Acyltransferases Regulate Oil Quality inCamelina sativaThrough Both Acyl Donor and Acyl Acceptor Specificities
FRONTIERS IN PLANT SCIENCE
Authors: Lager, Ida; Jeppson, Simon; Gippert, Anna-Lena; Feussner, Ivo; Stymne, Sten; Marmon, Sofia
Abstract
Camelina sativais an emerging biotechnology oil crop. However, more information is needed regarding its innate lipid enzyme specificities. We have therefore characterized several triacylglycerol (TAG) producing enzymes by measuringin vitrosubstrate specificities using different combinations of acyl-acceptors (diacylglycerol, DAG) and donors. Specifically,C. sativaacyl-CoA:diacylglycerol acyltransferase (DGAT) 1 and 2 (which both use acyl-CoA as acyl donor) and phospholipid:diacylglycerol acyltransferase (PDAT, with phosphatidylcoline as acyl donor) were studied. The results show that the DGAT1 and DGAT2 specificities are complementary, with DGAT2 exhibiting a high specificity for acyl acceptors containing only polyunsaturated fatty acids (FAs), whereas DGAT1 prefers acyl donors with saturated and monounsaturated FAs. Furthermore, the combination of substrates that resulted in the highest activity for DGAT2, but very low activity for DGAT1, corresponds to TAG species previously shown to increase inC. sativaseeds with downregulated DGAT1. Similarly, the combinations of substrates that gave the highest PDAT1 activity were also those that produce the two TAG species (54:7 and 54:8 TAG) with the highest increase in PDAT overexpressingC. sativaseeds. Thus, thein vitrodata correlate well with the changes in the overall fatty acid profile and TAG species inC. sativaseeds with altered DGAT1 and PDAT activity. Additionally,in vitrostudies ofC. sativaphosphatidycholine:diacylglycerol cholinephosphotransferase (PDCT), another activity involved in TAG biosynthesis, revealed that PDCT accepts substrates with different desaturation levels. Furthermore, PDCT was unable to use DAG with ricineoleyl groups, and the presence of this substrate also inhibited PDCT from using other DAG-moieties. This gives insights relating to previousin vivostudies regarding this enzyme.
Asymmetric porous cordierite ceramic membranes prepared by phase inversion tape casting and their desalination performance
CERAMICS INTERNATIONAL
Authors: Teng, Huai-De; Wei, Qi; Wang, Ya-Li; Cui, Su-Ping; Li, Qun-Yan; Nie, Zuo-Ren
Abstract
Asymmetric porous cordierite ceramic membranes were fabricated by phase inversion tape casting method. It is shown that the membranes consist of a relatively dense skin layer on the top, a sponge layer at the bottom and a finger-like layer in the middle. The membranes have a hierarchical pore structure, where macrovoids (denoted as dozens-micron-sized (DMS) pores) are present in the finger-like layer and micron-sized (MS) pores are located in the skin layer, sponge layer and the wall of macrovoids. After surface silylation by post-grafting with 1H,1H,2H,2H-perfluorodecyltriethoxysilane (FAS), the sample with a starting powder/polyethersulfone (PESf) weight ratio of 9 (M - 4) becomes hydrophobic, with a water contact angle of 150 degrees. At a NaCl concentration of 3.5 wt%, a feed rate of 18L/h and a feed temperature of 80 degrees C, the hydrophobic M - 4 membrane exhibits a water permeate flux of 22.33 kg/m(2)h, which is considerably larger than that of the membranes prepared by dry pressing method previously, and a salt rejection of 99.9%. The higher water permeate flux is attributed to the much lower transport resistance of water vapor in the membranes of the present work.