Study of the degradation of gelatin in paper upon aging using aqueous size-exclusion chromatography.

We studied the aging behaviour of gelatin used to size paper. Thus far, research on the aging of paper has largely ignored the sizing agent. Degradation of the protein was characterised and the impact of paper components, such as cellulose, and aluminium potassium sulphate was evaluated. Whatman No. 1 filter papers sized with two types of gelatins (A and B) were prepared as model samples. Commercially sized modern papers (Arches) were also studied in order to compare laboratory samples with real artist papers. Both types of papers were artificially aged (80 degrees C, 50% relative humidity for 35 and 94 days). Historic papers were included in the study in order to compare artificially aged with naturally aged gelatin. The aqueous extracts from the papers were characterised by aqueous size-exclusion chromatography (SEC) using four PL-Aquagel-OH columns and UV photodiode array detection at 220, 254 and 280 nm. Results showed that gelatin undergoes hydrolysis upon aging, type A gelatin showing a faster degradation rate than type B. The result was an increase in the lower-molar-mass fractions, under 50,000 g mol(-1), and especially in a characteristic fraction with a peak molecular mass (MP) of 14,000 g mol(-1). A significant decrease in the extraction yields of alpha-, beta- and gamma-chains occurred after aging. This was attributed to crosslinking, leading to the formation of less-soluble polypeptides with very high molar mass (>800,000 g mol(-1)) Less than 10% alum had no impact on the degradation rate; higher alum contents accelerated hydrolysis reactions.