The influence of enzymatic crosslinking by microbial transglutaminase (mTG) on the stability of casein micelles of ultrahigh temperature (UHT)-treated milk in the presence of EDTA (0-0.45 mM) or ethanol (0-74 vol%) as well as under high hydrostatic pressures up to 400 MPa was investigated. Disintegration of micelles and changes in micelle size were monitored by the measurement of turbidity as well as by dynamic light scattering. The results show that the incubation of UHTtreated milk with mTG resulted in an improved micelle stability toward disintegration on addition of EDTA, ethanol, or pressure treatment. Intramicellar formed isopetides significantly enhanced the stability of casein micelles. It is supposed that net-like crosslinks are formed within the external region of the micelles and they adopt the stabilizing role of colloidal calcium phosphate within the micelles, thus making the micelles less contestable for disrupting influences.
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http://dx.doi.org/10.1002/biot.200600232 | DOI Listing |
Int J Biol Macromol
January 2025
National R&D Center for Freshwater Fish Processing, College of Life Science, Jiangxi Normal University, Nanchang, Jiangxi, 330022, China. Electronic address:
This study investigated the progressive structural changes of fish gelatin in thermally reversible (TR) and irreversible (TI) states, formed through microbial transglutaminase (MTGase) cross-linking during in vitro gastric digestion. The focus was on dynamic structural changes and gastric digestion characteristics. Free amino content and SDS-PAGE analyses showed that both TR and TI groups were hydrolyzed into smaller fragments by pepsin during digestion.
View Article and Find Full Text PDFInt J Mol Sci
December 2024
Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Miklukho-Maklaya 16/10, 117997 Moscow, Russia.
Homogeneous antibody-drug conjugates (ADCs) exhibit significantly improved pharmacological properties compared to their heterogeneous counterparts. Site-specific conjugation of the payload to the IgG required for homogeneity can be achieved using enzymes. One example is microbial transglutaminase (MTGase), which can selectively perform transamidation on the Q295 residue of human Fc when N297 glycans are removed.
View Article and Find Full Text PDFFoods
December 2024
Department of Functional Food Product Development, Wroclaw University of Environmental and Life Sciences, 37 Chelmonskiego Str., 51-630 Wroclaw, Poland.
With growing environmental and health concerns surrounding meat consumption, meat analogs have emerged as sustainable and health-conscious alternatives. A major challenge in developing these products is replicating the fibrous, elastic texture of meat, where microbial transglutaminase (MTG) has shown significant potential. MTG catalyzes protein cross-linking, enhancing the structural integrity of meat analogs.
View Article and Find Full Text PDFACS Appl Mater Interfaces
January 2025
Department of Applied Chemistry, Graduate School of Engineering, Kyushu University, 744 Motooka, Fukuoka 819-0395, Japan.
The rising incidence of fungal infections, compounded by the emergence of severe antifungal resistance, has resulted in an urgent need for innovative antifungal therapies. We developed an antifungal protein-based formulation as a topical antifungal agent by combining an artificial lipidated chitin-binding domain of antifungal chitinase (LysM-lipid) with recently developed ionic liquid-in-oil microemulsion formulations (MEFs). Our findings demonstrated that the lipid moieties attached to LysM and the MEFs effectively disrupted the integrity of the stratum corneum in a mouse skin model, thereby enhancing the skin permeability of the LysM-lipids.
View Article and Find Full Text PDFInt J Biol Macromol
January 2025
State Key Laboratory of Food Science and Resources, Jiangnan University, Wuxi 214122, China; School of Food Science and Technology, Jiangnan University, Wuxi 214122, China. Electronic address:
In this work, six bovine bone gelatin (type B) samples with varying molecular weight (MW) fractions, comprising α-chains, high- and low-MW fractions, were prepared using ethanol precipitation and pH adjustment. The influence of molecular weight distribution (MWD) on gelatin gel strength was examined, along with the effects of these different MW fractions on microbial transglutaminase (MTGase) cross-linking gelatin. The results showed that, without MTGase treatment, high-MW fractions acted as key fillers in the formation of gelatin gel networks, while α-chains and their aggregates played a central role.
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