The Study Focused On Observation In Heat-induced Gelation Of Bovine Serum Albumin/Konjac Glucomannan Systems

Attention has been recently focused on the gelation of mixed aqueous solutions of protein and polysaccharide that lead to multicomponent biopolymer gels.Due to the complexity of process and limit in technology,there still unknown in the research up to now.This article is focused on bovine serum albumin(BSA),a globular protein,and Konjac glucomannan(KGM),which is natural and functional.To observe the microstructure of BSA,laser scanning confocal microscope(LSCM),an high resolution system,is used in this research with the staining of BSA through adding an fluorescent dye,rhodamine b.Meanwhile using the software of Matlab 7.9 is helphul to analysis the grey values in obtained pictures from LSCM.And using rheology is another way to study the gelatin in thermal process.The conclusions are as follows:1.For the only BSA solution,the influence of temperature on microstructure can be negligent from heating to cooling.80 ? is the start of the protein aggregates and the network occurs,and also is the main time of gelation.During the following procedure of cooling down,the gelation strength slightly increases until 20 °C.With the adding of calcium,the strength of gelation compared with without calcium increases.2.With the increasing of adding KGM,the connectivity of protein aggregates decreased in BSA/KGM mixed systems.Conversely,the increasing the protein concentration leads to an increased connectivity of protein aggregates.With adding of 0.1 wt%KGM,the strength of gelation increases,but the 0.25%wt KGM,0.5%wt KGM decreases the strength.Maybe the KGM contribute a phase-separation process and destroy the network of protein.While adding calcium induces the changing of gelation strength,it maybe the role of BSA and KGM change in gelation.3.We found that BSA had reacted with RHB and formed a certain new compound,the queching belonged to static fluorescence,the thermodynamic parameters were obtained.