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The degree of conversion of collagen into gelatin depends on the pretreatment, function of temperature, pH, and extraction time Johnston-Banks 19900). Johnston-Banks 1990
Conversion of collagen into gelatin during heating reduces the toughness of the connective tissue however this conversion is slow at low cooking temperatures (around 60 °C).
Called a "phase change" the conversion of collagen starts happening at about 160°F.
If the stall was caused by conversion of collagen to gelatin, since the transition happens within the foil and there is no stall, the phase change of collagen cannot be the cause.
The ideal cooking of meat would minimize moisture loss and toughening of the fibers while also maximizing the conversion of collagen to gelatin.
The mechanism behind the tenderizing action of acidic marinades is shown to involve increased proteolysis and increased conversion of collagen to gelatin.
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For example, Weiner et al. recognised the role high RH plays in the conversion of perturbed collagen into gelatine, Schilling et al. and Dernovšková et al. observed the change in volume of parchment from water absorption and desorption at different RH, and Hanson et al. recognised the change in mechanical properties of parchment with changes in RH.
However, BFA had a profound effect on the intracellular conversion of procollagen into collagen and the secretion of both procollagen and collagen (Table 1).
These results suggest that enhancing the conversion of procollagen to collagen is a key step in the formation of extracellular matrix by keratocytes in vitro.
Ideally, the RH range for parchment storage, display and handling would minimise a) the conversion of perturbed/pre-gelatinised collagen into gelatine, b) reduce the loss of water from the parchment, which will increase the brittleness, c) reduce mould growth and d) be cost effective.
Thus, increased serum levels of this N-terminal pro-collagen Type III peptide (PIIINP), found in patients with diseases presenting with fibrosis, indicate excessive conversion of Type III pro-collagen into Type III collagen.
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