The wide interest in protein films is mainly due to their biodegradability.

The frequent use of gelatin films

in food, pharmaceutical and photographic industries made it the most popular biodegradable protein film.
Dry protein products such as packaging, capsules are easily damaged during processing, transport and
storage. This damage, which often manifested itself in brittle fracture, is conditioned by a decrease of
resistance to external mechanical forces and governed by the physico-chemical structure of protein films.

For this laboratory report, we shall be discussing (3) points:

Discussion

1. Gelatin film is brittle when procured with a basic solvent under silicone plastics
2. Gelatin film is translucent due to excess amount of acid or base
3. Phosphate buffers cause gelatin films to be elastic

1. Brittle Gelatin Films

a. Gelatin forms a three-dimensional network with zones of intermolecular microcrystalline
junctions (Slade & Levine, 1987), and the dehydration of this system may produce brittle films.
b. In general, gelatin films are brittle and susceptible to crack due to the strong cohesive energy
density of the polymer (Arvanitoyannis et al., 1998a).
c. Plasticizing gelatin films using glycerol (alcohol) reduces the brittleness of the film.
d. At different pHs of type A pigskin gelatin, and their mechanical characteristics were
determined. At pHs higher than 9 and lower than 5, Young’s modulus, E, and the stress at
break, σb, of the films decreased significantly.

2. Translucent Gelatin due to Excess Acid/Base

a. Gelatin behaves like a weak acid, which, if in contact with a neutral salt, will exchange some
of its H ions for the cations of the salt. The anions of the salt do not enter into combination
with the gelatin or if they do their effect is not noticeable. When, however, we treat gelatin
with a comparatively low concentration of a strong acid, e.g. ~/lo0 HCI, gelatin chloride or
hydrochloride is formed which should be able to exchange its anion when treated with a
neutral salt, while the cation of the latter should not enter into any reaction with the gelatin,
or if it does its effect should not be noticeable.
b. The acidic treatment used to denature the collagen in animal hides leaves porcine gelatin
vulnerable to solutions with a pH of 3 or below—on par with distilled white vinegar.

3. Phosphate buffers cause gelatin films to be elastic

a. PBS salts play a very important role in gelatin gelation, which accelerate the formation of the
gelatin gel and enhanced the rigidity of gelatin.
b. The homogenously dispersed insoluble phosphate salts serve as doping granules improve the
elastic properties of gelatin gel.
c. Excess sodium chloride hinders the formation of the triple-helix, causing the longer gelation
time and a lower G′. The formation of hydrogen bonds is impeded by Na+ and Cl-, due to their
electrochemical properties, resulting in a reduction of hydrogen bonds and a decrease in
crosslink density.