狭鳕鱼皮胶原蛋白结构和物理特性的研究
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摘要
为了充分利用水产品加工废弃物,本文以资源丰富并且资源集中的水产品加工下脚料—狭鳕鱼鱼皮为原料,研究其中胶原纤维的分布和形态,并采用先进的分离技术和手段提取纯化鱼皮中的主要成分—胶原蛋白,主要进行胶原蛋白分子结构和物理特性的研究。
1.组织切片观察发现狭鳕鱼皮中主要含有胶原纤维,没有观察到肌纤维的存在,并且其类型主要为Ⅰ型胶原。胶原纤维表现周期性的明暗相间的条带,但是纤维的直径分布是不均匀的。
2.通过醋酸法提取了狭鳕鱼皮中的酸溶性胶原蛋白,经分析确定其为Ⅰ型胶原蛋白,并较好地保持了螺旋结构。但是,该胶原蛋白具有不同于哺乳动物胶原蛋白的热稳定性,其热变性温度和热收缩温度分别为24.6℃和47℃。
3.经DEAE-52纤维素柱和Sephacryl S-300 HR凝胶柱层析,得到进一步纯化的狭鳕鱼皮酸溶性胶原蛋白。该蛋白冻干样品为丝状纤维结构,并较好地保持了三螺旋结构,纤维中分子链之间的距离为1.18nm,螺旋结构上相邻氨基酸残基之间的距离为0.27nm。经肽质量指纹图谱分析发现狭鳕鱼皮胶原蛋白与纤维堆囊菌So ce 56的假定蛋白sce1263具有良好的同源性,肽段匹配度达31%。
4.不同浓度和不同温度下的狭鳕鱼皮胶原蛋白溶液的弹性模量G’和粘性模量G’’均表现剪切频率依赖性,并且高浓度的溶液中胶原蛋白分子间表现明显的缠结现象;30℃的溶液中由于分子原有结构的破坏,G’和G’’交点对应的频率较其它温度的高,而40℃和50℃的溶液中由于分子的聚集而表现明显的缠结现象。通过对狭鳕鱼皮胶原蛋白功能特性的研究分析发现该胶原蛋白溶解度良好,乳化性稍差但是稳定性较好。
5.狭鳕鱼皮胶原蛋白在溶液中表现自聚集的特性,与样品的质量浓度、pH和离子强度密切相关。当质量浓度高于0.6g/L时,胶原蛋白表现明显的聚集行为; pH7.2比较适合于胶原蛋白的聚集;而离子强度可延缓胶原蛋白的聚集,但当NaCl浓度为30和60mmol/L时,较容易形成大的聚集体。
芘荧光探针法研究了狭鳕鱼皮胶原蛋白的聚集行为,发现该胶原蛋白的聚集特性表现明显的浓度效应,存在质量浓度临界点(即临界聚集质量浓度,CAMC)。通过芘荧光探针I1/I3值与溶液中胶原蛋白质量浓度对数的关系,确定该胶原蛋白的CAMC为0.48g/L。通过测定胶原蛋白的聚集数(Nagg)发现,Nagg不是一定值,它随着质量浓度的变化而变化,在较低的胶原蛋白质量浓度下,Nagg随着质量浓度的增加而明显增加,当质量浓度达到1.2g/L时,Nagg增长缓慢。
此外,将芘荧光探针用来监测胶原凝胶的动态形成过程。在6.67%明胶溶液中,选用芘探针分子浓度为40μmol/L,以I1/I3值的变化来表征凝胶的交联情况。
6.天然植物多酚—没食子酸和芦丁用于狭鳕鱼皮凝胶的交联研究中。当没食子酸添加量为20mg/g gelatin时,凝胶的凝胶强度最大;而芦丁添加量为8 mg/g gelatin时,凝胶强度达到最大,并且具有显著性,但是二者对凝胶的凝胶点和溶胶点的影响均不显著。6mg/g gelatin和8mg/g gelatin的芦丁均使凝胶的热稳定性明显提高,热收缩温度增加了10℃,但是没食子酸对凝胶的热稳定几乎没有影响。凝胶微观结构观察发现没食子酸和芦丁均使凝胶发生了交联,以芦丁的交联现象更为明显。X—射线衍射实验表明,没食子酸和芦丁可与凝胶分子链发生相互作用。经红外光谱分析,没食子酸和芦丁主要与凝胶分子链中的C-N-C基团和羧基发生相互作用。
没食子酸和芦丁对鱼皮凝胶的溶胀性是有影响的。20和30mg/g gelatin的没食子酸以及6和8mg/g gelatin的芦丁均使凝胶的平衡溶胀度降低,以芦丁的影响更为显著。在凝胶溶胀初期,鱼皮凝胶和20mg/g gelatin没食子酸以及6和8mg/g gelatin芦丁交联的凝胶均表现非Fick扩散过程,而30mg/g gelatin的没食子酸交联凝胶表现Fick扩散过程。通过对整个溶胀过程动力学分析发现,没食子酸和芦丁均使凝胶到达平衡溶胀的时间缩短,而芦丁效果尤为明显。无论是鱼皮凝胶还是多酚交联凝胶,在溶胀过程中均是凝胶高分子链的松弛过程为速控步骤。
狭鳕鱼皮水凝胶以及多酚交联水凝胶中的水按照水凝胶的“三态水”模型可分为自由水、中间水和结合水,其中以自由水含量最高。没食子酸和芦丁的加入对凝胶的平衡水分含量没有明显影响,但可改变凝胶中可冻结水和非冻结结合水的分布。20和30mg/g gelatin的没食子酸的加入使水凝胶中非冻结结合水含量降低,而6和8mg/g gelatin的芦丁的加入却使水凝胶中非冻结结合水含量升高。
To make more effective use of underutilized resources, the distribution and morphology of collagen fiber was studied in the leftover in aquatic product processing-walleye pollock (Theragra chalcogramma) skin, from which, acid-soluble collagen was isolated to investigate the molecular structure and physical properties.
