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Assessment of Cross‐Linking in Combined Cross‐Linked Soy Protein Isolate Gels by Microbial Transglutaminase and Maillard Reaction
Author(s) -
Gan C.Y.,
Cheng L.H.,
Easa A.M.
Publication year - 2009
Publication title -
journal of food science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.772
H-Index - 150
eISSN - 1750-3841
pISSN - 0022-1147
DOI - 10.1111/j.1750-3841.2009.01053.x
Subject(s) - maillard reaction , browning , chemistry , soy protein , tissue transglutaminase , incubation , food science , lysine , ribose , biochemistry , chromatography , amino acid , enzyme
Soy protein isolate (SPI) gels were produced using single cross‐linking agents (SCLA) of microbial transglutaminase (MTG) via incubation for 5 or 24 h (SCLA‐MTG). When powdered SCLA‐MTG gels were heated for 2 h with ribose (R2) (2 g/100 mL), dark brown gels were formed, and these were designated as combined cross‐linking agent (CCLA) gels: MTG5(R2) and MTG24(R2). The results showed that the levels of Maillard‐derived browning and cross‐links of MTG5(R2) and MTG24(R2) gels were significantly ( P < 0.05) lower than a control gel produced without MTG (SCLA‐R2) even though the percentage of ribose remaining after heating of these gels was similar, indicating that a similar amount of ribose was consumed during heating. ɛ‐(γ‐glutamyl)lysine bonds formed during incubation of SPI with MTG may have reduced the free amino group of SPI to take part in the Maillard reaction; nevertheless, ribose took part in the Maillard reaction and initiated the Maillard cross‐linkings within the CCLA gels.