Pantaleoni Laura, Longoni Paolo, Ferroni Lorenzo, Baldisserotto Costanza, Leelavathi Sadhu, Reddy Vanga Siva, Pancaldi Simonetta, Cella Rino
Department of Biology and Biotechnology, University of Pavia, Via Ferrata 9, 27100, Pavia, Italy.
Protoplasma. 2014 May;251(3):639-48. doi: 10.1007/s00709-013-0564-1. Epub 2013 Oct 25.
The high cost of recombinant enzymes for the production of biofuel from ligno-cellulosic biomass is a crucial factor affecting the economic sustainability of the process. The use of plants as biofactories for the production of the suitable recombinant enzymes might be an alternative to microbial fermentation. In the case of enzyme accumulation in chloroplasts, it is fundamental to focus on the issue of full photosynthetic efficiency of transplastomic plants in the field where they might be exposed to abiotic stress such as high light intensity and high temperature. Xylanases (EC 3.2.1.8), a group of enzymes that hydrolyse linear polysaccharides of beta-1,4-xylan into xylose, find an application in the biofuel industry favouring biomass saccharification along with other cell-wall degrading enzymes. In the present study, we analysed how a high level of accumulation of a thermostable xylanase in tobacco chloroplasts does not impact on photosynthetic performance of transplastomic plants grown outdoors. The recombinant enzyme was found to be stable during plant development, ex planta and after long-term storage.
用于从木质纤维素生物质生产生物燃料的重组酶成本高昂，这是影响该过程经济可持续性的关键因素。利用植物作为生物工厂来生产合适的重组酶可能是微生物发酵的一种替代方法。就叶绿体中酶的积累而言，至关重要的是要关注转质体植物在田间的光合效率问题，因为它们可能会受到高光强度和高温等非生物胁迫。木聚糖酶（EC 3.2.1.8）是一类将β-1,4-木聚糖的线性多糖水解为木糖的酶，与其他细胞壁降解酶一起，在有利于生物质糖化的生物燃料工业中得到应用。在本研究中，我们分析了烟草叶绿体中高水平积累的热稳定木聚糖酶如何不影响在户外生长的转质体植物的光合性能。发现该重组酶在植物发育过程中、离体后以及长期储存后都很稳定。