1. Histological observation clarified the presence of collagen fibre in walleye pollock skin. The results of picric acid-sirius red stain indicated that typeⅠcollagen was found in pollock skin. And electron microscopic observation revealed that skin of pollock consisted of bundles of collagen fibrils with a repeating period composed of one dark segment plus one light segment, but collagen fibrils differed in diameter.
2. Acid-soluble collagen (ASC) was successfully extracted from the skin of pollock. It was identified as typeⅠcollagen with the existence of helical arrangements of collagen. The denaturation temperature (Td) and shrinkage temperature (Ts) were 24.6℃and 47℃, respectively, both lower than those of mammalian collagens.
3. Acid-soluble collagen from pollock skin was further purified using a combination of DEAE-52 cellulose and Sephacryl S-300 HR gel filtration chromatography. The purified collagen showed a structure of filamentary fibril with helical arrangements that the distance between the molecular chains was 1.18nm, and the unit height, typical of the triple helical structure, was 0.27nm. Peptide mapping revealed that the collagen exhibited the homology with the hypothetical protein sce1263 of sporangium cellulosum‘So ce 56’with the sequence coverage of 31%.
4. Dynamic viscoelastic properties of collagen solutions with concentrations of 0.1~1.0% (w/w) were characterized by means of oscillatory rheometry at temperatures ranging from 20 to 50℃. Results showed that both storage modulus (G’) and loss modulus (G’’) increased with the increase of frequency. According to a three-zone model, dynamic modulus of collagen solutions in the studied concentrations and temperatures showed terminal-zone and plateau-zone behavior. Entanglements could be viewed when the concentration of collagen solution was higher, as well as the temperature reaching 40 and 50℃. But there were no significant entanglements in collagen solution at the temperature of 30℃. On the other hand, the functional properties of collagen from pollock skin were evaluated. Results showed that pollock skin collagen showed the better solubility and worse emulsifying activity, but its emulsion was stable.
