A biochemical study of Pseudomonas prunicola Wormald. 1. Pectin esterase.
نویسنده
چکیده
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منابع مشابه
The measurement of the cytochrome oxidase activity of enzyme preparations.
containing 1 ml. 15 % glycerol solution, 1-0 ml. 0-1 M-sodium acetate, 0-5 ml. 0-3 M-bicarbonate solution and 0 5 ml. of the enzyme solution. Occurrence of the back reaction would have given rise to an uptake of C02 from the system, but in fact no such uptake was observed. Under these conditions, therefore, no back reaction takes place, so that the incompleteness ofthe de-esterification cannot ...
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It was reported by Beavan & Brown (1949) that cultures of By8aochlamy8 fulva Olliver & Smith produced protopectinase, but neither polygalacturonase nor pectin esterase; they concluded that B. fulva produced a disaggregating enzyme, which lowered the viscosity ofpectin solutions, without the formation of free reducing groups. A re-investigation of the problem has been made, and in a preliminary ...
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Background: Pectinases are pectin degrading class of enzymes including polygalacturonase (PG), polymethyl galacturonase (PMG), pectate lyase (PEL), and pectin esterase (PE) that are commonly used in processes involving the degradation of plant materials, such as speeding up the extraction of fruit juices. Objectives: A highly methylated pectin degrading bacterium from soil covered with fruit wa...
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A large number of bacteria and fungi secrete extracellularly the enzyme complex often termed 'pectinase', which causes the rapid disintegration of plant tissue and is consideredtheprimaryinstrument of the attack on plant tissues by these microorganisms. The action of pectinase on a solution of pectin results in the following changes: (a) a rapid lowering of the viscosity of the solution; (b) a ...
متن کاملCholinesterases from plant tissue: v. Cholinesterase is not pectin esterase.
Several properties of the cholinesterase from Phaseolus aureus Roxb. and of pectin (methyl) esterases from both Phaseolus aureus and Lycopersicon esculentum (L.) Mill. are contrasted. Cholinesterase activity is inhibited by all of the concentrations of NaCl tested, from 0.05 m to 0.9 m, a property which differs sharply from published data pertaining to pectin esterase. Although crude preparatio...
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ورودعنوان ژورنال:
- The Biochemical journal
دوره 44 3 شماره
صفحات -
تاریخ انتشار 1949