Thermal Stability of Chicken Keel Bone Collagen

Document Type

Article

Publication Date

1-1-2014

Abstract

Acid-soluble and pepsin-solubilized collagen were isolated from chicken keel bone and analyzed by electrophoresis and circular dichroism. The denaturation temperature of chicken keel bone was determined by circular dichroism and compared to denaturation temperature of black drum or alligator bone. Our results show that collagen from chicken keel bone is a mixture of type II and type I, has predominantly the amino acids glycine, proline and hydroxyproline, and its secondary structure is predominantly triple-helix. The onset of the denaturation temperature is 37C; at 44C, 50% of the collagen is denatured and the denaturation is complete at 48.8C making it the highest of vertebrate collagen denaturation temperatures reported in the literature. The high heat stability of chicken keel bone collagen may be in part ascribed to its imino acid content. Because of the high heat stability and low methionine content, chicken keel bone collagen is a high value-added product with several biochemical and biomedical applications. © 2013 Wiley Periodicals, Inc.

Publication Source (Journal or Book title)

Journal of Food Biochemistry

First Page

345

Last Page

351

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