Effect of Temperatures during the Lye Macerating on the Structure of Tripe Collagen

WANG Liyu; XIA Yangyi; ZHAO Luan

doi:10.13386/j.issn1002-0306.2021080119

Volume 43 Issue 9

Apr. 2022

Turn off MathJax

Article Contents

Abstract

References

Science and Technology of Food Industry > 2022 > 43(9): 56-62. > DOI: 10.13386/j.issn1002-0306.2021080119

WANG Liyu, XIA Yangyi, ZHAO Luan. Effect of Temperatures during the Lye Macerating on the Structure of Tripe Collagen[J]. Science and Technology of Food Industry, 2022, 43(9): 56−62. (in Chinese with English abstract). doi: 10.13386/j.issn1002-0306.2021080119.

Citation:

PDF (6072 KB)

Effect of Temperatures during the Lye Macerating on the Structure of Tripe Collagen

WANG Liyu^1,,
XIA Yangyi^{1, 2, ,},
ZHAO Luan¹

1.
College of Food Science, Southwest University, Chongqing 400700, China
2.
Chongqing Special Food Programme and Technology Research Center, Chongqing 400700, China

More Information

Received Date: August 11, 2021
Available Online: March 08, 2022

Graphical Abstract

Abstract

Abstract

In this paper, acidase compound method was used to extract collagen from tripe. The effects of NaOH rising temperature (40~60 ℃) on collagen structure of tritrium hairy were analyzed by UV spectrophotometer, fluorescence spectrophotometer, infrared spectrometer and scanning electron microscope. The results showed that the the lye macerating of tripe could decrease the UV absorption intensity of collagen in tribolus. With the increase of temperature during the lye macerating of tripe, the fluorescence intensity of collagen decreased and the content of sulfhydryl group increased. It indicated that heating treatment will gradually deepen the degeneration degree of collagen and eventually complete degeneration. When the temperature was 60 ℃, the surface hydrophobicity of tribolus collagen decreased. With the increase of temperature during the lye macerating of tripe, the microstructure of collagen of tripe showed that collagen molecules shrunk, gradually curled, accelerate agglutination, gap decrease and flake collagen was broken. Therefore, NaOH can destroy the secondary structure of collagen in tripe, presenting as fracture, fragmentation, stretching and loosening, and different temperature of hyperplasia has a significant impact on the structure of collagen.
- tripe,
- collagen,
- temperature,
- protein structure characterization

FullText(HTML)

References (29)

