Abstract
Six chitinases (EC 3.2.1.14) were purified from salicylate‐treated leek (Allium porrum L.). They all strongly bind to chitin and can roughly be divided into two groups. One group has blocked N‐termini, is completely inhibited by 1 mM AgNO3, has a relatively narrow pH optimum, a temperature optimum of 40°C and cannot degrade the tetramer of chitin. The other group has unblocked N‐termini showing homology to the chitin‐binding lectin WGA and is therefore considered as class I chitinases. This group is only moderately inhibited by 1 mM AgNO3 (30%), has a relatively broad pH optimum, has a higher temperature optimum (50 to 60°C) and can degrade the tetramer of chitin to dimers. Furthermore, all isoforms have molecular masses around 34 kDa as estimated by SDS‐PAGE. They have isoelectric points ranging from 4 to 8 and no detectable lysozyme activity. Two isoforms investigated in more detail differ in their antifungal potential.
Dates
Type | When |
---|---|
Created | 22 years, 5 months ago (March 12, 2003, 1:23 p.m.) |
Deposited | 1 year, 10 months ago (Oct. 28, 2023, 3:44 a.m.) |
Indexed | 1 year, 2 months ago (June 13, 2024, 1:14 p.m.) |
Issued | 26 years, 11 months ago (Oct. 1, 1998) |
Published | 26 years, 11 months ago (Oct. 1, 1998) |
Published Online | 23 years, 7 months ago (Jan. 17, 2002) |
Published Print | 26 years, 11 months ago (Oct. 1, 1998) |
@article{Vergauwen_1998, title={Purification and characterization of strongly chitin‐binding chitinases from salicylic acid‐treated leek (Allium porrum)}, volume={104}, ISSN={1399-3054}, url={http://dx.doi.org/10.1034/j.1399-3054.1998.1040205.x}, DOI={10.1034/j.1399-3054.1998.1040205.x}, number={2}, journal={Physiologia Plantarum}, publisher={Wiley}, author={Vergauwen, Rudy and Van Leuven, Fred and Van Laere, André}, year={1998}, month=oct, pages={175–182} }