Detailed kinetic model describing new oligosaccharides synthesis using different β-galactosidases.
نویسندگان
چکیده
The production of prebiotic galactooligosaccharides (GOS) from lactose has been widely studied whereas the synthesis of new prebiotic oligosaccharides with improved properties as those derived from lactulose is receiving an increasing interest. Understanding the mechanism of enzymatic oligosaccharides synthesis from lactulose would help to improve the quality of the products in a rational way as well as to increase the production efficiency by optimally selecting the operating conditions. A detailed kinetic model describing the enzymatic transgalactosylation reaction during lactulose hydrolysis is presented here for the first time. The model was calibrated with the experimental data obtained in batch assays with two different β-galactosidases at various temperatures and concentrations of substrate. A complete system identification loop, including model selection, robust estimation of the parameters by means of a global optimization method and computation of confidence intervals was performed. The kinetic model showed a good agreement between experimental data and predictions for lactulose conversion and provided important insights into the mechanism of formation of new oligosaccharides with potential prebiotic properties.
منابع مشابه
Synthesis of Oligosaccharides Derived from Lactulose (OsLu) Using Soluble and Immobilized Aspergillus oryzae β-Galactosidase
β-Galactosidase from Aspergillus oryzae offers a high yield for the synthesis of oligosaccharides derived from lactulose (OsLu) by transgalactosylation. Oligosaccharides with degree of polymerization (DP) ≥ 3 have shown to possess higher in vitro bifidogenic effect than di- and tetrasaccharides. Thus, in this work, an optimization of reaction conditions affecting the specific selectivity of A. ...
متن کاملRecombinant microbial systems for improved β-galactosidase production and biotechnological applications.
β-Galactosidases (EC 3.2.1.23) constitute a large family of proteins that are known to catalyze both hydrolytic and transgalactosylation reactions. The hydrolytic activity has been applied in the food industry for decades for reducing the lactose content in milk, while the transgalactosylation activity has been used to synthesize galacto-oligosaccharides and galactose containing chemicals in re...
متن کاملSynthesis of UDP-activated Oligosaccharides with Commercial β- galactosidase from Bacillus circulans under Microwave Irradiation
We report here on the synthesis of nucleotide activated oligosaccharides by transglycosylation with β-galactosidase from Bacillus circulans applying microwave irradiation (MWI) and conventional heating. The presented prod cts could serve as novel inhibitors or donor substrates of Leloir-glycosyltransferases. Some of them have been isolated from human milk but the biological role remains unclear...
متن کاملAnalysis of Domain Architecture and Phylogenetics of Family 2 Glycoside Hydrolases (GH2)
In this work we report a detailed analysis of the topology and phylogenetics of family 2 glycoside hydrolases (GH2). We distinguish five topologies or domain architectures based on the presence and distribution of protein domains defined in Pfam and Interpro databases. All of them share a central TIM barrel (catalytic module) with two β-sandwich domains (non-catalytic) at the N-terminal end, bu...
متن کاملIn Situ Random Microseeding and Streak Seeding Used for Growth of Crystals of Cold-Adapted -d-Galactosidases: Crystal Structure of DG from Arthrobacter sp. 32cB
There is an increasing demand for cold-adapted enzymes in a wide range of industrial branches. Nevertheless, structural information about them is still scarce. The knowledge of crystal structures is important to understand their mode of action and to design genetically engineered enzymes with enhanced activity. The most difficult task and the limiting step in structural studies of cold-adapted ...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید
ثبت ناماگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید
ورودعنوان ژورنال:
- Journal of biotechnology
دوره 153 3-4 شماره
صفحات -
تاریخ انتشار 2011