Application of Remote Sensing Techniques for Appraising Changes in Wildlife Habitat

An attempt was made to investigate the potential of airborne, multispectral, line scanner data acquisition and computer-implemented automatic recognition techniques for providing useful information about waterfowl breeding habitat in North Dakota. The spectral characteristics of the components of a landscape containing waterfowl habitat can be detected with airborne scanners. By analyzing these spectral characteristics it is possible to identify and map the landscape components through analog and digital processing methods. At the present stage of development multispectral remote sensing techniques are not ready for operational application to surveys of migratory bird habitat and other such resources. Further developments are needed to: (1) increase accuracy; (2) decrease retrieval and processing time; and (3) reduce costs

Remote functionalisation via sodium alkylamidozincate intermediates : access to unusual fluorenone and pyridyl ketone reactivity patterns

Treating fluorenone or 2-benzoylpyridine with the sodium zincate [(TMEDA)center dot Na(mu-Bu-t)(mu-TMP)Zn(Bu-t)] in hexane solution, gives efficient Bu-t addition across the respective organic substrate in a highly unusual 1,6-fashion, producing isolable organometallic intermediates which can be quenched and aerobically oxidised to give 3-tert-butyl-9H-fluoren-9-one and 2-benzoyl-5-tert-butylpyridine respectively

Solvent and recovery process for lignin

Methods for obtaining purified lignin and the lignin that can be obtained by the methods are described. Methods include processing pretreated lignocellulosic biomass feedstock to recover the lignin and provide a lignin composition with a very low level of impurities such as metals and ash. In addition, the lignin recovered from the process can have a narrow molecular weight distribution and, depending upon the specific stages utilized in the process, can have a predetermined molecular weight. The process includes one or more separation stages in which a lignin-containing feedstock is mixed with a solvent solution. The mixture fractionates to form a solvent-rich liquid phase and a lignin-rich liquid phase, the lignin being partitioned across the phases according to the molecular weight of the lignin. Furthermore, the metal salts of the pretreated lignocellulosic biomass feedstock also partition across the phases

Long-chain acyl-CoA synthetase isoforms differ in preferences for eicosanoid species and long-chain fatty acids

Because the signaling eicosanoids, epoxyeicosatrienoic acids (EETs) and HETEs, are esterified to membrane phospholipids, we asked which long-chain acyl-CoA synthetase (ACSL) isoforms would activate these molecules and whether the apparent FA substrate preferences of each ACSL isoform might differ depending on whether it was assayed in mammalian cell membranes or as a purified bacterial recombinant protein. We found that all five ACSL isoforms were able to use EETs and HETEs as substrates and showed by LC-MS/MS that ACSLs produce EET-CoAs. We found differences in substrate preference between ACS assays performed in COS7 cell membranes and recombinant purified proteins. Similarly, preferences and Michaelis-Menten kinetics for long-chain FAs were distinctive. Substrate preferences identified for the purified ACSLs did not correspond to those observed in ACSL-deficient mouse models. Taken together, these data support the concept that each ACSL isoform exhibits a distinct substrate preference, but apparent substrate specificities depend upon multiple factors including membrane character, coactivators, inhibitors, protein interactions, and posttranslational modification

Disulfide Engineered Lipase to Enhance the Catalytic Activity: A Structure-Based Approach on BTL2

Enhancement, control, and tuning of hydrolytic activity and specificity of lipases are major goals for the industry. Thermoalkaliphilic lipases from the I.5 family, with their native advantages such as high thermostability and tolerance to alkaline pHs, are a target for biotechnological applications. Although several strategies have been applied to increase lipases activity, the enhancement through protein engineering without compromising other capabilities is still elusive. Lipases from the I.5 family suffer a unique and delicate double lid restructuration to transition from a closed and inactive state to their open and enzymatically active conformation. In order to increase the activity of the wild type Geobacillus thermocatenulatus lipase 2 (BTL2) we rationally designed, based on its tridimensional structure, a mutant (ccBTL2) capable of forming a disulfide bond to lock the open state. ccBTL2 was generated replacing A191 and F206 to cysteine residues while both wild type C64 and C295 were mutated to serine. A covalently immobilized ccBTL2 showed a 3.5-fold increment in esterase activity with 0.1% Triton X-100 (2336 IU mg-1) and up to 6.0-fold higher with 0.01% CTAB (778 IU mg-1), both in the presence of oxidizing sulfhydryl agents, when compared to BTL2. The remarkable and industrially desired features of BTL2 such as optimal alkaliphilic pH and high thermal stability were not affected. The designed disulfide bond also conferred reversibility to the enhancement, as the increment on activity observed for ccBTL2 was controlled by redox pretreatments. MD simulations suggested that the most stable conformation for ccBTL2 (with the disulfide bond formed) was, as we predicted, similar to the open and active conformation of this lipase.Financial and logistic support from Colombian Universidad del Valle and COLCIENCIAS (CI 71083-Grant 745-2016-Project 110671250425), Spanish CICYT project BIO-2005-6018576, BFU2017-90030-P, and BFU2011-25326, B. Di G. In addition, thanks to the Spanish MINECO for a FPU fellowship.S