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Metabolic Engineering of Yeast, Zymomonas mobilis, and Clostridium thermocellum to Increase Yield of Bioethanol
Published in Ayerim Y. Hernández Almanza, Nagamani Balagurusamy, Héctor Ruiz Leza, Cristóbal N. Aguilar, Bioethanol, 2023
S. Sánchez-Muñoz, M. J. Castro-Alonso, F. G. Barbosa, E. Mier-Alba, T. R. Balbino, D. Rubio-Ribeaux, I. O. Hernández-De Lira, J. C. Santos, C. N. Aguilar, S. S. Da Silva
High temperature conditions, as well as stress due to ethanol tolerance, are answered by two main cellular mechanisms: the accumulation of HSP (described in Section 5.3.3) and carbohydrates (trehalose) [129, 132, 138]. In these stress conditions, the HSP and trehalose are responsible for folding proteins and reducing membrane permeability [139–141]. Additionally, the accumulation of trehalose makes cells able to tolerate high levels of ethanol and high temperatures, exchanging it with water and stabilizing the membrane and proteins [142]. Some genetic engineering tools aimed to reduce trehalose degradation. One of the enzymes responsible for trehalose degradation is vacuolar acid trehalase (ATH1). Performing a Null mutation of this gene caused high survival rates under various stress conditions, and the inhibition of ATH1 gene activity by antisense RNA decreased trehalose degradation and increased ethanol tolerance [143, 144].
Trehalose Metabolism in Plants under Abiotic Stresses
Published in Hasanuzzaman Mirza, Nahar Kamrun, Fujita Masayuki, Oku Hirosuke, Tofazzal M. Islam, Approaches for Enhancing Abiotic Stress Tolerance in Plants, 2019
Qasim Ali, Sumreena Shahid, Shafaqat Ali, Muhammad Tariq Javed, Naeem Iqbal, Noman Habib, Syed Makhdoom Hussain, Shahzad Ali Shahid, Zahra Noreen, Abdullah Ijaz Hussain, Muhammad Zulqurnain Haider
The first discovery of trehalose was in ergot (a malfunction of fungi) of rye. Later on, trehalose was found in several lower plants such as Botrychium lunaria and Selaginella lepidophylla. Regarding vascular plants, the discovery of trehalose is later and rare. It is found in ripened fruits of members of the Apiaceae family, as well as in leaves of the angiospermic plant Myrothamnus flabellifolius. Recently, aiming towards trehalose’s role as a stabilizing agent for engineered drought-tolerant food plants/crop, the genes responsible for trehalose biosynthesis were introduced into them from E. coli and yeast. However, the accumulation of trehalose is limited due to the presence of enzyme trehalase in plants. It is confirmed by the use of trehalase inhibitors that a high amount of trehalose accumulation was found in transgenic plants. Furthermore, this reported confirmation of trehalose biosynthesis has been found in yeast in a different type of complementation experiment.
Biochemistry
Published in Ronald Fayer, Lihua Xiao, Cryptosporidium and Cryptosporidiosis, 2007
Cryptosporidium can also make N-glycans from fructose-6P or mannose (via mannose-6P), which is required for synthesizing some glycolipids. Enzymes involved in the synthesis of amylopectin and amylose from glucose and glucose-6P, including amylopectin phosphorylase, amylopectin 1,6-glucosidase, and the branching enzyme, are all identified in the C. parvum genome. Another unique feature is the ability to synthesize trehalose via glucose-1P and UDP-glucose, which is not seen in other apicomplexans. Trehalose is commonly found in a wide range of organisms, including bacteria, fungi, plants, and some invertebrates, and may function as an antidesiccant, antioxidant, or protein-stabilizing agent (Schmatz, 1989; Michalski et al., 1992). Because the mannitol cycle found in Eimeria spp. is not present in Cryptosporidium, it is assumed that trehalose may play a role similar to mannitol in Eimeria oocysts (Schmatz, 1989; Michalski et al., 1992). Whether trehalose can serve as an energy source for Cryptosporidium is questionable, because no trehalase ortholog responsible for breaking down trehalose can be identified from the parasite genomes.
Evaluation of the effectiveness of two Iranian su-strains of Metarhizium anisopliae (ascomycota: hypocreales) on the mortality rate of American cockroach
Published in International Journal of Environmental Health Research, 2023
Hamed Ramezani Awal Riabi, Mehran Ghazavi
“Trehalases are also produced to convert trehalose, normally found in the host’s hemolymph, into glucose needed for energy production (Ment et al. 2010; Santi et al. 2010). Mad1 proteins start the expression of genes involved in the cell cycle and enable rapid proliferation of hyphae in the host’s hemolymph. M. anisopleae uses trehalose, which is the main blood sugar in the hemolymph of an insect (Wang and St Leger 2007; Wang et al. 2008)”. Aw and Hue. Aw and Hue (2017), “believes, Trehalase which utilizes trehalose commonly found in the host haemolymph, encoded by ATM1 reduces fertility and disrupts insect homeostasis and physiology, and affects insect locomotor behavior, especially flight movements. In M. anisopliae, dextroxins, especially dextroxins A and E, which are more insecticidal, are produced to subvert the host’s cellular and humoral immune responses. This is done by activating the M. anisopliae spore encapsulated by the host hemocyte”.
Novel treatment of gelatin-copper bio-nanoparticles as a management method against the spiny bollworm, Earias insulana, (Boisd.) (Lepidoptera: Noctuidae) in comparison studies with the uncoated nanoparticles
Published in Inorganic and Nano-Metal Chemistry, 2021
Hala A. Ammar, Eman M. Abd-ElAzeem
It was also observed that all nano-copper solutions caused disturbance between decrease and increase in the activity of trehalase enzyme. The G-CuNPsW and the G-CuNPsE increased its activity to 2095.86 ± 1.04 and 2045.49 µg-1 glucose, where G-CuNPsM highly significantly decreased the enzyme activity to 1015.76 ± 1.13 µg-1 glucose compared to control (1509.76 ± 0.78 µg -g glucose).