5. Aggregation kinetics of collagen from pollock skin was studied. The main factors including mass concentration of collagen, pH value and ionic strength, which affect the aggregation property, were discussed. The results proved that the aggregation characterization of collagen was closely related to the factors mentioned above. When mass concentration of collagen was increased to 0.6g/L and above, evident aggregation behavior was found in solution. And collagen showed higher aggregation rate at pH7.2. Ionic strength slowed down the collagen aggregation, but when the NaCl concentration reaching 30 or 60mmol/L, it was easier to form large aggregates. So these factors could be considered when the aggregation property of collagen from pollock skin was studied and applied.
The aggregation behavior of collagen from pollock skin was investigated by the fluorescence probe pyrene. Results showed that the aggregation property of collagen showed mass concentration dependence, and the threshold mass concentration was found, namely the critical aggregation mass concentration (CAMC). Using plots of pyrene I1/I3 ratio versus logarithm of different mass concentration of collagen, the CAMC was found to be at 0.48g/L. The subsequent dynamic fluorescence decaying study revealed that the aggregation number of collagen was not a constant, varying with different mass concentrations. The structure of aggregates tended to be integrated, when collagen mass concentration reaching 1.2g/L and above.
The fluorescence probe pyrene was also used to monitor the dynamic gelatin formation process. The concentration of pyrene was chosen as 40μmol/L in 6.67% (w/w) gelatin from pollock skin. It was shown that the changes of I1/I3 ratio in pyrene fluorescence spectra were well related to the cross-linking of gelatin.
6. Gelatin from pollock skin was cross-linked, respectively, by the natural plant polyphenols-gallic acid and rutin. Results showed that the maximal gel strength of gelatin could be obtained when the content of gallic acid was 20mg/g gelatin, or when the content of rutin was 8mg/g gelatin, but the gelling and melting point of gelatin showed no significant increase after gallic acid or rutin added. The shrinkage temperature of gelatin was about 10℃higher with the introduction of 6mg/g gelatin and 8mg/g gelatin rutin, while there were no obvious effects on the thermal stability of gelatin with addition of 20mg/g gelatin and 30mg/g gelatin gallic acid. Scanning electron microscopy (SEM) revealed that greater cross-linking of gelatin was found after gallic acid or rutin added, but it was evident in rutin-gelatin. There were two peaks in the X-ray diffraction diagrams of gelatin with and without ingredients (gallic acid or rutin). But the distance between the molecular chains of gelatin was smaller after the addition of gallic acid or rutin, revealing that they could cross-linked with the polypeptide chains of gelatin. FTIR investigations suggested that gallic acid and rutin mainly interacted with C-N-C group and carboxyl group.
The effect of gallic acid and rutin on swelling behavior of gelatin was investigated. It was shown that the equilibrium swelling ratio decreased with the introduction of 20mg/g gelatin and 30mg/g gelatin gallic acid, as well as 6mg/g gelatin and 8mg/g gelatin rutin, but it was evident in rutin-gelatin. In the primary swelling process, the swelling behavior of gelatin with and without cross-linking agent (20mg/g gelatin gallic acid, 6mg/g gelatin and 8mg/g gelatin rutin) followed the Fick’s law of diffusion, while that of gelatin containing 30mg/g gelatin gallic acid obeyed the non-Fick’s law of diffusion. Besides, the relaxation of polypeptide chains was the rate-determining step in the whole swelling process of gelatin with and without cross-linking agents.
Differential scanning calorimetry (DSC) was employed to probe the state of water in the hydrogel, and the effect of gallic acid and rutin on the state of water was discussed. The results indicated that there were freezing free, freezing bound and nonfreezing bound water in gelatin, when the swelling equilibrium was reached. Addition of gallic acid and rutin did not show obvious effect on equilibrium water content of gelatin, but produced much effect on the distribution of frozen and non-frozen water. The non-frozen water was lower after addition of 20mg/g gelatin and 30mg/g gelatin gallic acid, while it was higher after addition of 6mg/g gelatin and 8mg/g gelatin rutin.
