褐藻寡糖结合低磁场冷冻对鲢肌原纤维蛋白结构和性质的影响

丛海花; 逯晓燕; 周倩; 张紫薇; 郑志红; 刘丽; 宋关梁; 雷惠雯; 陈继伟

doi:10.12131/20220245

褐藻寡糖结合低磁场冷冻对鲢肌原纤维蛋白结构和性质的影响

doi: 10.12131/20220245

1.
苏州农业职业技术学院食品科技学院，江苏苏州 215008
2.
大连海洋大学食品科学与工程学院/辽宁省水产品加工及综合利用重点实验室，辽宁大连 116023
3.
中科荣耀 (苏州) 生物科技有限公司，江苏苏州 215152
4.
西北农林科技大学机械与电子工程学院，陕西杨凌 712100

基金项目: 国家自然科学基金青年科学基金项目 (31701630)；辽宁省教育厅2021年度高等学校基本科研项目 (LJKZ0715)；2022年青年教师科研能力提升计划 (BS〔2022〕18)

详细信息

作者简介:
丛海花 (1983—)，女，副教授，博士，研究方向为水产品加工。E-mail: hhcong@szai.edu.cn

中图分类号: TS 254.4
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- 被引次数: 0
出版历程
- 收稿日期: 2022-09-14
- 修回日期: 2022-11-03
- 录用日期: 2023-03-07
- 网络出版日期: 2023-03-31

Effect of alginate oligosaccharides combined with low magnetic field freezing on structure and properties of myofibrillar protein of silver carp

1.
College of Food Science and Technology, Suzhou Polytechnic Institute of Agriculture, Suzhou 215008, China
2.
College of Food Science and Engineering, Dalian Ocean University/Key Laboratory of Aquatic Product Processing and Utilization of Liaoning Province, Dalian 116023, China
3.
Zhongke Runyao (Suzhou) Biotechnology Co., Ltd., Suzhou 215152, China
4.
College of Mechanical and Electronic Engineering, Northwest A&F University, Yangling 712100, China

摘要

摘要: 为使以鲢 (Hypophthalmichthys molitrix) 为原料的水产预制菜在加工过程中获得良好的保鲜品质，探索了一种新的冷冻方法。研究了0.6% (w) 褐藻寡糖结合2 mT低磁场冷冻对鲢肌原纤维蛋白结构及功能的影响，以−20 ℃下无处理为空白组，在此基础上分别加入褐藻寡糖、褐藻寡糖+低磁场作为实验组，并在−30 ℃下添加褐藻寡糖作为常规冷冻组，同期冷冻鲢肌原纤维蛋白共28 d。通过测定溶解度、浊度、表面疏水性、巯基含量、热稳定性、傅里叶变换红外光谱以及内源性荧光光谱，综合比较冷冻后肌原纤维蛋白的结构和性质。结果表明：−20 ℃下的3种冷冻方式之间浊度无显著性差异；常规冷冻组蛋白质溶解度较高 (94.11%)；经褐藻寡糖+低磁场处理后，减少了疏水基团的暴露，表现出较高的总巯基质量摩尔浓度 (15 mmol·kg⁻¹)，并能减少色氨酸残基的暴露，有效保护蛋白质的三级结构；傅里叶变换红外光谱显示褐藻寡糖修饰后肌原纤维蛋白变性程度最低，α-螺旋含量较高，二级结构更加稳定。研究表明，0.6% (w) 褐藻寡糖协同低磁场处理可更好地维持鲢肌原纤维蛋白的稳定性，这为褐藻寡糖在冷冻水产品中的应用奠定了基础，并可为进一步研究低磁场冷冻提供参考。
- 鲢肌原纤维蛋白 /
- 褐藻寡糖 /
- 低磁场 /
- 冷冻
Abstract: In order to obtain good preservation quality in the processing of aquatic pre-made products with silver carp (Hypophthalmichthys molitrix) as raw material, we designed a new freezing method. We investigated the structural and functional changes of myofibrillar protein (MP) by freezing alginate oligosaccharides (AO) at a mass fraction of 0.6% with a low magnetic field (LMF) of 2 mT, and used no treatment at −20 ℃ as the blank group. On this basis, we added AO and AO+LMF as the experimental group, added AO as the common freezing (CF) group at −30 ℃, and had frozen the MP for 28 d. By measuring the solubility, turbidity, surface hydrophobicity, sulfhydryl content, thermal stability, Fourier transform infrared spectroscopy and endogenous fluorescence spectroscopy, we comprehensively compared the structure and properties of frozen MP. The results show that there were no significant differences in the turbidity among the three freezing methods at −20 ℃. The protein solubility of CF group was 94.11%. After AO+LMF treatment, the exposure of hydrophobic groups reduced, with a higher total sulfhydryl content of 15 mmol·kg⁻¹, and the exposure of tryptophan residues reduced, which protected its protein tertiary structure effectively. Fourier transform infrared spectroscopy shows that after AO modification and freezing, MP denaturation was the lowest, α-helix content was higher, and secondary structure was more stable. It it showed that 0.6% fucoidan with low magnetic field freezing treatment can better maintain the stability of MP in silver carp, which lays the foundation for the application of AO in frozen aquatic products and provides references for the further research on the low magnetic field freezing.
- Silver carp myofibrillar protein /
- Alginate oligosaccharides /
- Low magnetic field /
- Freezing