References

[1]	李凛, 李璟, 周世一, 等. 5种不同发制方式对毛肚增重和感官品质的影响[J]. 广东农业科学,2011,38(23):102−103, 113. [LI L, LI J, ZHOU S Y, et al. Effects of 5 different hair treatments on weight gain and sensory quality of hairy belly[J]. Guangdong Agricultural Sciences,2011,38(23):102−103, 113. doi: 10.3969/j.issn.1004-874X.2011.23.034
[2]	贾洪锋, 张淼, 邓红, 等. 加热对毛肚品质的影响[J]. 食品工业科技,2017,38(20):166−170. [JIA H F, ZHANG M, DENG H, et al. The effect of heating on the quality of hairy belly[J]. Food Industry Science and Technology,2017,38(20):166−170.
[3]	李凛, 李璟, 周世一, 等. 响应面法优化水发工艺参数改善毛肚感官品质[J]. 食品研究与开发,2012,33(1):80−84. [LI L, LI J, ZHOU S Y, et al. Response surface methodology to optimize water flood process parameters to improve the sensory quality of tripe[J]. Food Research and Development,2012,33(1):80−84. doi: 10.3969/j.issn.1005-6521.2012.01.023
[4]	陈玉茹, 杨静, 黄苏红, 等. 毛肚涨发工艺优化及其水分分布和组织结构变化研究[J]. 食品工业科技,2020,41(18):157−163, 169. [CHEN Y R, YANG J, HUANG S H, et al. Study on optimization of collagen swelling process and its water distribution and tissue structure changes[J]. Food Industry Science and Technology,2020,41(18):157−163, 169.
[5]	王哲平, 刘淇, 曹荣, 等. 温度对刺参胶原蛋白结构和分子量变化的影响[J]. 渔业科学进展,2011,32(6):80−84. [WANG Z P, LIU Q, CAO R, et al. The effect of temperature on changes in the structure and molecular weight of sea cucumber collagen[J]. Progress in Fishery Sciences,2011,32(6):80−84. doi: 10.3969/j.issn.1000-7075.2011.06.013
[6]	李朝阳, 李良玉, 刁静静. pH和温度对蛋白结构和功能特性影响的研究进展[J]. 科学技术创新,2019(18):59−60. [LI C Y, LI L Y, DIAO J J. Research progress on the effects of pH and temperature on protein structure and functional properties[J]. Science and Technology Innovation,2019(18):59−60. doi: 10.3969/j.issn.1673-1328.2019.18.034
[7]	王正雯, 田宏伟, 周富裕, 等. 加热温度对麻鸭肌原纤维蛋白结构与凝胶特性的影响[J]. 食品科学,2020,41(13):61−68. [WANG Z W, TIAN H W, ZHOU F Y, et al. The effect of heating temperature on the structure and gel properties of myofibrillar protein in ducks[J]. Food Science,2020,41(13):61−68. doi: 10.7506/spkx1002-6630-20191128-280
[8]	李清正, 张顺亮, 罗永康, 等. 温度对复合肌原纤维蛋白结构及其表面疏水性的影响[J]. 肉类研究,2017,31(2):6−10. [LI Q Z, ZHANG S L, LUO Y K, et al. The effect of temperature on the structure of composite myofibril protein and its surface hydrophobicity[J]. Meat Research,2017,31(2):6−10. doi: 10.7506/rlyj1001-8123-201702002
[9]	高昕, 刘莲凤, 刘倩, 等. 不同加热温度下刺参肌肉组织与胶原纤维结构的变化[J]. 水产学报,2012,36(9):1465−1472. [GAO X, LIU L F, LIU Q, et al. Changes in the structure of sea cucumber muscle tissue and collagen fibers under different heating temperatures[J]. Journal of Fisheries of China,2012,36(9):1465−1472. doi: 10.3724/SP.J.1231.2012.27937
[10]	李凛, 李璟, 周世一. 毛肚水发工艺的响应面法优化[J]. 湖北农业科学,2012,51(10):2092−2095. [LI L, LI J, ZHOU S Y, et al. Optimization of the collagen water hair process by response surface methodology[J]. Hubei Agricultural Sciences,2012,51(10):2092−2095. doi: 10.3969/j.issn.0439-8114.2012.10.040
[11]	赵鸾, 夏杨毅, 王立宇, 等. 鲜毛肚和盐渍毛肚胶原蛋白的结构表征[J/OL]. 食品与发酵工业: 1-9 2021-09-25]. https: //doi. org/10.13995/j. cnki. 11-1802/ts. 026755. ZHAO L, XIA Y Y, WANG L Y, et al. Structural characterization of fresh and salted collagen collagen[J/OL]. Food and Fermentation Industry: 1-9[2021-09-25].https://doi.org/10.13995/j.cnki.11-1802/ts.026755.
[12]	曲文娟, 宋雅婷, 张欣欣, 等. 胶原蛋白-壳聚糖膜的制备及其对猪肉的保鲜作用[J]. 现代食品科技,2020,36(3):89−98. [QU W J, SONG Y T, ZHANG X X, et al. Preparation of collagen-chitosan film and its fresh-keeping effect on pork[J]. Modern Food Science and Technology,2020,36(3):89−98.
[13]	庄永亮. 海蜇胶原蛋白理化性质及其胶原肽的护肤活性研究[D]. 青岛: 中国海洋大学, 2009. ZHUANG Y L. The physical and chemical properties of jellyfish collagen and the skin care activity of collagen peptides [D]. Qingdao: Ocean University of China, 2009.
[14]	LI S, YU Q. Extraction and characterization of collagens from yak rumen smooth muscle[J]. Animal Science Journal,2019,90(12):1581−1589. doi: 10.1111/asj.13296
