Use of OneNote class notebook as a combined electronic laboratory notebook and content delivery tool in an introductory biochemistry laboratory course.

The COVID-19 pandemic has forced a shift in thinking regarding the safe delivery of wet laboratory courses. While we were fortunate to have the capacity to continue delivering wet laboratory experiments with physical distancing and other measures in place, modifications to the mechanisms of delivery within courses were necessary to minimize risk to students and teaching staff. One such modification was introduced in BCH370H, an introductory biochemistry laboratory course, where a OneNote Class Notebook (ONCN) was used as an electronic laboratory notebook (ELN) in place of the traditional hardbound paper laboratory notebook (PLN) used prior to the pandemic. The initial reasoning for switching to an ELN was around safety-allowing course staff and students to maintain physical distancing whenever possible and eliminating the need for teaching assistants to handle student notebooks; however, the benefits of the ONCN proved to be significantly more. OneNote acted not only as a place for students to record notes but the Class Notebook's unique features allowed easy integration of other important aspects of the course, including delivery of laboratory manuals, posting of student results, notetaking feedback, sharing of instructional materials with teaching assistants, and more. Student and teacher experiences with the ONCN as used within a fully in person biochemistry laboratory course, as well as learned best practices, are reviewed.

Glucose oxidase kinetics using MnO2 nanosheets: confirming Michaelis-Menten kinetics and quantifying decreasing enzyme performance with increasing buffer concentration.

MnO2 nanosheets and ultraviolet-visible (UV-Vis) absorbance spectroscopy are used to study glucose oxidase (GOx) kinetics. Glucose oxidation by GOx produces H2O2, which rapidly decomposes the nanosheets and reduces their absorption. This direct approach for monitoring glucose oxidation enables simpler, real time kinetics analysis compared to methods that employ additional enzymes. Using this approach, the present study confirms that GOx kinetics is consistent with the Michaelis-Menten (MM) model, and reveals that the MM constant increases by an order of magnitude with increasing buffer concentration. Since larger MM constants imply higher enzyme substrate concentrations are required to achieve the same rate of product formation, increasing MM constants imply decreasing enzyme performance. These results demonstrate the facility of using MnO2 nanosheets to study GOx kinetics and, given the widespread applications of enzymes with buffers, the important sensitivity of enzyme-buffer systems on buffer concentration.