Food Biochemistry and Food Processing (2 edition)

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Fish Collagen


Soottawat Benjakul, Sitthipong Nalinanon, and Fereidoon Shahidi


Introduction
Collagen Composition and Structure
Isolation of Collagen
Preparation of Raw Materials
Extraction
Acid Solubilization Process
Pepsin Solubilization Process
Recovery of Collagen
Characteristics and Properties of Collagens
Mammalian Collagen
Fish Collagen
Protein Components
Fourier Transform Infrared Spectroscopy
Thermal Stability
Zeta (ζ) Potential
Invertebrate Collagen
Factor Affecting Collagen Properties
Applications of Collagen
Food Applications
Biomedical Applications
Pharmaceutical Applications
References

Abstract:Fish collagen has gained increasing interest as the al-
ternative for mammalian counterpart. It can be generally produced
from by-products generated during processing of fish and inverte-
brates. The potential raw materials include skin, bone, scale, and so
on. Types and molecular properties of collagen vary with the source,
habitat of fish, extraction process, and other factors. In general, col-
lagen can be extracted from collagenous materials at low tempera-
ture with the aid of various acids to avoid thermal denaturation. To
increase the extraction yield, pepsins from mammalian and fish ori-
gins, which specifically cleave at telopeptide region, have been used
successfully without the changes in molecular properties. Fish col-
lagen can be of food, biomedical, and pharmaceutical applications.

INTRODUCTION


Collagen is the fibrous protein of animal connective tissue,
contributing to the unique physiological functions of tissues in
skins, tendons, bones, cartilages, and so on and is associated
with toughness in mammalian muscle (Foegeding et al. 1996,
Ogawa et al. 2003, Muyonga et al. 2004, Yan et al. 2008,
Kittiphattanabawon et al. 2010a). The collagen fibers are
essentially inextensible and, therefore, provide mechanical
strength and also allow flexibility between various organs of the
body (Bailey et al. 1998).
Collagen is widely used in food, biomedical, pharmaceutical,
and cosmetics, and its consumption has been increasing along
with the development of new industrial application (Nalinanon
et al. 2007, Regenstein and Zhou 2007, Woo et al. 2008). Col-
lagen exhibits biodegradability, weak antigenecity, and superior
biocompatibility compared with other natural polymers, such as
albumin and gelatin (Lee et al. 2001). Generally, commercial col-
lagens are produced from bovine and porcine hides and bones.
Currently, the increasing attention of alternative sources for re-
placement of mammalian collagen has been paid, especially
from seafood processing by-products. Fish collagen can be used
for Halal and Kosher products for Muslim and Jewish communi-
ties, respectively. Because of the outbreak of bovine spongiform
encephalopathy and bird flu, the increasing demand of fish col-
lagen has been gained (Jongjareonrak et al. 2005, Nalinanon
et al. 2007, 2008, Regenstein and Zhou 2007, Duan et al. 2009,
Kittiphattanabawon et al. 2010a). Collagen can be extracted
from fish skin, scale, and bone. Collagen is also found in the
body walls and cuticles of invertebrates (Meena et al. 1999).
With the appropriate extraction technology, collagen from fish
or aquatic animals can be used as the potential alternative for
mammalian counterpart.

Food Biochemistry and Food Processing, Second Edition. Edited by Benjamin K. Simpson, Leo M.L. Nollet, Fidel Toldr ́a, Soottawat Benjakul, Gopinadhan Paliyath and Y.H. Hui.
©C2012 John Wiley & Sons, Inc. Published 2012 by John Wiley & Sons, Inc.

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