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Acid soluble collagen (ASC) and pepsin soluble collagen (PSC) were isolated from rohu skin with the yield of 64.2 and 6.8% (dry weight basis), respectively. Both collagens had glycine as the major amino acid with imino acid content of 196-202 residues/1,000 residues and were characterized as type I collagen with molecular composition of (1)(2)2-heterotrimer. Fourier transform infrared spectra of both collagens were similar, with no shift in wavenumber of all amide bands. The T-max value of ASC and PSC was 36.40 and 35.48 degrees C, respectively. The zero surface net charge of ASC and PSC was found at pH 5.9 and 5.3, respectively.

Pertenece a

Hokkaido University Collection of Scholarly and Academic Papers  

Autor(es)

Savedboworn, Wanticha -  Kittiphattanabawon, Phanat -  Benjakul, Soottawat -  Sinthusamran, Sittichoke -  Kishimura, Hideki - 

Id.: 70838753

Idioma: inglés  - 

Versión: 1.0

Estado: Final

Palabras claveCollagen - 

Tipo de recurso: article (author version)  - 

Tipo de Interactividad: Expositivo

Nivel de Interactividad: muy bajo

Audiencia: Estudiante  -  Profesor  -  Autor  - 

Estructura: Atomic

Coste: no

Copyright: sí

: This is an Accepted Manuscript of an article published by Taylor & Francis in Journal of Aquatic Food Product Technology 2017, available online: http://www.tandfonline.com/10.1080/10498850.2015.1133747.

Requerimientos técnicos:  Browser: Any - 

Fecha de contribución: 06-ene-2018

Contacto:

Localización:
* Journal of aquatic food product technology, 26(3): 248-257

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  3. Angiotensin I Converting Enzyme Inhibitory Peptides Derived from Phycobiliproteins of Dulse Palmaria palmata We examined the inhibitory activity of angiotensin I converting enzyme (ACE) in protein hydrolysates...
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