China
Africa
Explore chapters and articles related to this topic
Marine Algal Secondary Metabolites Are a Potential Pharmaceutical Resource for Human Society Developments
Published in Se-Kwon Kim, Marine Biochemistry, 2023
Somasundaram Ambiga, Raja Suja Pandian, Lazarus Vijune Lawrence, Arjun Pandian, Ramu Arun Kumar, Bakrudeen Ali Ahmed Abdul
Diabetes is one of the disorders of metabolic disorders. Many people have been affecting from this disorder. Due to the obvious growing percentage of diabetic patients and the limited number of anti-diabetic medications, the investigation for novel molecules, specifically from marine sources, has drawn great interest from the research community. Microorganisms such as cyanobacteria and actinomycetes, and marine fungi have been investigated for the anti-diabetic bioactivities. Glucosidase in bacteria enzyme is involved in the degradation of polysaccharides as well as the processing of glycoproteins and glycolipids, making it a promising target for diabetes and obesity treatments (Pandey et al., 2013). Bacteria linked with the marine sponge Aka coralliphaga produced a huge number of glucosidase inhibitors. Marine actinomycetes have produced a number of enzyme inhibitors and other useful substances (e.g., Streptomyces sp.).
Muscle Disorders
Published in Philip B. Gorelick, Fernando D. Testai, Graeme J. Hankey, Joanna M. Wardlaw, Hankey's Clinical Neurology, 2020
Kourosh Rezania, Peter Pytel, Betty Soliven
Enzyme replacement therapy (intravenous recombinant human α-glucosidase). Two brands of recombinant human α-glucosidase (Myozyme and Lumizyme) are approved by the US Food and Drug Administration, for infantile- and adult-onset acid maltase deficiency, respectively.
Gaucher disease
Published in William L. Nyhan, Georg F. Hoffmann, Aida I. Al-Aqeel, Bruce A. Barshop, Atlas of Inherited Metabolic Diseases, 2020
Recognition of Gaucher disease as a reticuloendothelial storage disease was as early as 1907 [7] and, in 1924, the stored material was identified as lipid and characterized as a cerebroside [8, 9]. Identification of the sugar in this cerebroside as glucose was reported by Aghion in 1934 in his thesis for the doctorate of philosophy (Figure 90.1) [10]. The molecular defect in glucocerebrosidase (Figure 90.2) was described in 1965, independently by Brady and colleagues [11], and by Patrick [12]. The defective enzyme is a lysosomal acid β-glucosidase, active in catalyzing the release of glucose from a number of substrates in addition to glucosylceramide. There is an activator of the enzyme, saposin C, which has a low molecular weight [13]. The gene for β-glucosidase is located on chromosome 1q21 [14]. The cDNA has been cloned and a number and variety of mutations have been identified [15–17]. The type 1 disease provides an interesting therapeutic model because enzyme replacement therapy has been quite successful [18]. Bone marrow transplantation may be curative.
α-Glucosidase inhibition by green, white and oolong teas: in vitro activity and computational studies
Published in Journal of Enzyme Inhibition and Medicinal Chemistry, 2023
Fabio Esposito, Nicolino Pala, Mauro Carcelli, Samuel T. Boateng, Paolo S. D’Aquila, Alberto Mariani, Sandro Satta, Jean Christopher Chamcheu, Mario Sechi, Vanna Sanna
The prevention of the fast breakdown of sugars, and the control of postprandial hyperglycaemia could have potential anti-diabetic effects and represents an efficient therapeutic approach to manage diabetes mellitus, especially type 21,2. α-glucosidase inhibitors moderate plasma triglycerides levels, cardiovascular disorders, and hypertension risks, reducing glucose and improving body insulin response3–5. Currently, the prescribed α-glucosidase inhibitor drugs, acarbose, miglitol or voglibose, are often associated with side effects such as diarrhoea, flatulence, and abdominal pain, which limit their long-term administration6,7. In this context, plant-based foods or dietary supplements have received particular interest as an alternative approach to α-glucosidase inhibitors due to their low cost, and relative safety, including a low incidence of gastrointestinal side effects6–9.
Antihyperglycemic effects of Lysiphyllum strychnifolium leaf extract in vitro and in vivo
Published in Pharmaceutical Biology, 2023
Arman Syah Goli, Vilasinee Hirunpanich Sato, Hitoshi Sato, Savita Chewchinda, Jiraporn Leanpolchareanchai, Jannarin Nontakham, Jantana Yahuafai, Thavaree Thilavech, Pongsatorn Meesawatsom, Metawee Maitree
Postprandial hyperglycemia is one of the main causes of diabetic complication. Suppression of glucose production from carbohydrates by the inhibition of α-glucosidase and α-amylase, and inhibition of intestinal glucose uptake are the potential strategies to inhibit glucose absorption in the small intestine (Duarte et al. 2020). To elucidate the effect of the LS extract on postprandial hyperglycemia, an OGTT model using STZ-NA-induced DM mice was employed. After pre-treatment with the LS extract at 1000 mg/kg (p.o.) for 30 min before 2 g/kg glucose loading in STZ-NA-induced DM mice, LS extract substantially retarded the elevation of blood glucose concentrations after glucose loading as compared with that of the control group. According to our in vitro results, the LS extract inhibited α-glucosidase activity with an IC50 value of 6.52 ± 0.42 μg/mL. The Lineweaver-Burk plots revealed that the LS extract inhibited α-glucosidase by a non-competitive mechanism with a Ki value of 1.32 µg/mL, which is in accordance with a previous kinetic analysis, indicating that trilobatin reversibly inhibited α-glucosidase in a non-competitive manner (He et al. 2022). This effect was stronger than that of acarbose, as positive control. However, our preliminary study found that it has no effect on α-amylase activity (data not shown). These results were corroborated by Noonong et al. (2022) who found that the isolated polyphenols from ethanol extract of LS stems exhibited more potent inhibitory effect towards α-glucosidase than that of α-amylase.
Microbially-derived cocktail of carbohydrases as an anti-biofouling agents: a ‘green approach’
Published in Biofouling, 2022
Harmanpreet Kaur, Arashdeep Kaur, Sanjeev Kumar Soni, Praveen Rishi
Cellulose, the most abundant natural biopolymer, is degraded by cellulases with β-1,4 glycoside hydrolytic activity. The cellulose plays a structural role in biofilms, provides strength, and aids in attachment, adherence, and subsequent substrate colonization (Augimeri et al. 2015). The complete degradation of cellulose requires the synergistic action of 3 kinds of cellulases, namely: (i) endoglucanases, (ii) exoglucanases, and (iii) β-glucosidases. The organisms producing cellulases are diverse, including a broad range of bacteria, fungi, and yeast (Acharya and Chaudhary 2012; Behera et al. 2017). The potential use of microbial cellulases in various industries such as the textile industry, pulp, and paper industry, brewing industry, feed and food processing industry, as well as the use of enzymes as additives in detergents have achieved global recognition (Karmakar and Ray 2011; Zhang and Zhang 2013). Moreover, the application of cellulases in biofuel production from agro-industrial waste, such as spent grain from brewers, fruit waste from citrus fruits, sugar cane bagasse, sludge, as well as municipal solid waste and kitchen waste, has become overwhelmingly important. The economic production of value-added products from lignocellulosic waste represents an exciting research area for academic and industrial research groups (Bansal et al. 2012; Rana et al. 2013).