Fungal β‐1,3‐1,4‐glucanases: production, proprieties and biotechnological applications

Abstract

β‐1,3‐1,4‐glucanases (or lichenases; EC 3.2.1.73) comprise one of the main enzymes used in industry during recent decades. These enzymes hydrolyze β‐glucans containing β‐1,3 and β‐1,4 linkages, such as cereal β‐glucans and lichenan. The β‐1,3‐1,4‐glucanases are produced by a variety of bacteria, fungi, plants and animals. A large number of microbial β‐1,3‐1,4‐glucanases have potential application in industrial processes, such as feed, food and detergent industries. The present review summarizes the available studies with respect to β‐1,3‐1,4‐glucanases production conditions, enzyme biochemical properties and potential industrial application. © 2018 Society of Chemical Industry

Stachybotrys chartarum—A Hidden Treasure: Secondary Metabolites, Bioactivities, and Biotechnological Relevance

“…β -Glucans comprise glucose polymers heterogeneous group, including lichenan (β-1,4-1,3-glucan), cellulose (β-1,4-glucan), β-1,3(4)-glucan, and laminarin (β-1,3-glucan). Their hydrolysis is catalyzed by various kinds of β -glucanases, such as lichenases, cellulases, laminarinases, and β -1,3(4)-glucanases [ 51 ]. Lichenases are produced by various microorganisms, including fungi and bacteria, and have remarkable applications in detergent, food, feed, brewing, and wine industries as well as biodiesel and bioethanol production [ 51 ].…”

“…Their hydrolysis is catalyzed by various kinds of β -glucanases, such as lichenases, cellulases, laminarinases, and β -1,3(4)-glucanases [ 51 ]. Lichenases are produced by various microorganisms, including fungi and bacteria, and have remarkable applications in detergent, food, feed, brewing, and wine industries as well as biodiesel and bioethanol production [ 51 ]. The expression of the gene Cel12A isolated from rotting cellulose rag-associated- S. chartarum by Picart et al was triggered by rice straw than 0.1% glucose or 1% lactose [ 52 , 53 ].…”

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“…Целевым (и одновременно репортерным) белком в исследовании служила 1,3-1,4-β-глюканаза Rhizomucor miehei [13][14][15], названная Bgl3. Интерес к биосинтезу Bgl3 в дрожжах K. kurtzmanii был связан с физико-химическими свойствами этого фермента [13][14][15], определяющими высокий потенциал его промышленного использования [13,16] Базовым вектором экспрессии служил pPH93-AOX1 Y727 [11]. Вектор экспрессии, содержавший клонированный ген белка Bgl3, был назван pPH727-AOX727.…”

Orthogonal Active-Site Labels for Mixed-Linkage endo-β-Glucanases

“…53 In addition to their biological importance in carbohydrate metabolism, 28,35,42,43,54 MLGases have numerous biotechnological applications in biomass transformation to high-value products, in animal feed treatment to improve digestibility, in brewing to reduce mash viscosity, and for the preparation of defined prebiotics. [36][37][38]43,47,55,56 Despite a long history of enzymological characterization, 43 including using bespoke aryl glycoside substrates, 57−59 there are few specific inhibitors for MLGases. These are essentially limited to nonhydrolyzable thio-oligosaccharide analogues as competitive (i.e., noncovalent, reversible) active site inhibitors.…”