1985
DOI: 10.1080/00021369.1985.10867087
|View full text |Cite
|
Sign up to set email alerts
|

Gelation of Casein and Soybean Globulins by Transglutaminase

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
1
1
1
1

Citation Types

2
36
0

Year Published

1986
1986
2009
2009

Publication Types

Select...
9
1

Relationship

3
7

Authors

Journals

citations
Cited by 33 publications
(40 citation statements)
references
References 7 publications
2
36
0
Order By: Relevance
“…Polyacrylamide gel electrophoresis (PAGE) was carried out on a slab gel in the presence of SDS, as previously described 2 ) The isoelectric points were obtained by isoelectric focusing using Pharmalyte pH 3 ~ 10 (Pharmacia Co.)…”
Section: Methods Of Purificationmentioning
confidence: 99%
“…Polyacrylamide gel electrophoresis (PAGE) was carried out on a slab gel in the presence of SDS, as previously described 2 ) The isoelectric points were obtained by isoelectric focusing using Pharmalyte pH 3 ~ 10 (Pharmacia Co.)…”
Section: Methods Of Purificationmentioning
confidence: 99%
“…TG can modify proteins by catalyzing acyl transfer between a l-carboxyamide of a peptide/protein bound glutamine and lysine forming an E-(l-glutamyl) lysine [E-(l-Glu)Lys] cross-link (Kuraishi, Yamazaki, & Susa, 2001). TG catalyzes conversion of soluble proteins to insoluble high-molecularweight polymers through formation of covalent crosslinks (Motoki, Aso, Seguro, & Nino, 1987;Nino, Motoki, & Takinami, 1985). This cross-linking results in the polymerization of protein/peptide molecules with a subsequent increase in molecular mass.…”
Section: Soy Proteinsmentioning
confidence: 99%
“…Transglutaminase and proteases have been successfully used for industrial applications (Nio et al, 1985;Motoki et al, 1986). In contrast, most chemical modifications have not been used for food applications, because of the potential health hazard or the appearance of detrimental products.…”
Section: Introductionmentioning
confidence: 99%