Pectin lyase (PL) activity was assayed by conducting the enzymatic reaction carried out in the following conditions 40[degrees]C; 6pH; length of light is 1cm and optical density at 235nm.
Moreover, our main objective of this study was to produce pectin lyase (PL) and Polygalacturonase (PG) utilizing the cheap raw pectin substrates like fruit peels as a major carbon source.
Maximum Pectin lyase activity (PL) activity was observed in peptone (21.
There is no report on the production and partial purification of pectin lyase and polygalacturonase utilizing different fruit peels as substrate by Bacillus cereus so far, which has been confirmed by the analysis of 16SrRNA Sequencing.
Pectin from Orange peels gave enhanced pectin lyase and polygalacturonase production compared to other sources.
from soil samples of Damascus, and then focus on optimizing the production and enzymatic characterization of extracellular pectin lyase by Bacillus subtilis strain RSY7.
Secondary screening of pectin lyase producing Bacillus:
The pectin lyase activity was determined in the supernatants by performing the pectin lyase assay.
The activity of pectin lyase was spectrophotometrically evaluated on citrus pectin as substrate, by monitoring the increase in optical density at [lambda] = 232 nm due to liberation of 4,5 unsaturated galacturonide product from citrus pectin .
Interactions between serine acetyltransferase and O-acetylserine (thiol) lyase in higher plants.
Cysteine biosynthesis in Chlamydomonas reinhardtii Molecular cloning and regulation of O-acetylserine (thiol) lyase.
Spinach chloroplast O-acetylserine (thiol) lyase exhibits two catalytically non-equivalent pyridoxal-5'-phosphate containing active sites.