Proteins used in biopharmaceutical and industrial applications often suffer from instability under thermal and chemical stress. To improve protein stability, dextrose, fructose, glycerol, and sorbitol (0.5 – 4.0 M) were evaluated for their ability to stabilize α-chymotrypsin, carbonic anhydrase, and Candida rugosa lipase using differential scanning fluorimetry. Dextrose and sorbitol were most consistent in preserving thermal stability, due to hydrogen bonding and preferential exclusion effects. Another strategy consisted of conjugating lysozyme to poly(acrylic acid) and poly(acrylamide) using EDC/NHS coupling. The conjugation extended lysozyme’s half-life to 4.43 ± 1.88 days with poly(acrylic acid). In contrast, physical mixtures offered little to no protection. The melting temperatures across samples remained in the range of 50 – 53 °C, indicating that conjugation likely provided improved kinetic stability primarily. These results show that both excipients and polymer conjugation are promising techniques to extend the shelf life of proteins.