HTML全文

图 1 不同冷冻方式下肌原纤维蛋白的浊度、溶解度和表面疏水性

注：相同颜色方柱上不同字母表示组间存在显著差异(P<0.05)；图2同此。

Figure 1. Turbidity, solubility and surface hydrophobicity of myofibrillar protein with different freezing methods

Note: Different letters on the same color bars indicate significant differences among the groups (P<0.05). The same case in Fig. 2.

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图 2 不同冷冻方式下肌原纤维蛋白的巯基质量摩尔浓度

Figure 2. Sulfhydryl molality of myofibrillar protein with different freezing methods

下载: 全尺寸图片幻灯片

图 3 不同冷冻方式下肌原纤维蛋白的红外光谱图

Figure 3. Fourier transform infrared spectra of myofibrillar protein with different freezing methods

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图 4 不同冷冻方式下肌原纤维蛋白内源性荧光光谱 (a) 和最大荧光强度 (b)

注：方柱上不同字母表示组间存在显著性差异 (P<0.05)。

Figure 4. Endogenous fluorescence spectra (a) and maximum fluorescence intensity (b) of myofibrillar protein with different freezing methods

Note: Different letters on the bars indicate significant differences among the groups (P<0.05).

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表 1 不同冷冻方式下肌原纤维蛋白的热变性温度与焓值

Table 1. Thermal denaturation temperature and enthalpy of myofibrillar protein with different freezing methods

组别 Group	ΔT/℃	ΔH/(J·kg⁻¹)
空白组 Blank group	55.24±0.97^b	6.5±2.8^a
褐藻寡糖 AO	52.42±3.64^bc	3.7±2.7^ab
褐藻寡糖+低磁场 AO+LFM	69.24±2.46^a	2.3±1.2^b
常规冷冻 CF	49.84±2.29^c	1.6±0. 2^b
注：不同字母表示不同处理间差异显著 (P<0.05)；后表同此。 Note: Different letters indicate significant differences (P<0.05). The same case in the following table.

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表 2 不同冷冻方式下肌原纤维蛋白的二级结构变化

Table 2. Change in secondary structure of myofibrillar protein with different freezing methods %

组别 Group	α-螺旋 α-helix	β-折叠 β-sheet	β-转角 β-turn	无规卷曲 Random coil
空白组 Blank group	21.78±0.03^ab	23.54±0.08^a	35.14±0.05^a	19.54±0.00^a
褐藻寡糖 AO	31.65±0.06^a	28.12±0.14^a	30.88±0.08^a	9.35±0.16^a
褐藻寡糖+低磁场 AO+LFM	13.90±0.12^b	29.63±0.05^a	34.04±0.03^a	22.43±0.07^a
常规冷冻 CF	23.85±0.02^ab	31.37±0.08^a	33.05±0.01^a	11.73±0.10^a

下载: 导出CSV

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