| Literature DB >> 12232066 |
J. P. Vincken1, G. Beldman, AGJ. Voragen.
Abstract
Two endoglucanases of Trichoderma viride, endoI and endoIV, were assayed for their activity toward alkali-extracted apple xyloglucans. EndoIV was shown to have a 60-fold higher activity toward xyloglucan than endoI, whereas carboxymethyl cellulose and crystalline cellulose were better substrates for the latter. The enzymic degradation of cellulose embedded in the complex cell-wall matrix of apple fruit tissue has been studied using cellobiohydrolase (CBH) and these two different endoglucanases. A high-performance liquid chromatographic method (Aminex HPX-22H) was used to monitor the release of cellobiose and oligomeric xyloglucan fragments. Synergistic action between CBH and endoglucanases on cell-wall-embedded cellulose was, with respect to their optimal ratio, slightly different from that reported for crystalline cellulose. The combination of endoIV and CBH solubilized twice as much cellobiose compared to a combination of endoI and CBH. Apparently, the concomitant removal of the xyloglucan coating from cellulose microfibrils by endoIV is essential for an efficient degradation of cellulose in a complex matrix. Cellulose degradation slightly enhanced the solubilization of xyloglucans. These results indicate optimal degradation of cell-wall-embedded cellulose by a three-enzyme system consisting of an endoglucanase with high affinity toward cellulose (endoI), a xyloglucanase (endoIV), and CBH.Entities:
Year: 1994 PMID: 12232066 PMCID: PMC159167 DOI: 10.1104/pp.104.1.99
Source DB: PubMed Journal: Plant Physiol ISSN: 0032-0889 Impact factor: 8.340