Selective and Sensitive Detection of Pectin Lyase Activity Using a Colorimetric Test: Application to the Screening of Microorganisms Possessing Pectin Lyase Activity

2001 ◽  
Vol 291 (2) ◽  
pp. 290-296 ◽  
Author(s):  
Mustapha Nedjma ◽  
Norbert Hoffmann ◽  
Abdel Belarbi
Keyword(s):  
Pectin Lyase ◽  
Sensitive Detection ◽  
Colorimetric Test ◽  
Test Application ◽  
Lyase Activity

Production and Thermal Characterization of an Alkaline Pectin Lyase from Penicillium notatum

2015 ◽  
Vol 11 (4) ◽  
pp. 517-525 ◽  
Author(s):  
Umme Habibah Siddiqua ◽  
Haq Nawaz Bhatti ◽  
Shazia Nouren ◽  
Saima Noreen ◽  
Ismat Bibi
Keyword(s):  
Ammonium Sulphate ◽  
Thermal Inactivation ◽  
Thermal Characterization ◽  
Maximal Activity ◽  
Inhibitory Effect ◽  
Pectin Lyase ◽  
Partial Purification ◽  
Penicillium Notatum ◽  
Enhanced Production ◽  
Lyase Activity

Abstract The present study was aimed to investigate the potential of Penicillium notatum for the production of pectin lyase under solid state culture using wheat bran as substrate. Different process parameters were optimized using completely randomized design for enhanced production of the pectin lyase. P. notatum showed maximum production (1875 U/gds) of pectin lyase with substrate amount 15 g/250 ml, moisture level 60%, pH 6, incubation period 120 h at 30°C. Pectin lyase activity was further improved with the addition of maltose and ammonium sulphate as carbon and nitrogen additives (1%), respectively. Partial purification of enzyme was carried out by ammonium sulphate precipitation at 80% saturation level. The P. notatum pectin lyase showed maximal activity at 65°C and pH 8. Km and Vmax values were 0.29% and 0.487 µmol/min, respectively. Energy of activation was found to be 5.33 kJ/mol. A detailed kinetic study of thermal inactivation was carried out. The results showed that pectin lyase exhibited resistance against thermal unfolding. Effect of various metals on pectin lyase activity was also investigated. All the metals showed inhibitory effect on the enzyme activity. The present investigation revealed that pectin lyase isolated from P. notatum is thermally stable and alkaline in nature.

Pectin Lyase Activity in Culture Medium of Lasidioplodia theobromae

2007 ◽  
Vol 2 (3) ◽  
pp. 334-340 ◽  
Author(s):  
A.O. Adejuwon ◽  
P.O. Olutiola .
Keyword(s):  
Culture Medium ◽  
Pectin Lyase ◽  
Lyase Activity

Evidence against involvement of pectic enzymes in the invasion of root hairs by Rhizobium trifolii

1969 ◽  
Vol 15 (6) ◽  
pp. 643-645 ◽  
Author(s):  
James D. Macmillan ◽  
Roderic C. Cooke
Keyword(s):  
Root Hairs ◽  
Red Clover ◽  
Infection Process ◽  
Pectin Lyase ◽  
Rhizobium Trifolii ◽  
Leguminous Plants ◽  
Pectic Enzymes ◽  
Lyase Activity ◽  
Rhizobium Spp ◽  
Polygalacturonate Lyase

It has been postulated that polygalacturonase is significant in the infection of root hairs of leguminous plants by Rhizobium spp. Recently this theory has been strongly questioned. Evidence for polygalacturonase was based on methods which would not distinguish between this enzyme and other pectic glycosidases. The possibility that pectin lyase or polygalacturonate lyase is involved in the invasion of red clover by Rhizobium trifolii was investigated. Weak pectin lyase activity was detected in uninoculated seedlings, but no increase in the activity was produced in inoculated seedlings. It was concluded that neither of the lyases has significance in the infection process.

Characteristics of the immobilized pectin lyase activity from a commercial pectolytic enzyme preparation

1990 ◽  
Vol 10 (6) ◽  
pp. 531-539 ◽  
Author(s):  
P. Lozano ◽  
A. Manjón ◽  
J. L. Iborra ◽  
D. M. Gálvez
Keyword(s):  
Enzyme Preparation ◽  
Pectin Lyase ◽  
Lyase Activity ◽  
Pectolytic Enzyme

scholarly journals An insight into the sequential changes in enzymatic activities during retting of jute (Corchorus spp. L.).

