TY - JOUR
T1 - Collagen extraction from mussel byssus
T2 - a new marine collagen source with physicochemical properties of industrial interest
AU - Rodríguez, F.
AU - Morán, L.
AU - González, G.
AU - Troncoso, E.
AU - Zúñiga, R.N.
PY - 2017/4
Y1 - 2017/4
N2 - Mussel byssus is a by-product of mussel production and is a potential source of collagen. The goal of this study was to extract collagen from the byssus of Chilean mussel using an enzymatic method and characterize it. A pepsin-aided extraction method was employed where first an enzymatic hydrolysis at two pepsin/substrate ratios (1:50 or 4:50) and times (4 or 24 h) was done. Extraction was conducted at 80 °C for 24 h, in a 0.5 N acetic acid solution. All samples were analyzed for collagen content, amino acid profile, turbidity, viscosity, solubility, denaturation temperature and surface tension. Hydrolysis time had significant effect on collagen content, hydroxyproline content and extraction yield. Hydrolysis with a pepsin/byssus ratio of 4:50 for 24 h gave the better extraction performance with values of 69 mg/g protein, 1.8 mg/g protein and 30%, for collagen content, hydroxyproline content and extraction yield, respectively. No differences were found for the viscosity and surface tension of collagen dispersions, suggesting that the enzymatic hydrolysis did not affect the integrity of the collagen molecule. Denaturation temperature of freeze-dried byssus collagen presented a high value (83–91 °C), making this kind of collagen a very interesting material for encapsulation of bioactive molecules and for biomedical applications.
AB - Mussel byssus is a by-product of mussel production and is a potential source of collagen. The goal of this study was to extract collagen from the byssus of Chilean mussel using an enzymatic method and characterize it. A pepsin-aided extraction method was employed where first an enzymatic hydrolysis at two pepsin/substrate ratios (1:50 or 4:50) and times (4 or 24 h) was done. Extraction was conducted at 80 °C for 24 h, in a 0.5 N acetic acid solution. All samples were analyzed for collagen content, amino acid profile, turbidity, viscosity, solubility, denaturation temperature and surface tension. Hydrolysis time had significant effect on collagen content, hydroxyproline content and extraction yield. Hydrolysis with a pepsin/byssus ratio of 4:50 for 24 h gave the better extraction performance with values of 69 mg/g protein, 1.8 mg/g protein and 30%, for collagen content, hydroxyproline content and extraction yield, respectively. No differences were found for the viscosity and surface tension of collagen dispersions, suggesting that the enzymatic hydrolysis did not affect the integrity of the collagen molecule. Denaturation temperature of freeze-dried byssus collagen presented a high value (83–91 °C), making this kind of collagen a very interesting material for encapsulation of bioactive molecules and for biomedical applications.
KW - Collagen
KW - Extraction
KW - Mussel byssus
KW - Pepsin
UR - http://www.scopus.com/inward/record.url?scp=85014531816&partnerID=8YFLogxK
U2 - 10.1007/s13197-017-2566-z
DO - 10.1007/s13197-017-2566-z
M3 - Article
AN - SCOPUS:85014531816
VL - 54
SP - 1228
EP - 1238
JO - Journal of Food Science and Technology
JF - Journal of Food Science and Technology
SN - 0022-1155
IS - 5
ER -