Food and Fermentation Industries >

2022 , Vol. 48 >Issue 23: 209 - 216

DOI: https://doi.org/10.13995/j.cnki.11-1802/ts.030378

Preparation and characterizations of ready-to-eat reconstructed fiber surimi products

  • ZHU Shichen ,
  • FENG Yuan ,
  • LIU Shulai ,
  • ZHOU Xuxia ,
  • DING Yuting
Expand
  • 1(College of Food Science and Technology, Zhejiang University of Technology, Hangzhou 310014, China)
    2(Key Laboratory of Marine Fishery Resources Exploitment & Utilization of Zhejiang Province, Hangzhou 310014, China)
    3(National R&D Branch Center for Pelagic Aquatic Products Processing (Hangzhou), Hangzhou 310014, China)
    4(Collaborative Innovation Center of Seafood Deep Processing, Dalian Polytechnic University,Dalian 116034, China)

Received date: 2021-12-08

  Revised date: 2022-01-13

  Online published: 2023-01-05

Fold

Abstract

In this study, the optimal parameters of ready-to-eat reconstructed fiber surimi products were obtained by response surface methodology, and the thermal stabilization mechanisms were further emphasized by SDS-PAGE, fluorescence spectra, chemical force analysis and microstructure observation (SEM and HE staining). A high chewiness value (2 812.8) was found for reconstructed fiber surimi products formulated with 0.5% salt, 4.1% water and 5.7% TGase after thermal treatments. The given heating treatment induced the exploration of active groups of myofibrillar proteins and the subsequent aggregation, which was responsible for the formation of the well-order microstructure. However, the increasing temperature disrupted the homogeneous network, leading to was obvious fiber fracture. Meanwhiles, with the increase in the treatment temperature, the MHC was significantly degraded, and the thermal stability of actin was better. The high resistance to thermal degradation was supported by hydrophobic interactions and disulfide covalent bonds. This work can provide some references to the development of ready-to-eat reconstructed surimi products.

Key words： thermal stability; fiber sense; chemical force; ready-to-eat products; muscle reorganization products

Cite this article

ZHU Shichen , FENG Yuan , LIU Shulai , ZHOU Xuxia , DING Yuting . Preparation and characterizations of ready-to-eat reconstructed fiber surimi products[J]. Food and Fermentation Industries, 2022 , 48(23) : 209 -216 . DOI: 10.13995/j.cnki.11-1802/ts.030378