2021 ◽  
Vol 42 (3) ◽  
pp. 636-643
Author(s):  
B. Majumdar ◽  
◽  
A.R. Saha ◽  
S. Sarkar ◽  
S.K. Sarkar ◽  
...  
Keyword(s):  
Water Samples ◽  
Large Scale ◽  
Microbial Consortium ◽  
Standard Procedure ◽  
Sharp Decrease ◽  
Quality Parameters ◽  
Enzymatic Activities ◽  
Pectin Lyase ◽  
Lyase Activity ◽  
Last Stage

Aim: To study the dynamics of enzymes involved in biochemical process of jute (Corchorus spp.) retting with and without microbial retting consortium. Methodology: Two large scale retting trials were conducted with and without microbial retting consortium in triplicate. The retting water samples were collected every day at 24 hrs interval from both the trials. Polygalcturonase (PG), pectin lyase (PNL) and xylanase activities along with the pH were measured from the collected retting water samples following standard procedure. Fibre quality parameters were also studied from the resultant fibre obtained from both the retting trials. Results: There was a sharp decrease in pH of retting liquor by 1.35 units and that of pectin lyase activity by 97.9 Uml-1 within 24 hrs of inoculation of microbial retting consortium. Thereafter, higher pectin lyase (123.1 Uml-1), polygalacturonase (3.56 Iuml-1) and xylanase (0.818 IUml-1) activities were recorded during middle stage of retting. The enzyme activities were lower and non-significant at last stage of retting (11-14 days). The completion of retting without microbial consortium took longer time due to lower enzymatic activities as compared to microbial consortium mediated retting. Interpretation: The PG, PNL and xylanase enzymes released by the microbial consortium during retting of jute helped in faster biodegradation of pectin and xylan compared to control retting. Hence, the pre retting treatment of jute with microbial consortium is suggested for quick retting.

scholarly journals Pectin Lyase Activity in a Penicillium italicum Strain

1990 ◽  
Vol 56 (12) ◽  
pp. 3755-3759 ◽  
Author(s):  
Aitor Alaña ◽  
Itziar Alkorta ◽  
Juan B. Domínguez ◽  
Maria J. Llama ◽  
Juan L. Serra
Keyword(s):  
Pectin Lyase ◽  
Penicillium Italicum ◽  
Lyase Activity

Multiple forms of pectic lyases and polygalacturonase from Fusarium oxysporum f,.sp. radicis lycopersici: regulation of their synthesis by galacturonic acid

1997 ◽  
Vol 43 (3) ◽  
pp. 245-253 ◽  
Author(s):  
M. A. Guevara ◽  
P. Estévez ◽  
M. T. González-Jaén
Keyword(s):  
Fusarium Oxysporum ◽  
Galacturonic Acid ◽  
Pectate Lyase ◽  
Pectin Lyase ◽  
Multiple Forms ◽  
Pectic Enzymes ◽  
Weak Preference ◽  
Absolute Requirement ◽  
Lyase Activity ◽  
Polygalacturonase Activity

The r2 isolate of Fusarium oxysporum f.sp. radicis-lycopersici produced several pectic enzymes that differ in substrate preference, reaction mechanism, and action pattern. We detected three forms that have lyase activity, four forms with polygalacturonase activity and one form with pectinesterase activity. Lyases had an absolute requirement for calcium and pIs of 9.20, 9.00, and 8.65. The two more alkaline forms had a weak preference for pectin, whereas the other was more active on polygalacturonate. Polygalacturonases had pIs of 9.30, 7.35, 6.85, and 6.55 and were inhibited by calcium ions. Lyases and polygalacturonases were induced by galacturonic acid and were subject to catabolite repression. Induced synthesis occurred at pHs 5.5 and 8.0 and no increase in lyase activities were promoted by alkalinization of cultures. Pectin lyase had an endo mode of action, whereas pectate lyase and polygalacturonase behaved more as exoenzymes. These results are discussed in relation to the appearance of the different pectic enzymes when the fungus is confronted with a pectic polymer.Key words: Fusarium oxysporum f.sp. radicis-lycopersici, Lycopersicon esculentum, pectate lyase, pectin lyase, polygalacturonase.

Comparison of fungal growth and production of extracellular pectin lyase activity by pathogenic and non-pathogenic races of Colletotrichum lindemuthianum cultivated under different conditions

2007 ◽  
Vol 70 (1-3) ◽  
pp. 88-95 ◽  
Author(s):  
Lorena Hernández-Silva ◽  
Carlos Piñón-Escobedo ◽  
Horacio Cano-Camacho ◽  
Ma. Guadalupe Zavala-Páramo ◽  
Ismael Acosta-Rodríguez ◽  
...  
Keyword(s):  
Fungal Growth ◽  
Pectin Lyase ◽  
Colletotrichum Lindemuthianum ◽  
Lyase Activity ◽  
Pathogenic Races
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