Raman spectroscopy is a powerful analytical technique in contemporary medicine and biomedical research due to its exceptional ability to provide an unambiguous spectroscopic signature of the molecular chemical composition, structure and atom arrangements. Among other applications, investigations of the Raman spectra of porphyrins and their derivatives have been critical in the study of ligand binding mechanisms and drug interactions with healthy and diseased blood cells, as well as for the analysis of blood, hemoproteins and the oxygenation process of human erythrocyte. However, obtaining Raman spectra with satisfactory definition of porphyrin-based molecules can be challenging due to their inherent photo- and thermal sensitivity which leads to laser damage even at low laser power. This severely affects the Raman spectra of porphyrins and limits the Raman signal strength and spectra quality. In this study, we examine two important porphyrins, hemin and protoporphyrin IX, at cryogenic temperatures down to 77 K using a 532 nm excitation Raman instrument in order to study the Raman signal strength and spectral quality dependence on the sample temperature at these extreme low temperatures. We report a significant Raman signal enhancement of up to 310% in the spectra at cryogenic temperatures compared to room temperature measurements. This provides a remarkable improvement of the quality and definition within the spectra and demonstrates that cryogenic Raman measurements can be used as an exceptionally effective method of enhancing the Raman signal and spectra quality for investigations of porphyrins and their derivatives regardless of the excitation wavelength selection. This can greatly improve the effectiveness of Raman spectroscopy in biomedical research, especially in the field of drug design and development, medical diagnostics and disease monitoring and analysis.