scholarly journals Correlation of Pectolytic Enzyme Activity with the Programmed Release of Cells from Root Caps of Pea (Pisum sativum)

1990 ◽  
Vol 94 (4) ◽  
pp. 1855-1859 ◽  
Author(s):  
Martha C. Hawes ◽  
Hao-Jan Lin
1972 ◽  
Vol 18 (7) ◽  
pp. 1065-1072 ◽  
Author(s):  
Hassan A. Melouk ◽  
Chester E. Horner

Pectolytic enzyme activity of P. strasseri was highest in filtrates from cultures 5 and 23 days old, as determined by reducing-groups assay (RGA). Pectolytic enzyme activity, as determined by viscosity-reduction assay (VRA), was highest in cultures 7 days old. Macerating enzyme activities were highest in cultures 10 days old. Young peppermint-rhizome sections were more susceptible to maceration by P. strasseri filtrates than older sections. Colored phenolic compounds were released from macerated rhizomes and amounts released were correlated with degree of maceration.Differential inhibition of pectolytic enzyme activity (as judged by VRA and RGA assays) by a range of phenolic compounds suggests that at least two pectolytic enzymes capable of hydrolyzing α-1,4 linkages of pectic substances are produced by P. strasseri.Highest activities of pectolytic and macerating enzyme in extracts from diseased rhizomes were detected 5 days after inoculation with P. strasseri. Extracts from healthy rhizomes did not show pectolytic and macerating enzyme activity.Healthy peppermint-rhizome tissues had higher activities of polyphenoloxidase than diseased tissues; also, polyphenoloxidase activities in inoculated rhizomes decreased as time of incubation increased.


1963 ◽  
Vol 48 (4) ◽  
pp. 439-444 ◽  
Author(s):  
M. S. Nour El Dein ◽  
M. S. Sharkas

2011 ◽  
Vol 75 (1) ◽  
pp. 33-38 ◽  
Author(s):  
Marzena Sujkowska ◽  
Wojciech Borucki ◽  
Władysław Golinowski

Changes in the activity of acid phosphatase (AcPase) in the apoplast of pea root nodule were investigated. The activity was determined using lead and cerium methods. The results indicated a following sequence of AcPase activity appearance during the development of the infection thread: 1) low AcPase activity appears in the outer part of cells of symbiotic bacteria; 2) bacteria show increased AcPase activity, and the enzyme activity appears in the thread walls; 3) activity exhibits also matrix of the infection thread; 4) bacteria just before their release from the infection threads show high AcPase activity; 5) AcPase activity ceases after bacteria transformation into bacteroids. The increase in bacterial AcPase activity may reflect a higher demand for inorganic phosphorus necessary for propagation of the bacteria within the infection threads and/or involved in bacteria release from the infection threads.


2010 ◽  
Vol II (4) ◽  
pp. 109-114
Author(s):  
Margarita Kouzmanova ◽  
Milena Dimitrova ◽  
Daniela Dragolova ◽  
Gabriela Atanassova ◽  
Nikolai Atanassov

1996 ◽  
Vol 61 (2) ◽  
pp. 311-314 ◽  
Author(s):  
F. ARTÉS ◽  
A. CANO ◽  
J.P. FERNÁNDEZ-TRUJILLO

1979 ◽  
Vol 34 (9-10) ◽  
pp. 738-741 ◽  
Author(s):  
Josie L. Shute ◽  
Pablo S. Jourdan ◽  
Richard L. Mansell

Abstract From young, light-grown seedlings of Pisum sativum L. an enzyme activity catalyzing the glucosylation of kaempferol and quercetin in the 3-position to form the 3-O-triglucoside derivative has been demonstrated. The reaction proceeds from the aglycone via the mono-and diglucoside intermediates. The triglucoside can be produced from any of the less substituted derivatives with uridine diphosphate-D-glucose (UDPG) as the glucosyl donor. Young leaf tissues had much high­er levels of glucosyltransferase activity than the petioles and internodes. This is the first report of the synthesis of flavonol-3-0-triglucosides in vitro.


1969 ◽  
Vol 47 (6) ◽  
pp. 1007-1010 ◽  
Author(s):  
L. Van Den Berg ◽  
S. M. Yang

B. cinerea and S. sclerotiorum growing in a nutrient medium on the surface of carrots at 20 °C produced significantly more extracellular pectolytic enzymes when the carrots were exposed to 94–96% relative humidity than when exposed to 98–100% relative humidity. Tests in which these organisms were grown in a nutrient solution containing pectic substances showed that they produced pectolytic enzymes in significant quantities only when readily metabolizable sources of energy (e.g. ethanol, carbohydrates) were not available. These results suggest that the low relative humidity increased enzyme production by concentrating nutrients on the carrot surface to the point where they inhibited growth of the organisms and stimulated enzyme production. Tests also showed that pectolytic enzyme activity on the surface of unwashed carrots stored 9 months at 0–1 °C was substantially higher at 90–95% relative humidity than at 98–100% relative humidity. The results indicated that reduced decay at 98–100% relative humidity was largely due to lower pectolytic enzyme production.


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