Research - Hydrolyzed Collagen Extract
Hydrolyzed Collagen Extract (MonoColl™)
Analysis of Degradation activity of Hydrolyzed Collagen Extract against Recombinant Spike Glycoprotein of SARS-CoV2
In 2020, we collaborated with University Malaysia Sabah (UMS) in carrying out an in vitro experiment to determine the degradation of protein by our mouth spray. Given the proteolytic function of Trypsin, a collaboration with UMS was carried out to test Pro FX on non-living SARS-CoV-2 viruses procured from USA.
From the lab tests, it was concluded that Pro FX is able to degrade spiked proteins of Coronavirus-19, specifically S1 and S2 subunits of SARS-CoV-2.
Link to test report below:
Benefits of Collagen Hydrolysates
Role of Trypsin in tissue repair
Tissue damage of all types, such as surgical or accidental injuries, fractures, and burns, stimulates a well-orchestrated, physiological process of healing, which ultimately leads to structural and functional restoration of the damaged tissues. The tissue repair process can be broadly divided into four continuous and overlapping phases—hemostasis and coagulation, inflammation, proliferation, and remodelling. If the process is interrupted or halted during any stage, it leads to impaired healing and the formation of a chronic wound. Chronic wounds are associated with significant morbidity, mortality, and poor quality of life. Therefore, prompt and effective management of acute tissue injury is necessary to prevent it from progressing to a chronic wound. Proteolytic enzymes have been used to facilitate tissue repair since ancient times. Trypsin: chymotrypsin is an oral proteolytic enzyme preparation that has been in clinical use since the 1960s. It provides better resolution of inflammatory symptoms and promotes speedier recovery of acute tissue injury than several of the other existing enzyme preparations. This review article revisits the role and clinical utility of trypsin: chymotrypsin combination in tissue repair.
Trypsin enzyme cleaves COVID-19 virus binding sites
Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), the causative agent of coronavirus disease 19 (COVID-19) has rapidly spread to the entire world within a few months. The origin of SARS-CoV-2 has been related to the lineage B Betacoronavirus SARS-CoV and SARS-related coronaviruses found in bats. Early characterizations of the SARS-CoV-2 genome revealed the existence of a distinct four amino acid insert within the spike (S) protein (underlined, SPRRAR↓S), at the S1/S2 site located at the interface between the S1 receptor binding subunit and the S2 fusion subunit. Notably, this insert appears to be a distinguishing feature among SARS-related sequences and introduces a potential cleavage site for the protease furin. Here, we investigate the potential role of this novel S1/S2 cleavage site and present direct biochemical evidence for proteolytic processing by a variety of proteases. We discuss these findings in the context of the origin of SARS-CoV-2, viral stability, and transmission.