1.组织切片观察发现狭鳕鱼皮中主要含有胶原纤维,没有观察到肌纤维的存在,并且其类型主要为Ⅰ型胶原。胶原纤维表现周期性的明暗相间的条带,但是纤维的直径分布是不均匀的。
2.通过醋酸法提取了狭鳕鱼皮中的酸溶性胶原蛋白,经分析确定其为Ⅰ型胶原蛋白,并较好地保持了螺旋结构。但是,该胶原蛋白具有不同于哺乳动物胶原蛋白的热稳定性,其热变性温度和热收缩温度分别为24.6℃和47℃。
3.经DEAE-52纤维素柱和Sephacryl S-300 HR凝胶柱层析,得到进一步纯化的狭鳕鱼皮酸溶性胶原蛋白。该蛋白冻干样品为丝状纤维结构,并较好地保持了三螺旋结构,纤维中分子链之间的距离为1.18nm,螺旋结构上相邻氨基酸残基之间的距离为0.27nm。经肽质量指纹图谱分析发现狭鳕鱼皮胶原蛋白与纤维堆囊菌So ce 56的假定蛋白sce1263具有良好的同源性,肽段匹配度达31%。
4.不同浓度和不同温度下的狭鳕鱼皮胶原蛋白溶液的弹性模量G’和粘性模量G’’均表现剪切频率依赖性,并且高浓度的溶液中胶原蛋白分子间表现明显的缠结现象;30℃的溶液中由于分子原有结构的破坏,G’和G’’交点对应的频率较其它温度的高,而40℃和50℃的溶液中由于分子的聚集而表现明显的缠结现象。通过对狭鳕鱼皮胶原蛋白功能特性的研究分析发现该胶原蛋白溶解度良好,乳化性稍差但是稳定性较好。
5.狭鳕鱼皮胶原蛋白在溶液中表现自聚集的特性,与样品的质量浓度、pH和离子强度密切相关。当质量浓度高于0.6g/L时,胶原蛋白表现明显的聚集行为; pH7.2比较适合于胶原蛋白的聚集;而离子强度可延缓胶原蛋白的聚集,但当NaCl浓度为30和60mmol/L时,较容易形成大的聚集体。
芘荧光探针法研究了狭鳕鱼皮胶原蛋白的聚集行为,发现该胶原蛋白的聚集特性表现明显的浓度效应,存在质量浓度临界点(即临界聚集质量浓度,CAMC)。通过芘荧光探针I1/I3值与溶液中胶原蛋白质量浓度对数的关系,确定该胶原蛋白的CAMC为0.48g/L。通过测定胶原蛋白的聚集数(Nagg)发现,Nagg不是一定值,它随着质量浓度的变化而变化,在较低的胶原蛋白质量浓度下,Nagg随着质量浓度的增加而明显增加,当质量浓度达到1.2g/L时,Nagg增长缓慢。
此外,将芘荧光探针用来监测胶原凝胶的动态形成过程。在6.67%明胶溶液中,选用芘探针分子浓度为40μmol/L,以I1/I3值的变化来表征凝胶的交联情况。
6.天然植物多酚—没食子酸和芦丁用于狭鳕鱼皮凝胶的交联研究中。当没食子酸添加量为20mg/g gelatin时,凝胶的凝胶强度最大;而芦丁添加量为8 mg/g gelatin时,凝胶强度达到最大,并且具有显著性,但是二者对凝胶的凝胶点和溶胶点的影响均不显著。6mg/g gelatin和8mg/g gelatin的芦丁均使凝胶的热稳定性明显提高,热收缩温度增加了10℃,但是没食子酸对凝胶的热稳定几乎没有影响。凝胶微观结构观察发现没食子酸和芦丁均使凝胶发生了交联,以芦丁的交联现象更为明显。X—射线衍射实验表明,没食子酸和芦丁可与凝胶分子链发生相互作用。经红外光谱分析,没食子酸和芦丁主要与凝胶分子链中的C-N-C基团和羧基发生相互作用。
没食子酸和芦丁对鱼皮凝胶的溶胀性是有影响的。20和30mg/g gelatin的没食子酸以及6和8mg/g gelatin的芦丁均使凝胶的平衡溶胀度降低,以芦丁的影响更为显著。在凝胶溶胀初期,鱼皮凝胶和20mg/g gelatin没食子酸以及6和8mg/g gelatin芦丁交联的凝胶均表现非Fick扩散过程,而30mg/g gelatin的没食子酸交联凝胶表现Fick扩散过程。通过对整个溶胀过程动力学分析发现,没食子酸和芦丁均使凝胶到达平衡溶胀的时间缩短,而芦丁效果尤为明显。无论是鱼皮凝胶还是多酚交联凝胶,在溶胀过程中均是凝胶高分子链的松弛过程为速控步骤。
狭鳕鱼皮水凝胶以及多酚交联水凝胶中的水按照水凝胶的“三态水”模型可分为自由水、中间水和结合水,其中以自由水含量最高。没食子酸和芦丁的加入对凝胶的平衡水分含量没有明显影响,但可改变凝胶中可冻结水和非冻结结合水的分布。20和30mg/g gelatin的没食子酸的加入使水凝胶中非冻结结合水含量降低,而6和8mg/g gelatin的芦丁的加入却使水凝胶中非冻结结合水含量升高。
To make more effective use of underutilized resources, the distribution and morphology of collagen fiber was studied in the leftover in aquatic product processing-walleye pollock (Theragra chalcogramma) skin, from which, acid-soluble collagen was isolated to investigate the molecular structure and physical properties.
1. Histological observation clarified the presence of collagen fibre in walleye pollock skin. The results of picric acid-sirius red stain indicated that typeⅠcollagen was found in pollock skin. And electron microscopic observation revealed that skin of pollock consisted of bundles of collagen fibrils with a repeating period composed of one dark segment plus one light segment, but collagen fibrils differed in diameter.
