Effects of deacetylation of konjac glucomannan on the physico-chemical properties of surimi gels from silver carp (Hypophthalmichthys molitrix). Issue 34 (25th June 2019)

• Record Type: Journal Article
• Authors: Yuan, Li; Yu, Jiamei; Mu, Jianlou; Shi, Tong; Sun, Quancai; Jin, Wengang; Gao, Ruichang
• Is Part Of: RSC advances. Volume 9:Issue 34(2019)
• Page Start: 19828
• Page End: 19836
• Publication Date: 2019-06-25
• Subjects: Chemistry -- Periodicals; 540.5
• DOI: 10.1039/c9ra03517f
• Languages: English
• ISSNs: 2046-2069

Abstract

Abstract : This work studied the effects of KGM with different degrees of deacetylation (DDs) on the physicochemical properties of silver carp ( Hypophthalmichthys molitrix ) surimi gels. Abstract : 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.