The quest to better refine the structure –function relationship of proteins/enzymes has been a long sought-after goal by those involved in protein chemistry/biochemistry; those involved in food protein research are no different. Better refinement will allow for more accurate/precise prediction of protein functionality under various environmental conditions and/or the design of proteins for targeted applications.  Part of the challenge has been to move from descriptive towards mechanistic research and understanding.  As part of this effort, we have applied a variety of techniques including chemical modification, molecular biology, physicochemical analyses and molecular modelling to a variety of food (both pure and mixtures, e.g., cowpea, composite blends animal and plant) and non-food-related proteins/enzymes. Much of our recent work has focused on the aspartic proteases, a class of hydrolytic enzymes that have been isolated from a number of natural sources (e.g., plants, animals, fungi) and are characterized by two catalytic aspartate residues in the active site. In the food area, aspartic proteinases have been used as processing aids in the manufacture of a variety of products (e.g., milk coagulant in cheese making) while non-food related examples include those involved in areas such as anti-malarial therapeutics and plant pathogen inhibitors. This talk will present an overview of the non-linear journey our group has travelled.

The quest to better refine the structure – function relationships of proteins/enzymes: A food scientist’s journey

ACS Fall 2021

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