2. Acid-soluble collagen (ASC) was successfully extracted from the skin of pollock. It was identified as typeⅠcollagen with the existence of helical arrangements of collagen. The denaturation temperature (Td) and shrinkage temperature (Ts) were 24.6℃and 47℃, respectively, both lower than those of mammalian collagens.
3. Acid-soluble collagen from pollock skin was further purified using a combination of DEAE-52 cellulose and Sephacryl S-300 HR gel filtration chromatography. The purified collagen showed a structure of filamentary fibril with helical arrangements that the distance between the molecular chains was 1.18nm, and the unit height, typical of the triple helical structure, was 0.27nm. Peptide mapping revealed that the collagen exhibited the homology with the hypothetical protein sce1263 of sporangium cellulosum‘So ce 56’with the sequence coverage of 31%.
4. Dynamic viscoelastic properties of collagen solutions with concentrations of 0.1~1.0% (w/w) were characterized by means of oscillatory rheometry at temperatures ranging from 20 to 50℃. Results showed that both storage modulus (G’) and loss modulus (G’’) increased with the increase of frequency. According to a three-zone model, dynamic modulus of collagen solutions in the studied concentrations and temperatures showed terminal-zone and plateau-zone behavior. Entanglements could be viewed when the concentration of collagen solution was higher, as well as the temperature reaching 40 and 50℃. But there were no significant entanglements in collagen solution at the temperature of 30℃. On the other hand, the functional properties of collagen from pollock skin were evaluated. Results showed that pollock skin collagen showed the better solubility and worse emulsifying activity, but its emulsion was stable.
5. Aggregation kinetics of collagen from pollock skin was studied. The main factors including mass concentration of collagen, pH value and ionic strength, which affect the aggregation property, were discussed. The results proved that the aggregation characterization of collagen was closely related to the factors mentioned above. When mass concentration of collagen was increased to 0.6g/L and above, evident aggregation behavior was found in solution. And collagen showed higher aggregation rate at pH7.2. Ionic strength slowed down the collagen aggregation, but when the NaCl concentration reaching 30 or 60mmol/L, it was easier to form large aggregates. So these factors could be considered when the aggregation property of collagen from pollock skin was studied and applied.
