Skip to main page content
U.S. flag

An official website of the United States government

Dot gov

The .gov means it’s official.
Federal government websites often end in .gov or .mil. Before sharing sensitive information, make sure you’re on a federal government site.

Https

The site is secure.
The https:// ensures that you are connecting to the official website and that any information you provide is encrypted and transmitted securely.

Access keys NCBI Homepage MyNCBI Homepage Main Content Main Navigation
. 2014 Apr;51(4):750-5.
doi: 10.1007/s13197-011-0539-1. Epub 2011 Sep 23.

Detection of collagen through FTIR and HPLC from the body and foot of Donax cuneatus Linnaeus, 1758

R A Nazeer  1 , R Kavitha  1 , R Jai Ganesh  1 , Shabeena Yousuf Naqash  1 , N S Sampath Kumar  1 , R Ranjith  1
Affiliations

Detection of collagen through FTIR and HPLC from the body and foot of Donax cuneatus Linnaeus, 1758

R A Nazeer et al. J Food Sci Technol. 2014 Apr.

Abstract

To make more effective use of available marine resources, acid soluble collagen (ASC) was isolated from body and foot of wedge clam Donax cuneatus Linnaeus, 1758 with acetic acid and was characterized for their potential and commercial applications. The yield of ASC was 17% and 23% respectively. SDS PAGE, UV and FTIR spectroscopy showed that both were type I mainly with slight differences. HPLC was used for identifying the presence of different types of amino acids, where glycine was more or less 20% in both the samples and takes the lead amino acid position and presence of imino acids (11.8 and 12.6%) has been the characteristic feature of type I collagen.

Keywords: Collagen; Donax cuneatus; FTIR; HPLC; Imino acids.

PubMed Disclaimer

Figures

Fig. 1
Fig. 1
SDS-PAGE patterns of ASC from the body and foot of Donax cuneatus on 7.5% gel. Lane 1 ASC foot; lane 2 ASC body; lane 3 high molecular protein marker
Fig. 2
Fig. 2
UV spectra of ASC from foot and body of Donax cuneatus
Fig. 3
Fig. 3
FTIR analysis of collagen from body of Donax cuneatus
Fig. 4
Fig. 4
FTIR analysis of collagen from foot of Donax cuneatus
See this image and copyright information in PMC

References

    1. Birk DE, Bruckner P. Collagen suprastructures. Topi Curr Chem. 2005;247:185–205.
    1. Doyle BB, Bendit EG, Blout ER. Infrared spectroscopy of collagen and collagen-like polypeptides. Biopoly. 1975;14(5):937–957. doi: 10.1002/bip.1975.360140505. - DOI - PubMed
    1. Giraud Guille MM, Besseau L, Chopin C, Durand P, Herbage D. Structural aspects of fish skin collagen which forms ordered arrays via liquid crystalline states. Biomat. 2000;21:899–906. doi: 10.1016/S0142-9612(99)00244-6. - DOI - PubMed
    1. Huesgen G. Sensitive and reliable amino acid analysis in protein hydrolysates using the HP1100 series HPLC. Hewlett Packard Technical Note. 1998;12:5966–3110.
    1. Jongjareonrak A, Bnjakul SJ, Visessanguan W, Nagai M, Tanaka M. Isolation and characterisation of acid and pepsin-solubilised collagens from the skin of brownstripe red snapper (Lutjanus vitta) Food Chem. 2005;93:475–484. doi: 10.1016/j.foodchem.2004.10.026. - DOI

LinkOut - more resources