Introduction:

During Colombian silk transformation to obtain threads, a protein called sericin is removed and discarded. Nevertheless, due to its properties, it should be industrially recovered and used.

Objective:

Characterize the sericin obtained, through spray drying, from Colombian silk threads.

Materials and methods:

The sericin was extracted using hot water in autoclave and later spray-dried. Obtained solution was dehydrated in dry spray equipment. The obtained powdered sample was characterized by morphological tests (SEM), isoelectric point and protein content, antimicrobial activity, solubility, aqueous activity (aw) and color.

Results:

The results obtained by SEM showed that the degumming process extracted the most of sericin from the threads. In addition, it was seen that dehydrated samples have a spherical shape, with a rough, concave and collapsed surface. The protein content and the isoelectric point of sericin were 99.5 % and 4.07, respectively. No antimicrobial properties were observed against the microorganisms studied. The solubility of the protein increased with temperature (44.11 % ± 5.75 at 90 °C), its aw was 0.287, and its color showed a white trend whose CIELAB coordinates are L: 89.55 ± 0.20, a*: +0.44 ± 0.04 and b*: +5.16 ± 0.30.

Conclusions:

The results show that it is possible to extract sericin from silk threads using autoclave, with high percentages of yield. Additionally, it was observed that the sample is susceptible to be dehydrated by spray drying, showing characteristics that can be studied in greater depth to evaluate the viability of using this protein in the development of different products.

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