Characterization of silver carp myosin glycated with phosphorylated konjac oligo-glucomannan.
Characterization of silver carp myosin glycated with phosphorylated konjac oligo-glucomannan.
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DOI:
10.1002/jsfa.11268
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发表时间:
2021-04
影响因子:
4.1
通讯作者:
Jianyou Zhang;Wei Zhou;Mingjiang Xu;Chunhua Fang;Qiwei Du;Xia Xu;Fei Lyu;Yuting Ding;
中科院分区:
文献类型:
--
作者:
Jianyou Zhang;Wei Zhou;Mingjiang Xu;Chunhua Fang;Qiwei Du;Xia Xu;Fei Lyu;Yuting Ding;
BACKGROUND Myosin (Ms) is abundant in fish meat, but it has limited application in food industry because of its low solubility and thermal stability. Our previous reports found that these functional properties of Ms can be significantly improved after glycation with konjac oligo-glucomannan (KOG). However, the effects of phosphorylated KOG (PKOG) on physico-chemical, structural and functional properties of silver carp Ms are still unknown. RESULTS This study characterized the silver carp Ms protein glycated with PKOG under 50 °C and 75% relative humidity for 48 h. As degree of phosphorylation (DP) increased, free amino content increased, whereas degree of grafting (DG) decreased. Meanwhile, isoelectric point (pI) reduced, however, PKOGs showed no differences in pI. Sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS-PAGE) analysis suggested the formation of glycoconjugates, and scanning electron microscopy (SEM) revealed thinner flakes and uneven appearance of glycoconjugates. Fourier transform infrared spectroscopy (FT-IR) indicated that the amide I, II and III bands of Ms were changed by the glycation. Ms became highly soluble in 0.5 M NaCl with the increase of phosphate addition in PKOGs. Thermal stability of Ms was effectively improved when heated at 80 °C for 60 min. CONCLUSION Glycation with appropriate PKOG might be a promising way for Ms modification due to improved solubility and thermal stability. This article is protected by copyright. All rights reserved.