capillary electrophoresis (CE) gel procedures (CE-SDS-CGE) and isoelectric focusing (CE-IEF). PE resolved as a single peak using noncoated fused silica columns with CE-SDS-CGE.
R J, Braddock, C R, Bryan, J K, Burns
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The Pectinesterase of the Pulp of the Banana Fruit.

Australian Journal of Plant Physiology, 1976
The pectinesterase (pectin pectyl-hydrolase, EC 3.1.1.11) of the pulp of the banana fruit is completely solubilized by buffers containing 0.5M sodium acetate, and the activity of the enzyme in the pulp remains constant during ripening. An apparent change in the ease of extraction as ripening progresses may be artefactual.
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Purification and properties of two pectinesterases from tomatoes

Phytochemistry, 1992
Pectinesterase is present in green tomato fruit and increases several-fold during ripening. Several isoenzymes of pectinesterase are known to exist in tomatoes, but one isoenzyme predominates in the fruit of most cultivars. A few cherry tomato cultivars have been identified that contain low levels of this isoenzyme and much higher levels of another ...
R, Pressey, F M, Woods
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Kinetic Compensation and the Role of Cations in Pectinesterase Catalysis

Journal of Agricultural and Food Chemistry, 1999
The catalytic rate constant of thermostable pectinesterase (TS-PE) from Marsh grapefruit pulp was determined at pH 7 at temperatures between 25 and 60 degrees C. TS-PE activity was measured at NaCl concentrations of 0.05, 0.10, 0.15, and 0.20 M and at CaCl(2) concentrations of 0.005, 0.010, 0.015, and 0.020 M.
D, Sun, L, Wicker
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Effect of Temperature and/or Pressure on Tomato Pectinesterase Activity

Journal of Agricultural and Food Chemistry, 2000
The activity of tomato pectinesterase (PE) was studied as a function of pressure (0.1-900 MPa) and temperature (20-75 degrees C). Tomato PE was rather heat labile at atmospheric pressure (inactivation in the temperature domain 57-65 degrees C), but it was very pressure resistant.
I, Van Den Broeck, L R, Ludikhuyze, A M, Van Loey, M E, Hendrickx   +3 more
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Total and Thermostable Pectinesterases in Citrus Juices

Journal of Food Science, 1996
ABSTRACT Grapefruits, tangerines and several orange cultivars were evaluated for total and thermostable pectinesterase (TS‐PE) activity. Juices were extracted with a Fresh'n Squeeze TM Multi Fruit Juicer. Variation in total pectinesterase (PE) and TS‐PE was not significantly
R. SNIR, P.E. KOEHLER, K.A. SIMS, L. WICKER   +3 more
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Heat-inactivation of mango pectinesterase and polygalacturonase

Food Chemistry, 1995
Abstract The present work involves isolation of mango pectinesterase (PE) and polygalacturonase (PG), and investigating some of its characteristics, mainly with respect to heat-stability of the enzymes. Within a reaction time of 10 min, mango PE shows its maximal activity at pH 7.5 in a reaction mixture containing 1% citrus pectin and 0.1 or 0.2 m ...
Azza A.S. Labib, F.A. El-Ashwah, H.T. Omran, A. Askar   +3 more
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Partial purification and characterisation of potato pectinesterase

Food Chemistry, 1982
Abstract Pectinesterase (EC 3.1.1.11) was extracted from potato (Solanum tuberosum var. Russet Burbank) tissue and purified 9.6-fold by ammonium sulphate precipitation and chromatography on Sephadex G-100. The enzyme preparation thus obtained has a molecular weight of 25,000, an apparent Km of 0.09% for citrus pectin and a pH optimum of 7.5.
A. Puri, T. Solomos, A. Kramer
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PARTIAL PURIFICATION AND CHARACTERIZATION OF PEACH PECTINESTERASE

Journal of Food Biochemistry, 1991
Pectinesterase (EC 3.1.1.11) was extracted from peaches (Prunus persica) and partially purified by preparative free solution isoelectric focusing. On SDS-PAGE gels, protein bands at 36.3 and 33.9 kilodaltons represented the major bands; minor bands were observed at 108.4, 40.7, and 17.0 kilodaltons.
H. JAVERI, L. WICKER
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