The aggregation behavior of collagen from pollock skin was investigated by the fluorescence probe pyrene. Results showed that the aggregation property of collagen showed mass concentration dependence, and the threshold mass concentration was found, namely the critical aggregation mass concentration (CAMC). Using plots of pyrene I1/I3 ratio versus logarithm of different mass concentration of collagen, the CAMC was found to be at 0.48g/L. The subsequent dynamic fluorescence decaying study revealed that the aggregation number of collagen was not a constant, varying with different mass concentrations. The structure of aggregates tended to be integrated, when collagen mass concentration reaching 1.2g/L and above.
The fluorescence probe pyrene was also used to monitor the dynamic gelatin formation process. The concentration of pyrene was chosen as 40μmol/L in 6.67% (w/w) gelatin from pollock skin. It was shown that the changes of I1/I3 ratio in pyrene fluorescence spectra were well related to the cross-linking of gelatin.
6. Gelatin from pollock skin was cross-linked, respectively, by the natural plant polyphenols-gallic acid and rutin. Results showed that the maximal gel strength of gelatin could be obtained when the content of gallic acid was 20mg/g gelatin, or when the content of rutin was 8mg/g gelatin, but the gelling and melting point of gelatin showed no significant increase after gallic acid or rutin added. The shrinkage temperature of gelatin was about 10℃higher with the introduction of 6mg/g gelatin and 8mg/g gelatin rutin, while there were no obvious effects on the thermal stability of gelatin with addition of 20mg/g gelatin and 30mg/g gelatin gallic acid. Scanning electron microscopy (SEM) revealed that greater cross-linking of gelatin was found after gallic acid or rutin added, but it was evident in rutin-gelatin. There were two peaks in the X-ray diffraction diagrams of gelatin with and without ingredients (gallic acid or rutin). But the distance between the molecular chains of gelatin was smaller after the addition of gallic acid or rutin, revealing that they could cross-linked with the polypeptide chains of gelatin. FTIR investigations suggested that gallic acid and rutin mainly interacted with C-N-C group and carboxyl group.
The effect of gallic acid and rutin on swelling behavior of gelatin was investigated. It was shown that the equilibrium swelling ratio decreased with the introduction of 20mg/g gelatin and 30mg/g gelatin gallic acid, as well as 6mg/g gelatin and 8mg/g gelatin rutin, but it was evident in rutin-gelatin. In the primary swelling process, the swelling behavior of gelatin with and without cross-linking agent (20mg/g gelatin gallic acid, 6mg/g gelatin and 8mg/g gelatin rutin) followed the Fick’s law of diffusion, while that of gelatin containing 30mg/g gelatin gallic acid obeyed the non-Fick’s law of diffusion. Besides, the relaxation of polypeptide chains was the rate-determining step in the whole swelling process of gelatin with and without cross-linking agents.
Differential scanning calorimetry (DSC) was employed to probe the state of water in the hydrogel, and the effect of gallic acid and rutin on the state of water was discussed. The results indicated that there were freezing free, freezing bound and nonfreezing bound water in gelatin, when the swelling equilibrium was reached. Addition of gallic acid and rutin did not show obvious effect on equilibrium water content of gelatin, but produced much effect on the distribution of frozen and non-frozen water. The non-frozen water was lower after addition of 20mg/g gelatin and 30mg/g gelatin gallic acid, while it was higher after addition of 6mg/g gelatin and 8mg/g gelatin rutin.
引文
Aguiar J., Carpena P., Molina-Bolivar J. A., et al. On the determination of the critical micelle concentration by the pyrene 1:3 ratio method. Journal of Colloid and Interface Science, 2003, 258: 116-122.
Andrew W. Textbook of Comparative Histology. New York: Oxford University Press; Gross J. Collagen. Scientific American, 1961, 204: 120-130.
Anfinsen C. B. Principles that govern the folding of the protein chains. Science, 1973, 181: 223-227
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