[15]	NOORZAI S, VERBEEK C J R, LAY M C, et al. Collagen extraction from various waste bovine hide sources[J]. Waste and Biomass Valorization,2020,11(11):5687−5698. doi: 10.1007/s12649-019-00843-2
[16]	DISIMPLICIO P, CHEESEMAN K H, SLATER T F. The reactivity of the sh-group of bovine serum-albumin with free-radicals[J]. Free Radical Research Communications,1991,14(4):253−262. doi: 10.3109/10715769109088954
[17]	LI P H, LU W C, CHAN Y J, et al. Extraction and characterization of collagen from sea cucumber (Holothuria cinerascens) and its potential application in moisturizing cosmetics[J]. Aquaculture,2020,515(15):734590.
[18]	CHEN S, TANG L, HAO G, et al. Effects of alpha(1)/alpha(2) ratios and drying temperatures on the properties of gelatin films prepared from tilapia (Tilapia zillii) skins[J]. Food Hydrocolloids,2016,52:573−580. doi: 10.1016/j.foodhyd.2015.07.026
[19]	VASANTHI C, VENKATARAMANUJAM V, DUSHYANTHAN K. Effect of cooking temperature and time on the physico-chemical, histological and sensory properties of female carabeef (buffalo) meat[J]. Meat Science,2007,76(2):274−280. doi: 10.1016/j.meatsci.2006.11.018
[20]	VIDAL A R, DUARTE L P, SCHMIDT M M, et al. Extraction and characterization of collagen from sheep slaughter by-products[J]. Waste Management,2020,102:838−846. doi: 10.1016/j.wasman.2019.12.004
[21]	马明思. 兔皮胶原快速明胶化机理及明胶制备过程中胶原结构变化[D]. 重庆: 西南大学, 2018. MA M S. The rapid gelatinization mechanism of rabbit skin collagen and the change of collagen structure during the preparation of gelatin[D]. Chongqing: Southwest University, 2018.
[22]	BHUIMBAR M V, BHAGWAT P K, DANDGE P B. Extraction and characterization of acid soluble collagen from fish waste: Development of collagen-chitosan blend as food packaging film[J]. Journal of Environmental Chemical Engineering,2019,7(2):102983. doi: 10.1016/j.jece.2019.102983
[23]	BERISIO R, VITAGLIANO L, MAZZARELLA L, et al. Crystal structure of the collagen triple helix model (Pro-Pro-Gly)(10) (3)[J]. Protein Science,2002,11(2):262−270.
[24]	ZIMM B H, BRAGG J K. Theory of the phase transition between helix and random coil in polypeptide chains[J]. Journal of Chemical Physics,1959,31(2):526−535. doi: 10.1063/1.1730390
[25]	PRYSTUPA D A, DONALD A M. Infrared study of gelatin conformations in the gel and sol states[J]. Polymer Gels and Networks,1996,4(2):87−110. doi: 10.1016/0966-7822(96)00003-2
[26]	CHYS P, GIELENS C, MEERSMAN F. FTIR 2D correlation spectroscopy of alpha(1) and alpha(2) fractions of an alkali-pretreated gelatin[J]. Biochimica Et Biophysica Acta-Proteins and Proteomics,2011,1814(2):318−325. doi: 10.1016/j.bbapap.2010.10.003
[27]	文鹏程, 余丹丹, 汪昕昕, 等. 不同处理条件对乳铁蛋白构象的影响研究[J]. 光谱学与光谱分析,2012(1):162−165. [WEN P C, YU D D, WANG X X, et al. The effect of different treatment conditions on the conformation of lactoferrin[J]. Spectroscopy and Spectral Analysis,2012(1):162−165. doi: 10.3964/j.issn.1000-0593(2012)01-0162-04
[28]	VETRI V, LIBRIZZI F, LEONE M, et al. Thermal aggregation of bovine serum albumin at different pH: Comparison with human serum albumin[J]. European Biophysics Journal with Biophysics Letters,2007,36(7):717−725. doi: 10.1007/s00249-007-0196-5
[29]	徐永霞, 王瑞, 李学鹏, 等. 热处理对鱼肌原纤维蛋白结构及腥味物质结合能力的影响[J]. 中国食品学报,2020,20(9):131−138. [XU Y X, WANG R, LI X P, et al. Effects of heat treatment on the structure of fish myofibril protein and the binding ability of fishy substances[J]. Chinese Journal of Food Science,2020,20(9):131−138.

Supplements (0)

Cited By

Cited by

Periodical cited type(5)

1.	赵斌，李娣娣，袁源，韦婷. 发酵型功能酒的现代研究进展. 酿酒. 2025(02): 43-49 .
2.	陈乙源，洪嘉欣，黄河，王硕，武亚帅，赵东瑞，孙金沅，黄明泉，孙啸涛. 基于GC×GC-MS分析不同等级浓香型白酒的关键风味化合物. 中国酿造. 2025(03): 29-35 .
3.	舒翔，邱奇琦. 果酒降酸专利技术分析. 安徽农学通报. 2024(04): 97-101 .
4.	廖娟，李嘉宇，黄杰惠，陈博慧，杨涛. 耐低温酵母的分离鉴定及对低温酿造米酒品质的影响. 食品工业科技. 2024(07): 159-166 . 本站查看
5.	王爱灵，张梅，申娜娜，徐梦文，章骏伟，李瑞龙，兰伟. 黑果腺肋花楸果酒生产工艺研究进展. 滁州学院学报. 2024(02): 21-28 .