Proceedings of the 8th International Conference on Advanced Materials and Systems 2020
DOI: 10.24264/icams-2020.v.13
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Micro DSC and NMR MOUSE studies of collagen–vegetable tannin interaction mechanism during leather making

Abstract: In this study NMR MOUSE and micro DSC techniques were used to investigate the interaction between collagen and various vegetable tannins during leather making process with the aim of gaining a deeper understanding of different water environment in relation to tannin type. We have previously showed that relaxation times may provide useful information on collagen matrix properties. The vegetable tanned leathers were obtained by patented techniques inspired from ancient recipes at the National R&D Institute f… Show more

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Cited by 2 publications
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“…Van Stiphout claimed that the short and long components of T 2 are connected to more or less rigid collagen matrix structures, i.e., short relaxation times correspond to rigid (tightly bound) structures, while long relaxation times correspond to more loosely bonded structures [ 73 ]. Accordingly, the increase of the percentage of W B corresponding to the looser bonded structures ( Table 2 and Figure 2 ) in S-OSA3 (32%) compared to S-OSA2 (14%) and S-GA1 (12%) can be interpreted in terms of an increased chain mobility and reduction of tightly bonded structures [ 74 ]. This suggest a less densely packed collagen matrix and could be explained by the higher molecular mass distribution and lower amount of aldehyde groups of low OD OSA [ 55 ].…”
Section: Resultsmentioning
confidence: 99%
“…Van Stiphout claimed that the short and long components of T 2 are connected to more or less rigid collagen matrix structures, i.e., short relaxation times correspond to rigid (tightly bound) structures, while long relaxation times correspond to more loosely bonded structures [ 73 ]. Accordingly, the increase of the percentage of W B corresponding to the looser bonded structures ( Table 2 and Figure 2 ) in S-OSA3 (32%) compared to S-OSA2 (14%) and S-GA1 (12%) can be interpreted in terms of an increased chain mobility and reduction of tightly bonded structures [ 74 ]. This suggest a less densely packed collagen matrix and could be explained by the higher molecular mass distribution and lower amount of aldehyde groups of low OD OSA [ 55 ].…”
Section: Resultsmentioning
confidence: 99%
“…Van Stiphout claimed that the short and long components of T 2 are connected to more or less rigid collagen matrix structures, i.e., short relaxation times correspond to rigid (tightly bound) structures, while long relaxation times correspond to more loosely bonded structures [73]. Accordingly, the increase of the percentage of W B corresponding to the looser bonded structures (Table 2 and Figure 2) in S-OSA3 (32%) compared to S-OSA2 (14%) and S-GA1 (12%) can be interpreted in terms of an increased chain mobility and reduction of tightly bonded structures [74]. This suggest a less densely packed collagen matrix and could be explained by the higher molecular mass distribution and lower amount of aldehyde groups of low OD OSA [55].…”
Section: H Unilateral Nmr and Ftir-atr Analysis Of Collagen-osa Chemi...mentioning
confidence: 99%