References

[1] ZHANG T, LI Z J, WANG Y M, et al.Effects of konjac glucomannan on heat-induced changes of physicochemical and structural properties of surimi gels[J].Food Research International, 2016, 83:152-161.
[2] NÚÑEZ-FLORES R, CANDO D, BORDERÍAS A J, et al.Importance of salt and temperature in myosin polymerization during surimi gelation[J].Food Chemistry, 2018, 239:1 226-1 234.
[3] TAKANO K, FUNAHASHI J, YAMAGATA Y, et al.Contribution of water molecules in the interior of a protein to the conformational stability[J].Journal of Molecular Biology, 1997, 274(1):132-142.
[4] ZHAO Z L, WANG Q, YAN B W, et al.Synergistic effect of microwave 3D print and transglutaminase on the self-gelation of surimi during printing[J].Innovative Food Science & Emerging Technologies, 2021, 67:102546.
[5] YANG X Q, ZHANG Y M.Expression of recombinant transglutaminase gene in Pichia pastoris and its uses in restructured meat products[J].Food Chemistry, 2019, 291:245-252.
[6] ARDIANSYAH A, SAHUBAWA L, USTADI.Restructuring steak from flakes of yellowfin tuna meat using low salt microbial transglutaminase (MTGase)[J].IOP Conference Series:Earth and Environmental Science, 2020, 404(1):012073.
[7] OLIVARES A, NAVARRO J L, SALVADOR A, et al.Sensory acceptability of slow fermented sausages based on fat content and ripening time[J].Meat Science, 2010, 86(2):251-257.
[8] 姚光明, 张猛, 刘佳彤, 等.脂代果蔬/鹿肉复合发酵香肠加工特性与工艺优化[J].肉类研究, 2014, 28(11):21-26.
YAO G M, ZHANG M, LIU J T, et al.Fermented venison sausages with added fruits and vegetables made by replacement of pork fat with vegetable oils:Processing properties and process optimization[J].Meat Research, 2014, 28(11):21-26.
[9] 蒋娅婷, 曹锦轩, 张玉林, 等.蛋白质与挥发性风味成分相互作用研究进展[J].核农学报, 2014, 28(2):285-291.
JIANG Y T, CAO J X, ZHANG Y L, et al.A proceeding of research in the interactions of protein with volatile flavor compounds[J].Acta Agriculturae Nucleatae Sinica, 2014, 28(2):285-291.
[10] LIU Y J, YU J M, ZHU J, et al.Effects of salt-induced changes in protein network structure on the properties of surimi gels:Computer simulation and digestion study[J].International Journal of Food Science & Technology, 2021, 56(8):3 914-3 923.
[11] 王雪松, 谢晶.不同冻结方式对竹荚鱼品质的影响[J].食品与发酵工业, 2020, 46(11):184-190.
WANG X S, XIE J.Effects of different freezing methods on the quality of horse mackerel[J].Food and Fermentation Industries, 2020, 46(11):184-190.
[12] 林忠武. 不同来源肌肉组织的耐煮性比较研究[D].杭州:浙江工业大学, 2016.
LIN Z W.Comparative study on the cooking tolerance of muscle tissues from different sources[D].Hangzhou:Zhejiang University of Technology, 2016.
[13] 韩静文. 鱼糜凝胶热加工特性及耐热型鱼糜肠配方研究[D].无锡:江南大学, 2018.
HAN J W.Study on thermal processing properties of surimi gels and formulation of the heat tolerant surimi sausage[D].Wuxi:Jiangnan University, 2018.
[14] BEVERIDGE T, TOMA S J, NAKAI S.Determination of sh- and ss-groups in some food proteins using ellman’s reagent[J].Journal of Food Science, 1974, 39(1):49-51.
[15] 杨珊珊. 鸡肉糜脯加工工艺以及品质改善的研究[D]. 广州:华南理工大学, 2010.
YANG S S. Study on processing technology and quality improvement of chicken minced meat[D]. Guangzhou: South China University of Technology, 2010.
[16] BLIKRA M J, JESSEN F, FEYISSA A H, et al.Low-concentration salting of cod loins:The effect on biochemical properties and predicted water retention during heating[J].LWT, 2020, 118:108702.
[17] THORARINSDOTTIR K A, ARASON S, GEIRSDOTTIR M, et al.Changes in myofibrillar proteins during processing of salted cod (Gadus morhua) as determined by electrophoresis and differential scanning calorimetry[J].Food Chemistry, 2002, 77(3):377-385.
[18] JIA R, KATANO T, YOSHIMOTO Y, et al.Effect of small granules in potato starch and wheat starch on quality changes of direct heated surimi gels after freezing[J].Food Hydrocolloids, 2020, 104:105732.
[19] FANG M X, LUO X Y, XIONG S B, et al.In vitro trypsin digestion and identification of possible cross-linking sites induced by transglutaminase (TGase) of silver carp (Hypophthalmichthys molitrix) surimi gels with different degrees of cross-linking[J].Food Chemistry, 2021, 364:130443.
[20] FANG M X, XIONG S B, YIN T, et al.In vivo digestion and absorption characteristics of surimi gels with different degrees of cross-linking induced by transglutaminase (TGase)[J].Food Hydrocolloids, 2021, 121:107007.
[21] DONG X P, PAN Y X, ZHAO W Y, et al.Impact of microbial transglutaminase on 3D printing quality of Scomberomorus niphonius surimi[J].LWT, 2020, 124:109123.
[22] 朱嵩. 基于高水分挤压技术的花生蛋白素肠制备及其贮藏特性研究[D].北京:中国农业科学院, 2019.
ZHU S.Study on preparation and storage characteristics of peanut protein sausage by high moisture extrusion[D].Beijing:Chinese Academy of Agricultural Sciences, 2019.
[23] RIBEIRO W O, OZAKI M M, DOS SANTOS M, et al.Interaction between papain and transglutaminase enzymes on the textural softening of Burgers[J].Meat Science, 2021, 174:108421.
[24] VASKOSKA R, HA M, ONG L, et al.Myosin sensitivity to thermal denaturation explains differences in water loss and shrinkage during cooking in muscles of distinct fibre types[J].Meat Science, 2021, 179:108521.
[25] VASKOSKA R, HA M, ONG L, et al.Ageing and cathepsin inhibition affect the shrinkage of fibre fragments of bovine semitendinosus, biceps femoris and psoas major during heating[J].Meat Science, 2021, 172:108339.
[26] LIU H T, WANG Z, BADAR I H, et al.Combination of high-intensity ultrasound and hydrogen peroxide treatment suppresses thermal aggregation behaviour of myofibrillar protein in water[J].Food Chemistry, 2022, 367:130756.
[27] 康怀彬, 邹良亮, 张慧芸, 等.高温处理对牛肉蛋白质化学作用力及肌原纤维蛋白结构的影响[J].食品科学, 2018, 39(23):80-86.
KANG H B, ZOU L L, ZHANG H Y, et al.Effect of high temperature treatment on chemical forces of beef proteins and structure of myofibrillar protein[J].Food Science, 2018, 39(23):80-86.
[28] QI J, ZHANG W W, FENG X C, et al.Thermal degradation of gelatin enhances its ability to bind aroma compounds:Investigation of underlying mechanisms[J].Food Hydrocolloids, 2018, 83:497-510.
[29] 周绪霞, 陈红, 陈小草, 等.谷氨酰胺转氨酶对白姑鱼鱼糜蛋白-油脂复合凝胶特性及微观结构的影响[J].中国食品学报, 2020, 20(6):106-113.
ZHOU X X, CHEN H, CHEN X C, et al.Effect of transglutaminase on properties and microstructure of surimi protein-lipids composite gels[J].Journal of Chinese Institute of Food Science and Technology, 2020, 20(6):106-113.
[30] DU X, ZHAO M N, PAN N, et al.Tracking aggregation behaviour and gel properties induced by structural alterations in myofibrillar protein in mirror carp (Cyprinus carpio) under the synergistic effects of pH and heating[J].Food Chemistry, 2021, 362:130222.
Options
Outlines

/

〈 〉

Powered by Beijing Magtech Co. Ltd,.