Research - Hydrolyzed Collagen Trypsin (HCT)

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Hydrolyzed Collagen Trypsin (HCT)

Benefits of Collagen Hydrolysates

Collagen hydrolysate (CH) has received increasing attention in recent decades. This review mainly summarizes the recent developments (the year 2010-2017) regarding the beneficial effects of CH in animal experiments and clinical trials. These beneficial effects include antioxidant, anti-ageing, anti-osteoporotic and anti osteoarthritis, anti-inflammatory, anti-tumour, wound healing, antihypertensive and anti-atherosclerotic, anti-obesity and hypoglycemic effects. We also provide comments on current research and give suggestions for future studies in this review. Considering the wide availability of CH in the field of pharmaceuticals and foods, the study of the potential beneficial effects of CH provides guidance to develop CH-based health care supplements for disease prevention and/or treatment.

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.