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Precise Preparation of Functional Polysaccharides Nanoparticles by an Enzymatic Approach
Published in Raj K. Keservani, Anil K. Sharma, Rajesh K. Kesharwani, Drug Delivery Approaches and Nanosystems, 2017
Phosphorylases are the enzymes that catalyze phosphorolytic cleavage of a respective glycosidic linkage in the saccharide chain in the presence of inorganic phosphate (Pi) to produce the corresponding monosaccharide 1-phosphate and the saccharide chain with one smaller degree of polymerization (DP) (Figure 4.3) (Kitaoka and Hayashi, 2002; Nakai et al., 2013; Puchart, 2015). Because the bond energy of a phosphate ester in the monosaccharide 1-phosphate product is comparable with that of the glycosidic linkage, the reversibility of the phosphorylase-catalyzed reactions is conceived. Accordingly, phosphorylases have been employed as catalysts in the practical synthesis of saccharide chains via enzymatic glycosylations. In the reactions, monosaccharide 1-phosphates are used as glycosyl donors and the monosaccharide residue is transferred from the donor to the nonreducing end of a specific glycosyl acceptor to form a stereo- and regiocontrolled glycosidic linkage accompanied with liberating Pi. Of the phosphorylases, which have been known so far, α-glucan phosphorylase (glycogen phosphorylase, starch phosphorylase, hereafter, this enzyme is simply called ‘phosphorylase’ in this chapter) is the most extensively studied and used as a catalyst for the enzymatic preparation of polysaccharide materials based on the α(1→4)-glucan structure (Kadokawa and Kaneko, 2013; Seibel et al., 2006b).
Biodegradation of Starch
Published in Jean-Luc Wertz, Bénédicte Goffin, Starch in the Bioeconomy, 2020
Jean-Luc Wertz, Bénédicte Goffin
Several enzymes participate in the subsequent degradation of starch, including BAM, debranching enzymes, phosphoglucan phosphatases, α-amylase, disproportionating enzyme, and starch phosphorylase.13 This results in a network of reactions rather than a linear pathway (Figure 4.5).
Toxicity, metabolism, and mitigation strategies of acrylamide: a comprehensive review
Published in International Journal of Environmental Health Research, 2022
Leila Peivasteh-Roudsari, Marziyeh Karami, Raziyeh Barzegar-Bafrouei, Samane Samiee, Hadis Karami, Behrouz Tajdar-Oranj, Vahideh Mahdavi, Adel Mirza Alizadeh, Parisa Sadighara, Gea Oliveri Conti, Amin Mousavi Khaneghah
Asparagine synthetase catalyzes the ATP-dependent transfer of the amino group of glutamine to a molecule of aspartate to generate glutamate and asparagine (Halford 2018). Low AA genetically modified (GM) potato varieties have been developed by suppressing the expression of asparagine synthetase and starch phosphorylase genes of potato via genome modification and DNA transformation, which significantly decline synthesis of free asparagine and slow down starch breakdown during storage, consequently lowering the potential to form AA during cooking. A new generation of GM potatoes was produced by reduced expression of a vacuolar invertase gene, being less prone to cold sweetening (Halford et al. 2022)