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Cellulase Sale

(Synonyms: 纤维素酶) 目录号 : GC30228

Cellulase是一种酶,能够催化纤维素和其他碳水化合物的水解.10u/mg

Cellulase Chemical Structure

Cas No.:9012-54-8

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1g
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产品描述

Cellulase is an enzyme catalyzing the hydrolysis of certain linkages in cellulose and other carbohydrates.

Cellulase exhibits significant antibiofilm activity against B. cepacia, but does not have much action on its growth[1]. Cellulase and protease leads to the CST increasing in the case of activated sludge, but the effect of cellulase is lower than that of protease at the same concertration. Cellulase decreases the particle size of activated sludge. Cellulase has no significantly effect on sludge dewatering in terms of solid concentration after centrifugation[2].

[1]. Rajasekharan SK, et al. Cellulase inhibits Burkholderia cepacia biofilms on diverse prosthetic materials. Pol J Microbiol. 2013;62(3):327-30. [2]. Pei HY, et al. Effect of protease and cellulase on the characteristic of activated sludge. J Hazard Mater. 2010 Jun 15;178(1-3):397-403.

Chemical Properties

Cas No. 9012-54-8 SDF
别名 纤维素酶
Canonical SMILES [Cellulase]
分子式 分子量
溶解度 Water : 1 mg/mL ;DMSO : 1 mg/mL 储存条件 Store at -20°C
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Research Update

Microbial cellulase production using fruit wastes and its applications in biofuels production

The present review explores fruit wastes as potential and low-cost substrates for economical production of cellulase enzymes. Being renewable, vast availability and having rich organic nutrient, these fruit wastes can be exploited to produce cellulase enzyme for various industrial applications. This review aimed to explore recent insight in sustainable production of microbial cellulolytic enzymes following solid state fermentation (SSF) wherein different types of fruit wastes as a potentially viable and alternative form of substrates have been utilized. In addition, detailed about the characteristics, mechanisms and market scenario of cellulase enzymes produced through a range of microbial species have been discussed. Further, impacts of different physicochemical parameters on solid-state fermentation based enzyme production and scale up issues have also analyzed. Moreover, applications of cellulases to produce different types of biofuels have been evaluated while emphases are made on existing hindrances and the possible strategies to improve the enzyme production process using fruit wastes.

Signal peptide of cellulase

Cellulase is an enzyme playing a crucial role in biotechnology industries ranging from textile to biofuel because of tremendous amount of cellulose produced in plant. In order to improve cellulase productivity, huge resource has been spent in search for good cellulases from microorganism in remote areas and in creation of ideal cellulase by engineering. However, not much attention is given to the secretion of cellulases from cell into extracellular space, where a cellulase plays its enzymatic role. In this minireview, the signal peptides, which lead secreted proteins to specific secretion systems and scatter in literature, are reviewed. The patterns of signal peptides are checked against 4,101 cellulases documented in UniProtKB, the largest protein database in the world, to determine how these cellulases are secreted. Simultaneous review on both literature and cellulases from the database not only provides updated knowledge on signal peptides but also indicates the gap in our research.

Cellulase processivity

There are two types of processive cellulases, exocellulases and processive endoglucanases. There are also two classes of exocellulases, ones that attack the reducing ends of cellulose chains and ones that attack the nonreducing ends. There are a number of ways of assaying processivity but none of them are ideal. It appears that exocellulases, all of which have their active sites in a tunnel, couple movement along a cellulose chain with cleavage of cellobiose from the end of the cellulose molecule. There are two sets of structures that suggest how an exocellulase might move along a cellulose chain. For family 48 exocellulases there are two different ways that a chain can be bound in the active site while for family 6 exocellulases there are several different ligand-bound structures. Site-directed mutagenesis of Thermobifida fusca exocellulases Cel48A and Cel6B and the processive endoglucanase Cel9A have identified some mutations that increase processivity and some that decrease processivity. In addition a mutation in Cel6B was identified that appears to allow the mutant enzyme to move along a cellulose chain in the absence of cleavage.

Cellulase immobilized on kaolin as a potential approach to improve the quality of knitted fabric

Biopolishing is a textile process that uses cellulases to improve the pilling resistance of fabrics. Although the process improves the pilling resistance, softness and color brightness of fabrics, it causes a significant loss of tensile strength in treated fabrics. The present work studied the use of cellulase immobilized on kaolin by adsorption and covalent bonding in biopolishing to get around this problem. The cellulase immobilization has been reported as promising alternative to overcome the inconvenient of biopolishing, but it has been very poorly explored. The results showed that cellulase immobilized by both covalent bonding and adsorption methods provided to the knitted fabric similar or superior pilling resistance to free cellulase, but with greater tensile strength. Immobilization also allowed for efficient recovery and reuse of the enzyme. The present work is a relevant contribution to the literature, since, as far as we know, it is the first work that shows it is possible to minimize the loss of tensile strength and also reuse the immobilized enzyme, giving a better-quality product and also contribution to reducing the cost of the polishing step.