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Secondary Metabolites from Lichen Genus (Ramalina Ach.): Applications and Biological Activities
Published in Megh R. Goyal, Durgesh Nandini Chauhan, Assessment of Medicinal Plants for Human Health, 2020
T. R. Prashith-Kekuda, K. S. Vinayaka
Parizadeh and Garampalli71 revealed the potential of solvent extracts of R. sinensis to inhibit the activity of β-glucosidase. Ethyl acetate and methanol extracts of R. celastri were screened for inhibitory activity against pancreatic lipase. Both extracts inhibited enzyme dose dependently with marked activity shown by methanol extract.91 Ramalin isolated from the Antarctic lichen R. terebrata was shown to have tyrosinase inhibitory activity, cell-free tyrosinase activity, and intracellular tyrosinase activity. At a noncytotoxic concentration, ramalin resulted in a decrease in melanin synthesis in melan-a-cells in a dose-dependent manner. Ramalin also possesses skin brightness property.14 Zrnzevic et al.120 showed that extract of R. capitata inhibited the activity of pooled human serum cholinesterase.
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.
Antidiabetic Potential of Medicinal Mushrooms
Published in Hafiz Ansar Rasul Suleria, Megh R. Goyal, Masood Sadiq Butt, Phytochemicals from Medicinal Plants, 2019
Vivek K. Chaturvedi, Sushil K. Dubey, M.P. Singh
β-Glucosidase enzyme secreted by the epithelium of small intestine converts disaccharides and oligosaccharides into glucose. A triterpenoid lanostane, called as ganoderol B [(3β, 24E)-lanosta-7, 9(11), 24-trien-3, 26-diol] isolated from G. lucidum, is a potent inhibitor of β-glucosidase enzyme.23 Since lanostane inhibits the activity of β glucosidase, it hinders the carbohydrate digestion and prevents absorption of glucose. The in-vitro study revealed that ganoderol B has high β-glucosidase inhibition rate with an IC50 of 48.5 μg/mL (119.8 μM).
Cassava toxicity, detoxification and its food applications: a review
Published in Toxin Reviews, 2021
Anil Panghal, Claudia Munezero, Paras Sharma, Navnidhi Chhikara
Vicki et al. (1999) compared the microorganism impact on degradation of cyanogenic glycosides during fermentation. Four microorganisms were screened for their enzymatic activities; i.e. L. plantarum, Leuconostoc mesenteroides, Candida tropicalis, Penicillium sclerotiorum. The first three species showed β glucosidase activities but P. sclerotiorum was not able to exhibit degradation of any cyanogenic glycosides. The co-culture of highly active strain of L. plantarum and C. tropical showed faster degradation of linamarin compared to mono-culture. The degradation of linamarin during fermentation is due to chemical hydrolysis by weak acids of microbial fermentation. Linamarase enzymes during fermentation process act upon cyanogenic glycosides and are responsible for the detoxification of cassava. Milena et al. (2013) reported that peeling and grating of roots are done before fermentation that results in enhanced reduction in HCN. The cyanogenic glycosides are largely distributed in the cortex of the root and grating provides more surface area for fermentation and the linamarin-linamarase contact increases. The temperature variations do not have any effect on cyanogenic glycosides degradation during fermentation, there is no significant changes in HCN contents at 25 °C, 30 °C, and 35 °C. The other factor affecting HCN reduction during fermentation is the variety of cassava as the percentage of cyanogens loss in bitter type is more than in sweet type of cassava.
Deprivation of dietary fiber in specific-pathogen-free mice promotes susceptibility to the intestinal mucosal pathogen Citrobacter rodentium
Published in Gut Microbes, 2021
Mareike Neumann, Alex Steimle, Erica T. Grant, Mathis Wolter, Amy Parrish, Stéphanie Willieme, Dirk Brenner, Eric C. Martens, Mahesh S. Desai
Given the relevance of mucus erosion on pathogen-susceptibility of fiber-deprived mice in a gnotobiotic mouse model,13 we evaluated whether the increase in these potentially mucus-degrading taxa resulted in the increased activities of microbial enzymes that are involved in the degradation of host-secreted colonic mucus. We studied activities of five different enzymes in the mouse fecal samples before, and after a switch to the FF diet. Our results show a significant increase in the activities of three microbial enzymes, namely α-fucosidase, β-N-acetylglucosaminidase and sulfatase (Figure 3b), that are involved in colonic mucus degradation. Conversely, the activity of β-glucosidase, an enzyme involved in the degradation of plant glycans, was significantly decreased in the FF-fed animals.
Absorption, disposition, metabolism and excretion of [14C]mizagliflozin, a novel selective SGLT1 inhibitor, in rats
Published in Xenobiotica, 2019
Hitoshi Ohno, Yasunari Kojima, Hiroshi Harada, Yoshikazu Abe, Takuro Endo, Mamoru Kobayashi
Enzymes with β-glycosidase activity expressed in epithelial cells of the small intestine also play a role in the degradation of glycosides as well. Usually, these enzymes are responsible for the degradation of compounds such as sugar and flavonoid glycosides contained in dietary foods and supplements. Several kinds of β-glycosidase were reported to have β-glucosidase activity including lactase phlorizin hydrolase (LPH), cytosolic β-glycosidase, glucocerebrosidase and so on (Ketudat Cairns & Esen, 2010). Among these, LPH is known to hydrolyse phlorizin that is known to inhibit SGLT1 and SGLT2 non-selectively (Ehrenkranz et al., 2005). Other flavonoid or isoflavonoid glycosides, such as quercetin 3-O-β-glucoside, are also metabolised by LPH (Day et al., 2000; Németh et al., 2003). A recent study demonstrated that broad-specific β-glucosidase metabolise calycosin 7-O-β-glucoside (Shi et al., 2016). It is possible for these enzymes to metabolise mizagliflozin to its aglycone KP232. To summarise, mizagliflozin has a glucoside moiety, which is probably cleaved to form aglycone KP232 by glucosidase in the gut wall and/or that of gut microflora. KP232 is suggested to be absorbed and conjugated with glucuronic acid. KP232 glucuronide can be excreted into bile and then metabolised to KP232 in the gut again. Thus, it is possible that secondary peak occurred in rat is also observed in humans if there is no difference between rats and humans in glucosidase activity of mizagliflozin and also possibly in UDP-glucuronosyltransferase activity and biliary excretion.