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首页> 外文期刊>RSC Advances >Effects of deacetylation of konjac glucomannan on the physico-chemical properties of surimi gels from silver carp (Hypophthalmichthys molitrix)
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Effects of deacetylation of konjac glucomannan on the physico-chemical properties of surimi gels from silver carp (Hypophthalmichthys molitrix)

机译：Konjac Glucomannan脱乙酰化对银鲤鱼菌凝胶物理化学性质的影响（次疗法莫里斯莫里斯）

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摘要

This work studied the effects of KGM with different degrees of deacetylation (DDs) on the physicochemical properties of silver carp (Hypophthalmichthys molitrix) surimi gels. Compared with KGM, deacetylated KGM (DKGM) weakened the water-holding capacity, but increased the gel strength of surimi gels. The storage modulus (G ') and loss modulus (G '') of surimi showed an upward trend, and the aggregation rate of surimi with DKGM changed. The number of ionic bonds of mixed surimi gels increased on the whole, but those of hydrogen bonds declined; a hydrophobic interaction was the main driving force, and improved with the DDs of DKGM. FT-IR results indicated that the deacetylation of KGM had a slight influence on the secondary structure of the proteins. SDS-PAGE results showed that DKGM enhanced the intensity of the main heavy chains of myosin and actin. Examination of the network structure of the surimi gels revealed that DKGM might combine around the filaments of myofibrillar proteins like a rosary through hydrophobic interactions and hydrogen bonding. As a consequence, the myfibrillar protein aggregation was changed and the microstructures of the surimi became more compact and fibrous. The results indicated that the deacetylation of KGM led to an increase in hydrophobicity, which influenced the hydrophobic interaction of the myofibrillar proteins. As a result, the aggregation of the myofibrillar proteins was promoted and the physico-chemical properties of the surimi gel were improved.
机译：这项工作研究了KGM对不同程度的脱乙酰化（DDS）对银鲤鱼（次疗中的摩尔氏菌摩尔胶）Surimi凝胶的影响。与kgm相比，脱乙酰kgm（dkgm）削弱了水持能力，但增加了Surimi凝胶的凝胶强度。 SURIMI的储存模量（G'）和损耗模量（G''）显示出趋势的趋势，与DKGM改变的SURIMI的聚集速率。混合鱼糜凝胶的离子键数整体增加，但氢键的含量下降;疏水性相互作用是主要的驱动力，并随着DDS的DDS改善。 FT-IR结果表明，KGM的脱乙酰化对蛋白质的二级结构有轻微影响。 SDS-PAGE结果表明，DKGM增强了Myosin和Actin的主要重链的强度。考察SURIMI凝胶的网络结构显示，DKGM可以通过疏水相互作用和氢键相结合毫在毫纤维蛋白的长丝周围。因此，改变了MyFibrillar蛋白质聚集，SURIMI的微观结构变得更加紧凑和纤维化。结果表明，KGM的脱乙酰化导致疏水性增加，影响肌原纤维蛋白的疏水相互作用。结果，促进了肌原纤维蛋白的聚集，提高了Surimi凝胶的物理化学性质。

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  • 来源
    《RSC Advances》 |2019年第34期|共9页
  • 作者

    Yuan Li; Yu Jiamei; Mu Jianlou; Shi Tong; Sun Quancai; Jin Wengang; Gao Ruichang;

  • 作者单位

    Jiangsu Univ Sch Food &

    Biol Engn 301 Xuefu Rd Zhenjiang 212013 Jiangsu Peoples R China;

    Jiangsu Univ Sch Food &

    Biol Engn 301 Xuefu Rd Zhenjiang 212013 Jiangsu Peoples R China;

    Agr Univ Hebei Prov Coll Food Sci &

    Technol Baoding 071000 Hebei Peoples R China;

    Jiangsu Univ Sch Food &

    Biol Engn 301 Xuefu Rd Zhenjiang 212013 Jiangsu Peoples R China;

    Jiangsu Univ Sch Food &

    Biol Engn 301 Xuefu Rd Zhenjiang 212013 Jiangsu Peoples R China;

    Shaanxi Univ Technol Sch Biol Sci &

    Engn Bioresources Key Lab Shaanxi Prov Hanzhong 723001 Peoples R China;

    Jiangsu Univ Sch Food &

    Biol Engn 301 Xuefu Rd Zhenjiang 212013 Jiangsu Peoples R China;

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  • 正文语种 eng
  • 中图分类 化学;
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