The enzymatic degradation of thermal treated alpha-glucans with amylolytic enzymes depends on the reaction environment (T, pH, moisture), the degree of polymerisation (DP) and the branch of the substrates as well as on the presence of amino compounds. The chemical changes of the alpha-glucans due to thermolysis at 180 degrees C are characterized by means of the amount of reducing substances and the amount of maltooligosaccharides (HPLC). In general the enzymatic degradability of the thermal treated alpha-glucans is decreased with increasing time of thermolysis, temperature and moisture content. The enzyme activity with the thermal treated alpha-glucans is diminished in the same way. The addition of amino compounds reduces the enzymatic degradability only at the beginning of the reaction. With increasing time of thermolysis the thermolysates without glycine addition are hardly degraded. As reason for these differences in the enzymatic degradation transglycosylation and non-enzymatic browning reactions (caramalisation/Maillard-reaction) are assumed.

Download full-text PDF

Source
http://dx.doi.org/10.1007/BF01231079DOI Listing

Publication Analysis

Top Keywords

enzymatic degradation
12
thermal treated
12
treated alpha-glucans
12
amylolytic enzymes
8
amino compounds
8
enzymatic degradability
8
increasing time
8
time thermolysis
8
enzymatic
5
alpha-glucans
5

Similar Publications

Background: Androgenic anabolic steroids (AASs) are synthetic drugs structurally related to testosterone, with the ability to bind to androgen receptors. Their uncontrolled use by professional and recreational sportspeople is a widespread problem. AAS abuse is correlated with severe damage to the cardiovascular system, including changes in homeostasis and coagulation disorders.

View Article and Find Full Text PDF

Acute lung injury (ALI) is a severe respiratory disease with high mortality, mainly due to overactivated oxidative stress and subsequent pyroptosis. Mesencephalic astrocyte-derived neurotrophic factor (MANF), an inducible secretory endoplasmic reticulum (ER) stress protein, inhibits lipopolysaccharide (LPS)-induced acute lung injury (ALI). However, the exact molecular mechanism remains unclear.

View Article and Find Full Text PDF

Enterovirus-D68 (EV68) continues to present as a global health issue causing respiratory illness and outbreaks associated with long-lasting neurological disease, with no antivirals or specific treatment options. The development of antiviral therapeutics, such as small-molecule inhibitors that target conserved proteins like the enteroviral 3C protease, remains to be achieved. While various 3C inhibitors have been investigated, their design does not consider the potential emergence of drug resistance mutations.

View Article and Find Full Text PDF

Emerging Roles of TRIM56 in Antiviral Innate Immunity.

Viruses

January 2025

Department of Microbiology, Immunology and Biochemistry, University of Tennessee Health Science Center, Memphis, TN 38163, USA.

The tripartite-motif protein 56 (TRIM56) is a RING-type E3 ubiquitin ligase whose functions were recently beginning to be unveiled. While the physiological role(s) of TRIM56 remains unclear, emerging evidence suggests this protein participates in host innate defense mechanisms that guard against viral infections. Interestingly, TRIM56 has been shown to pose a barrier to viruses of distinct families by utilizing its different domains.

View Article and Find Full Text PDF

L-Threonine-Derived Biodegradable Polyurethane Nanoparticles for Sustained Carboplatin Release.

Pharmaceutics

December 2024

Department of Polymer Science and Engineering, Pusan National University, Busan 46241, Republic of Korea.

The use of polymeric nanoparticles (NPs) in drug delivery systems offers the advantages of enhancing drug efficacy and minimizing side effects; In this study, L-threonine polyurethane (LTPU) NPs have been fabricated by water-in-oil-in-water emulsion and solvent evaporation using biodegradable and biocompatible LTPU. This polymer was pre-synthesized through the use of an amino acid-based chain extender, desaminotyrosyl L-threonine hexyl ester (DLTHE), where urethane bonds are formed by poly(lactic acid)-poly(ethylene glycol)-poly(lactic acid) (PLA-PEG-PLA) triblock copolymer and 1,6-hexamethylene diisocyanate (HDI). LTPU is designed to be degraded by hydrolysis and enzymatic activity due to the presence of ester bonds and peptide bonds within the polymer backbone.

View Article and Find Full Text PDF

Want AI Summaries of new PubMed Abstracts delivered to your In-box?

Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!