Baixe Cellulose-binding domains e outras Notas de estudo em PDF para Engenharia de Produção, somente na Docsity!
Review article
Cellulose-binding domains
Biotechnological applications
Ilan Levy, Oded Shoseyov*
The Institute of Plant Science and Genetics in Agriculture and The Otto Warburg Centre for Agricultural Biotechnology, The Faculty of Agricultural, Food and Environmental Quality Sciences, The Hebrew University of Jerusalem, PO Box 12, Rehovot 76100, Israel Accepted 6 January 2002
Abstract
Many researchers have acknowledged the fact that there exists an immense potential for the application of the cellulose-binding domains (CBDs) in the field of biotechnology. This becomes apparent when the phrase ‘‘cellulose-binding domain’’ is used as the key word for a computerized patent search; more then 150 hits are retrieved. Cellulose is an ideal matrix for large-scale affinity purification procedures. This chemically inert matrix has excellent physical properties as well as low affinity for nonspecific protein binding. It is available in a diverse range of forms and sizes, is pharmaceutically safe, and relatively inexpensive. Present studies into the application of CBDs in industry have established that they can be applied in the modification of physical and chemical properties of composite materials and the development of modified materials with improved properties. In agro-biotechnology, CBDs can be used to modify polysaccharide materials both in vivo and in vitro. The CBDs exert nonhydrolytic fiber disruption on cellulose-containing materials. The potential applications of ‘‘CBD technology’’ range from modulating the architecture of individual cells to the modification of an entire organism. Expressing these genes under specific promoters and using appropriate trafficking signals, can be used to alter the nutritional value and texture of agricultural crops and their final products. D 2002 Elsevier Science Inc. All rights reserved.
Keywords: Cellulose; Cell wall; Cellulose-binding domain (CBD); Pulp; Paper; Biotechnology
0734-9750/02/$ – see front matter D 2002 Elsevier Science Inc. All rights reserved. PII: S 0 7 3 4 - 9 7 5 0 ( 0 2 ) 0 0 0 0 6 - X
- Corresponding author. The Faculty of Agricultural, Food and Environmental Quality Sciences, The Hebrew University of Jerusalem, PO Box 12, Rehovot 76100, Israel. Tel.: +972-8-9481084; fax: +972-8-9462283. E-mail address: [email protected] (O. Shoseyov).
www.elsevier.com/locate/biotechadv
Biotechnology Advances 20 (2002) 191 – 213
- Introduction
It was proposed in late 1940s, that the initial stage in the enzymatic degradation of crystalline cellulose involves the action of an unknown nonhydrolytic component termed C 1. This component was thought to be responsible for destabilization (nonhydrolytic disruption) of the cellulose structure, making the substrate accessible to the enzyme, Cx component (Reese et al., 1950). The cellulose-binding domain (CBD) was first demonstrated in the fungus Trichoderma reesei and the bacterium Cellulomonas fimi (Van Tilbeurgh et al., 1986; Gilkes et al., 1988). The connecting linker between the CBD moiety and the enzyme proved to be susceptible to proteolysis, thus allowing for isolation of the individual domain by limited proteolysis. Forty years after the C 1 –CX model was proposed, the first C 1 component was cloned from Clostridium cellulovorans and C. fimi (Shoseyov et al., 1990; Shoseyov and Doi, 1990; Din et al., 1991; Goldstein et al., 1993). This achievement gave researchers an opportunity to study the C 1 –CX hypothesis. To date, domain structures and biochemical functions of many CBDs have been deciphered (for review, see Gilkes et al., 1991; Davis, 1998; Tomme et al., 1995b, 1998). In earlier studies of CBD–cellulose interactions, the presence of a CBD was shown to increase the effective concentration of enzyme on insoluble cellulose substrates, thereby assisting the enzyme through the phase transfer from soluble fraction (the enzyme) to insoluble fraction (the substrate) (Shoseyov and Doi, 1990; Beguin and Aubert, 1994; Din et al., 1994; Linder et al., 1995; Tomme et al., 1995a; Bolam et al., 1998; Suurnakki et al., 2000). CBDs have been found in hydrolytic and nonhydrolytic proteins. In proteins that possess hydrolytic activity (cellulases, xylenases), the CBD is a discrete domain