Extraction and characterisation of telopeptide-poor collagen from porcine lung

被引：14

作者：

Lin, Yung-Kai ^{[1
]}

Lin, Tung-Yung ^{[1
]}

Su, Hou-Pin ^{[2
]}

机构：

[1] Chinese Culture Univ, Dept Anim Sci, Taipei 11114, Taiwan

[2] Natl Taiwan Univ, Dept Anim Sci & Technol, Taipei, Taiwan

来源：

FOOD CHEMISTRY | 2011年 / 124卷 / 04期

关键词：

Porcine lung; Telopeptide-poor collagen; Optimum extraction condition; I COLLAGEN; PURIFICATION;

D O I：

10.1016/j.foodchem.2010.08.018

中图分类号：

O69 [应用化学];

学科分类号：

070301 [无机化学];

摘要：

The aim of the investigation was to develop optimum extraction conditions of telopeptide-poor collagen from porcine lung (TPCPL). Chemical composition, histological properties of porcine lung, removal efficiency of haemoglobin by different solvents and effects of pepsin solubilisation time on TPCPL properties were evaluated. Histological observation of lung tissue revealed collagen coexists with elastin. Treatment with 0.1 M Tris-HCl/5% Triton X-100 (pH 8.2) for 12 h exhibited the highest efficiency for removal of haemoglobin. The maximal yield of TPCPL reached 6.702 g/kg by pepsin solubilisation for 72 h. SDS-PAGE indicated that type I collagen was a major component of TPCPL: FTIR spectra of all TPCPL were similar to commercial porcine collagen and absent from denatured product (gelatin) and TPCPL 72 exhibited the lowest denaturation temperature (36.4 degrees C) and maximum enzymatic sensitivity. Finally, the optimum pepsin solubilisation of TPCPL was controlled at 4 degrees C for 48 h for better structural integrity and acceptable yield. (C) 2010 Elsevier Ltd. All rights reserved.

引用

页码：1583 / 1588

页数：6

共 31 条

[1]

Ahmed Hafiz, 2005, P1

[2]

Influence of different collagen species on physico-chemical properties of crosslinked collagen matrices [J].

Angele, P ;

Abke, J ;

Kujat, R ;

Faltermeier, H ;

Schumann, D ;

Nerlich, M ;

Kinner, B ;

Englert, C ;

Ruszczak, Z ;

Mehrl, R ;

Mueller, R .

BIOMATERIALS, 2004, 25 (14) :2831-2841

[3]

PEPSIN TREATMENT OF AVIAN SKIN COLLAGEN - EFFECTS ON SOLUBILITY, SUBUNIT COMPOSITION AND AGGREGATION PROPERTIES [J].

BANNISTER, DW ;

BURNS, AB .

BIOCHEMICAL JOURNAL, 1972, 129 (03) :677-+

[4]

Purification and characterization of type II collagen from chick sternal cartilage [J].

Cao, Hui ;

Xu, Shi-Ying .

FOOD CHEMISTRY, 2008, 108 (02) :439-445

[5]

Effect of different acids on the extraction of pepsin-solubilised collagen containing melanin from silky fowl feet [J].

Cheng, Fu-Yuan ;

Hsu, Feng-Wen ;

Chang, His-Shan ;

Lin, Liang-Chuan ;

Sakata, Ryoichi .

FOOD CHEMISTRY, 2009, 113 (02) :563-567

[6]

Forest P, 2007, BIO-MED MATER ENG, V17, P199

[7]

MICRO-BIURET METHOD FOR ESTIMATING PROTEINS [J].

ITZHAKI, RF ;

GILL, DM .

ANALYTICAL BIOCHEMISTRY, 1964, 9 (04) :401-&

[8]

CLEAVAGE OF STRUCTURAL PROTEINS DURING ASSEMBLY OF HEAD OF BACTERIOPHAGE-T4 [J].

LAEMMLI, UK .

NATURE, 1970, 227 (5259) :680-+

[9]

Biomedical applications of collagen [J].

Lee, CH ;

Singla, A ;

Lee, Y .

INTERNATIONAL JOURNAL OF PHARMACEUTICS, 2001, 221 (1-2) :1-22

[10]

Effects of pepsin digestion at different temperatures and times on properties of telopeptide-poor collagen from bird feet [J].

Lin, YK ;

Liu, DC .

FOOD CHEMISTRY, 2006, 94 (04) :621-625

← 1 2 3 4 →