Protein engineering explores and manipulates protein functions and molecular interactions to garner knowledge about and improve upon existing protein frameworks. Phage display technologies have been essential to the advancement of high-throughput analysis of such efforts. The research described herein explores the use of phage display for engineering thermostability and antigen binding. Chapter One overviews the expansive utility of protein engineering and phage display in creating novel proteins and cites examples of such efforts. Described in Chapter Two, three mutagenesis strategies were separately applied to the enzyme 5-epi-aristolochene synthase (TEAS) in efforts to engineer a thermostable terpene synthase. Chapter Three details how diverse phage-displayed antibody antigen-binding fragment (Fab) libraries can be used to select for antigen binding. The antibody Fab is responsible for molecular recognition, and as such, a synthetic Fab library was used to engineer binding to the human immunodeficiency virus class 1 (HIV-1) protein Nef. The selected Fab binds Nef with high affinity and specificity, and allows for future study of the protein and virus. Thus, this thesis investigates how phage display can be used to facilitate protein engineering.