» Articles » PMID: 1369234

The Cellulose Paradox: Pollutant Par Excellence And/or a Reclaimable Natural Resource?

Overview
Journal Biodegradation
Date 1992 Jan 1
PMID 1369234
Citations 16
Authors
Affiliations
Soon will be listed here.
Abstract

The various aspects of cellulose as a pollutant are considered in view of its lack of toxicity on the one hand and its recalcitrant durable nature on the other. The microbial degradation of cellulosics is discussed, and the contrast between its success in handling natural cellulosic wastes versus its failure to cope with man-made refuse is described. Research carried out in the past decade has demonstrated that cellulolytic organisms are provided with cell surface multifunctional multienzyme conglomerates, called cellulosomes, which are capable of solubilizing solid cellulosic substrates. The intriguing properties of such complexes include their cohesive nature, their many enzymatic components, and a characteristic glycosylated cellulose-binding, 'scaffolding' component. The latter appears to serve as a substrate-targeting carrier, which delivers the other (hydrolytic) components to the cellulose. Progress in establishing efficient model systems for in vitro solubilization of purified cellulose or natural cellulosic substrates has been achieved using purified cellulosome preparations, fortified with beta-glucosidase and pectinase. The latter enzymes were required in order to alleviate the phenomenon of product inhibition which reduces the efficiency of the free cellulosome. Such combined enzyme systems are proposed as examples of future tailor-made cellulolytic systems for the degradation of natural cellulosics.

Citing Articles

Microbial communities responsible for the degradation of poly(lactic acid)/poly(3-hydroxybutyrate) blend mulches in soil burial respirometric tests.

Jeszeova L, Puskarova A, Buckova M, Krakova L, Grivalsky T, Danko M World J Microbiol Biotechnol. 2018; 34(7):101.

PMID: 29934788 DOI: 10.1007/s11274-018-2483-y.


Deletion of a Gene Encoding a Putative Peptidoglycan-Associated Lipoprotein Prevents Degradation of the Crystalline Region of Cellulose in .

Wang X, Wang Z, Bai X, Zhao Y, Zhang W, Lu X Front Microbiol. 2018; 9:632.

PMID: 29666619 PMC: 5891637. DOI: 10.3389/fmicb.2018.00632.


The effect of switchgrass loadings on feedstock solubilization and biofuel production by .

Verbeke T, Garcia G, Elkins J Biotechnol Biofuels. 2017; 10:233.

PMID: 29213307 PMC: 5708108. DOI: 10.1186/s13068-017-0917-7.


Functional Studies of β-Glucosidases of and Their Effects on Cellulose Degradation.

Bai X, Wang X, Wang S, Ji X, Guan Z, Zhang W Front Microbiol. 2017; 8:140.

PMID: 28210251 PMC: 5288383. DOI: 10.3389/fmicb.2017.00140.


Cellulosomics of the cellulolytic thermophile Clostridium clariflavum.

Artzi L, Dassa B, Borovok I, Shamshoum M, Lamed R, Bayer E Biotechnol Biofuels. 2015; 7:100.

PMID: 26413154 PMC: 4582956. DOI: 10.1186/1754-6834-7-100.


References
1.
Morag E, Bayer E, Lamed R . Relationship of cellulosomal and noncellulosomal xylanases of Clostridium thermocellum to cellulose-degrading enzymes. J Bacteriol. 1990; 172(10):6098-105. PMC: 526935. DOI: 10.1128/jb.172.10.6098-6105.1990. View

2.
Durrant A, Hall J, Hazlewood G, Gilbert H . The non-catalytic C-terminal region of endoglucanase E from Clostridium thermocellum contains a cellulose-binding domain. Biochem J. 1991; 273(Pt 2):289-93. PMC: 1149844. DOI: 10.1042/bj2730289. View

3.
Bayer E, Lamed R . Ultrastructure of the cell surface cellulosome of Clostridium thermocellum and its interaction with cellulose. J Bacteriol. 1986; 167(3):828-36. PMC: 215948. DOI: 10.1128/jb.167.3.828-836.1986. View

4.
Kadam S, DEMAIN A . Addition of cloned beta-glucosidase enhances the degradation of crystalline cellulose by the Clostridium thermocellum cellulose complex. Biochem Biophys Res Commun. 1989; 161(2):706-11. DOI: 10.1016/0006-291x(89)92657-0. View

5.
Cowling E . Physical and chemical constraints in the hydrolysis of cellulose and lignocellulosic materials. Biotechnol Bioeng Symp. 1975; (5):163-81. View