China
Africa
Explore chapters and articles related to this topic
Value-Added Products and Bioactive Compounds from Fruit Wastes
Published in Megh R. Goyal, Arijit Nath, Rasul Hafiz Ansar Suleria, Plant-Based Functional Foods and Phytochemicals, 2021
Ranjay Kumar Thakur, Rahel Suchintita Das, Prashant K. Biswas, Mukesh Singh
Invertase has lower crystallinity level than sucrose, which helps in keeping products soft and fresh for long time [85]. Reddy et al. [142] studied banana waste as fermentation substrate for Aspergillus niger to produce cellulase [167]. Okafor et al. [119] investigated production of pectinolytic enzymes using Penicillium chrysogenum and Aspergillus niger. Penicillium chrysogenum produced pectinase at a level of 220.3 IU mg protein1 when pineapple peel was used as a substrate.
Antifungal Activity of Seaweeds and their Extracts
Published in Leonel Pereira, Therapeutic and Nutritional Uses of Algae, 2018
In the work by Galal et al. (2011), crude methanolic extracts of Codium fragile exhibited strong activity against most of the tested fungi (Alternaría, Botryotrichum, Fusarium, and Ulocladium species). All the tested fungi were sensitive to Nestatin (standard antibiotic), except F. oxysporium (the most resistant fungi), where the dry weight recorded from 68% to 69%, protein recorded 69% to 52%, pectinase and cellulase activity 62% to 58% of control. The most sensitive fungi were U. botrytis, where the dry weight, protein content, pectinase, and cellulase activities all were completely inhibited in cellulose and pectin media. The most active algae are the methanolic extract of C. fragile inhibited pectinase and cellulase enzymes activities for all the tested fungi except A. brassicicola and F oxysporum. This study confirms the broad antifungal effect of C. fragile using the methanolic extracts (Galal et al. 2011).
Contact Urticaria, Dermatitis, and Respiratory Allergy Caused by Enzymes
Published in Ana M. Giménez-Arnau, Howard I. Maibach, Contact Urticaria Syndrome, 2014
Stanciu Monica, Denis Sasseville
Pectinase is an enzyme that breaks down pectin from plant cell walls. It is used in fresh fruit and fruit juice processing. Glucanase and pullulanase (a subtype of glucanase), additional enzymes that hydrolyze polysaccharides, are also used in the food industry.[69] There are no reports of contact urticaria or dermatitis to these enzymes.
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
Pectinolytic enzymes or pectinases are a unique group of enzymes that catalyze the degradation of pectin, a complex heterogeneous polysaccharide (Rangarajan et al. 2010; Prathyusha and Suneetha 2011). Bacteria belonging to the genus Bacillus and Erwinia are the primary pectinase producers (Matsumoto et al. 2003). Large-scale, cost-effective production of pectinolytic enzymes involves filamentous fungi, which are among the most efficient producers of pectinases. Commercially available pectinases can be commonly acquired from A. niger, A. oryzae, Aspergillus fumigatus, Aspergillus sojae, A. awamori (Gummadi and Panda 2003), Penicillium, Fusarium, Neurospora crassa, and Mucor (Pedrolli and Carmona 2014). Pectinases present a vast range of applications in various industries, including extraction of fruits juice in the food industries (Sandri et al. 2011), scoring of cotton and ramie fabric (Sharma and Satyanarayana 2012), and fermentation of coffee and tea (Rangarajan et al. 2010; Murthy and Naidu 2011). Interestingly, pectinases have demonstrated successful application as an antibiofilm agent against several multi-drug resistant pathogens associated with various diseases (Torres et al. 2011; Coradi et al. 2018). A study conducted by Muslim et al. (2016) on S. aureus, E. coli, Enterococcus faecalis, and A. baumanni demonstrated the antibiofilm and anti-adhesive properties of pectinases. The authors suggested that pectinases would be promising in the fight against mono- and multispecies biofilms.
Colon-specific tablets containing 5-fluorouracil microsponges for colon cancer targeting
Published in Drug Development and Industrial Pharmacy, 2020
Mahmoud H. Othman, Gamal M. Zayed, Usama F. Ali, Ahmed A. H. Abdellatif
Figure 4 represents the release profile of pectin: HPMC-coated tablets containing 5-FU-Eudragit RS 100 MS. The results of in vitro drug release in pH 1.2 and 7.4 without pectinase enzyme showed no drug release in the first 5 h. After a lag time of 5 h. (Figure 3(A,B)) show the photographic images after in vitro release of HPMC-pectin-coated tablets after 2 h and after 5 h, respectively. The results showed that all tablets remain intact, while the change was observed upon pectinase enzyme addition. The drug release started at the beginning of 6 h due to the addition of the pectinase enzyme and continued up to 9 h (Figure 3(C)). These findings revealed that the pectin-HPMC combination was able to preserve cores for up to the 6 h (The period time to arrive at the colon). During this travel, the compound could be destroyed faster by the action of the pectinase enzyme and transferred into the proximal colon, the principal location of bacterial carbon metabolism. The findings then contrasted with the distal colon and the pectin may be degraded with the bacterial enzyme in the colon due to the extremely active metabolism in the proximal region.
Natural compounds and extracts as novel antimicrobial agents
Published in Expert Opinion on Therapeutic Patents, 2020
Paolo Guglielmi, Virginia Pontecorvi, Giulia Rotondi
Regarding the first object (i), extracts obtained from pectinase-treated American cranberries can be treated by means of chromatographic procedures (ii) in order to rise the concentration of: pectic oligosaccharides (modified oligomers of poly-galacturonic acid, ranging from monomers to octamers) (Figure 1);xyloglucan oligosaccharides (oligomers with degrees of polymerization from 2-mers to 10-mers, being ‘mers’ the average number of monomeric units) (Figure 1);terpene glycosides (monotropein, 6,7-dihydromonotropein or deacetylasperulosidic acid, Figure 2) compounds.