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Bioactive Compounds in agricultural and Food production Waste
Published in Quan V. Vuong, Utilisation of Bioactive Compounds from Agricultural and Food Waste, 2017
Nenad Naumovski, Senaka Ranadheera, Jackson Thomas, Ekavi Georgousopoulou, Duane Mel lor
Vegetable-based food commodities, such as onion (Allium cepa L., Alliaceae) waste, which includes brown skin, the outer two fleshy leaves and the top and bottom bulbs (Schieber et al. 2001, Turner et al. 2006), potato peel (Reyes et al. 2005), lettuce and collard leaves (Young et al. 2005), cabbage (Brassica) leaves (Nielsen et al. 1993), pumpkin varieties, such as Curcubita pepo (Iheanacho and Udebuani 2009) and pericarp of red pepper fruit (Capsicum annuum L.) (Materska and Perucka 2005) have also been used in recovering glycosides. Various other agricultural and food production wastes including cottonseed as a by-product (Piccinelli et al. 2007), defatted soybean (Nemitz et al. 2015), tea leaves (Wan et al. 2009), almond hulls (Prunus amygdalus) (Sang et al. 2002), industrial horse chestnut (Aesculus hippocastanum) waste (Kapusta et al. 2007), green barley (Hordeum vulgare L.) leaves (Kitta et al. 1992) and seed coat of lentils (Dueñas et al. 2002) and beans (Madhujith et al. 2004, Shahidi and Ambigaipalan 2015) are recognized as natural sources of glucosides.
Sodium-glucose transporter (SGLT2) inhibition: A potential target for treatment of type-2 Diabetes Mellitus with Natural and Synthetic compounds
Published in Egyptian Journal of Basic and Applied Sciences, 2023
Shubham Batra, Prabhjeet Kaur Bamrah, Manjusha Choudhary
Phlorizin, an O-glucoside dihydrochalcone molecule, was initially isolated from apple tree bark discovered in 1835 and has been found to improve healthy individuals’ excretion of glucose in urine [9]. Phlorizin was discovered to have the potential to block both SGLT1 and SGLT2 sodium-glucose cotransporters, however, it has not been developed as an antihyperglycemic medication for usage in humans due to its poor bioavailability and GIT side effects like diarrhea, dehydration, and malabsorption by inhibiting SGLT1(in the small intestine) [10]. Keeping in view the adverse effects, phlorizin was deemed unsuitable for continued research as an antihyperglycemic drug. Phlorizin derivates with more focused SGLT2 inhibition (Table 1), were created to prevent SGLT1-dependent side effects [8]
Engineering Trichoderma reesei for the hyperproduction of cellulose induced protein 1 (Cip1) on a sophorose-containing inducer to efficiently saccharify alkali-pretreated corn stover
Published in Preparative Biochemistry & Biotechnology, 2023
Jianghong Li, Yudian Chen, Yushan Gao, Yi Mo, Tingting Long, Bo Yao, Yonghao Li
After fermentation of wild-type T. reesei and two recombinant strains with MGD as an inducer for 48 and 60 h, the FPA (Figure 3A), endoglucanase activity (Figure 3B), cellobiohydrolase activity (Figure 3C), β-glucosidase activity (Figure 3D), and protein concentration (Figure 3E) were analyzed. According to the results, the activity of the four glucoside hydrolases and secreted protein were not improved after overexpression of Trcip1, consistent with the qPCR results (Figures 2A,B) and with the finding that CIP1 has no glycoside hydrolase activity.[24] When APCS was used as an inducer, the results were similar to those of MGD (Figure S1). Overexpression of the CIP1 gene had no significant effect on the activities of the above four enzymes and secreted protein, further indicating that CIP1 has no glycosidic hydrolase activity.
An effective immobilization of β-glucosidases by partly cross-linking enzyme aggregates
Published in Preparative Biochemistry & Biotechnology, 2022
Yuefeng Deng, Jie Ouyang, Hu Liu, Jianjun Wang, Yihui Zhu, Ziqian Chen, Chengli Yang, Dali Li, Kefeng Ma
As a kind of glycoside hydrolase, the β-glucosidase (EC 3.2.1.21) can hydrolyze β-D-glucoside existing in non-reducing end of carbohydrate to produce β-D-glucose.[1] It is widely distributed in nature.[2,3] Beta-glucosidase have been used in many fields, e.g., production of bioethanol by degrading cellulose,[4] biotransformation of soybean isoflavone[5] and as flavor enhancer.[6] However, industrial applications of β-glucosidase are still limited due to its low stability under harsh conditions, high cost and difficulty in recycling. Enzyme immobilization can effectively overcome these obstacles. Immobilization of β-glucosidase on different carriers can improve its operational stability and achieve good recyclability.[7–10]