Screening and Optimization of Pectin Lyase and Polygalacturonase Activity from Ginseng Pathogen Cylindrocarpon Destructans.
Enzymatic clarification of fruit juices by fungal pectin lyase.
et al Purification and characterization of a new bioscouring pectate lyase from Bacillus pumilus BK2.
Effect of nitrogen sources on Pectin lyase activity
0) and temperature (30, 35, 40, 45, 50 and 55[degrees]C) were optimized for maximal pectin lyase production by culturing the bacteria in 250 ml Erlenmeyer flasks containing 50 ml of sterile production medium, and incubated in rotary shaker (150 rpm).
The pH and temperature dependant activity of crude pectin lyase was determined by carrying out the standard assay as described above.
Pectin lyase has biotechnological potential in fruit juice industries due to the fact that it degrades pectin without disturbing the ester group which is responsible for specific aroma of the juice and also it does not lead to methanol formation which is toxic .
These 7 isolates (RSY1, RSY5, RSY7, RSY10, RSY11, RSY13 and RSY15) were subjected to secondary screening for pectin lyase (PL) production using submerged fermentation.
In submerged fermentation, the production of pectin lyase was reached maximum activity of 1.
Several experiments were carried out at different temperatures (30[degrees]C, 35[degrees]C, 37[degrees]C, 40[degrees]C, 45[degrees]C, 50[degrees]C and 55[degrees]C) to study the effect of incubation temperature on pectin lyase production by strain RSY7.
The determination of the optimal pH and temperature of the crude enzymatic extracts obtained by submerged fermentation was carried out using the standard pectin lyase assay.
In order to determine the effect of temperature, the pectin lyase activity was performed at optimum pH of 8.