The O‐linked β‐N‐acetylglucosamine (O‐GlcNAc) modification, termed O‐GlcNAcylation, is an essential and dynamic post‐translational modification in cells. O‐GlcNAc transferase (OGT) installs this modification on serine and threonine residues, whereas O‐GlcNAcase (OGA) hydrolyzes it. O‐GlcNAc modifications are found on thousands of intracellular proteins involved in diverse biological processes. Dysregulation of O‐GlcNAcylation and O‐GlcNAc cycling enzymes has been detected in many diseases, including cancer, diabetes, cardiovascular and neurodegenerative diseases. Here, recent advances in the development of molecular tools to investigate OGT and OGA functions and substrate recognition are discussed. New chemical approaches to study O‐GlcNAc dynamics and its potential roles in the immune system are also highlighted. It is hoped that this minireview will encourage more research in these areas to advance the understanding of O‐GlcNAc in biology and diseases.
This research investigated the role of agitation, high-melting emulsifier and water content on the crystallization process and the texture of water-in-oil emulsions produced on a pilot plant scale using a scraped surface heat exchanger (SSHE). Our results indicated that shear affected the hardness of the emulsions as they exited the SSHE, with softer emulsions processed at higher shear; once the emulsions reached equilibrium temperature, no differences in texture due to shear were observed. The added emulsifier delayed the crystallization of emulsions processed in the SSHE with no further effect on the equilibrium solid fat content (SFC) or textural properties of emulsions after 24 h of storage. The texture of the crystallized emulsions at early stages of processing was influenced by the amount of water and water droplet size; the larger the amount of water and the smaller the droplets, the higher the hardness of emulsions. Once the emulsions reached equilibrium temperature, further crystallization took place, and the texture depended only on the SFC.
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