Measure to Manage: Ghost PLUZ Collector App

The Ghost Public Land Use Zone (PLUZ), located 60 km northwest of Calgary, is a popular area for recreation activities such as camping, hiking, fishing, and driving off-highway vehicles (OHVs), despite lack of sufficient facilities to support these activities. There is a desire among concerned residents for a better understanding of the current land use to warrant the development of more facilities, to help decrease widespread environmental damage resulting from recreation. Using Esri’s Collector for ArcGIS, a smartphone app was created which allows residents to record incidents of environmental damage related to recreation, with or without cell reception. The data fields and the data input structure were designed in collaboration with the residents to ensure optimal usability. Data is automatically georeferenced and stored on ArcGIS Online, Esri’s cloud-based mapping platform, allowing multiple people to use the app and view the data simultaneously. The app was successfully tested by the community users, their feedback was recorded, and the app has drawn interest from Alberta government representatives who make decisions about recreational planning in the Ghost PLUZ. * Indicates faculty mentor

Recent advances in immobilization strategies for glycosidases

Glycans play important biological roles in cell-to-cell interactions, protection against pathogens, as well as in proper protein folding and stability, and are thus interesting targets for scientists. Although their mechanisms of action have been widely investigated and hypothesized, their biological functions are not well understood due to the lack of deglycosylation methods for large-scale isolation of these compounds. Isolation of glycans in their native state is crucial for the investigation of their biological functions. However, current enzymatic and chemical deglycosylation techniques require harsh pretreatment and reaction conditions (high temperature and use of detergents) that hinder the isolation of native glycan structures. Indeed, the recent isolation of new endoglycosidases that are able to cleave a wider variety of linkages and efficiently hydrolyze native proteins has opened up the opportunity to elucidate the biological roles of a higher variety of glycans in their native state. As an example, our research group recently isolated a novel Endo-β-N-acetylglucosaminidase from Bifidobacterium longum subsp. infantis ATCC 15697 (EndoBI-1) that cleaves N-N'-diacetyl chitobiose moieties found in the N-linked glycan (N-glycan) core of high mannose, hybrid, and complex N-glycans. This enzyme is also active on native proteins, which enables native glycan isolation, a key advantage when evaluating their biological activities. Efficient, stable, and economically viable enzymatic release of N-glycans requires the selection of appropriate immobilization strategies. In this review, we discuss the state-of-the-art of various immobilization techniques (physical adsorption, covalent binding, aggregation, and entrapment) for glycosidases, as well as their potential substrates and matrices. © 2016 American Institute of Chemical Engineers Biotechnol. Prog., 33:104-112, 2017