that concentrates the catalytic domains on the surface of the insoluble cellulose substrate (Gilkes et al., 1991; Tomme et al., 1995a,b, 1998; Linder et al., 1997; Teeri et al., 1998). The CBDs present in proteins that do not have hydrolytic activity compose part of a scaffolding subunit that organizes the catalytic subunits into a cohesive multienzyme complex known as a cellulo- some. The enzymatic complex was found to function more efficiently in the degradation of cellulosic substrates (Woodward et al., 1988; Shoseyov and Doi, 1990; Doi et al., 1994; Beguin and Alzari, 1998; Bayer et al., 1998a,b). Removal of the CBD from the cellulase molecule or from the scaffolding in cellulosomes dramatically decreased enzymatic activity (Van Tilbeurgh et al., 1986; Tomme et al., 1988; Hefford et al., 1992; Goldstein et al., 1993; Coutinho et al., 1993; Carrard and Linder, 1999). CBDs have also been found in several polysaccharide-degrading enzymes. In T. reesei, CBD has been identified in hemicellulase, endo-mannanase and acetyl-xylanesterase (Stal- brand et al., 1995; Margolles-Clark et al., 1996). CBDs have been recognized in xylanase originating from Clostridium thermocellum (Kulkarni et al., 1999; Kim et al., 2000), esterase from Penicillium funiculosum (Kroon et al., 2000), and pectate lyase in Pseudomonas cellulosa (Brown et al., 2001). In addition, there exists the intriguing presence of such a domain in b-glucosidase located in Phanerochaete chrysosporium (Lymar et al., 1995). The presence of putative CBDs in plant endoglucanases has also been reported (Catala and Bennett, 1998; Trainotti et al., 1999). Expansins, that are believed to play a role in
CBDs, constituting isolated modules, are utilized in many different applications. This article will review the potential applications of CBDs in diverse fields of biotechnology.
- Bioprocessing
Large-scale recovery and purification of biologically active molecules continues to be a challenge for many biotechnology companies. Various purification procedures have been developed, of which biospecific affinity purification (affinity chromatography) has become one of the most rapidly developing divisions of immobilized affinity ligand technology. To date, several affinity tags have been developed that vary in size from several amino acids to a complete protein. Each individual affinity-based purification system embodies specific advantages. Cellulose, when compared with most immobilization systems, is an economical support-matrix for large-scale protein purification (for review, see Harakas, 1994; Wilchek and Chaiken, 2000; Lowe, 2001). The wide use of CBD as an affinity tag in expression and purification is illustrated in Fig. 1. This subject has been extensively reviewed (Ong et al., 1989; Greenwood et al., 1992; Bayer et al., 1994; Tomme et al., 1998; Saleemuddin, 1999) and described in several patents (Shoseyov et al., 1997, 1998a,b; Kilburn et al., 1999a,b;
Fig. 1. CBD-based expression and purification of recombinant proteins. Protein expression and purification via CBD involves several steps. (1) Gene fusion between cbd and a gene of interest. (2) Transformation of ligated plasmid vector into a prokaryotic or eukaryotic expression system. (3) Overexpression of the recombinant protein. (4) Purification by immobilization of CBD-tagged protein on cellulose. (5) Reconstitution of the target protein by (A) gentle elution of target protein from cellulosic matrix, (B) addition of a ligand or a substrate, or (C) proteolytic cleavage of the engineered sequence located between the CBD and the target protein.
Meade, 2000; Meade et al., 2001); therefore, this section will review only current develop- ments. Recent reports relating to multifunctional studies have further affirmed the feasibility of employing CBD as an affinity tag. Atrazin dechlorinating enzyme (Kauffmann et al., 2000), a-amylase (Bjornvad et al., 1998), lipase B (Rotticci-Mulder et al., 2001), glucoamylase (Jiang and Radford, 2000), and organophosphorus hydrolase (Richins et al., 2000) have been expressed as CBD-fused enzymes while retaining their high specific activity. In addition, human T cell connective tissue-activator peptide-III (CTAP-III) (Rechter et al., 1999), human hsp60 epitope (Shpigel et al., 1998a,b), protein A (Shpigel et al., 2000), and murine stem-cell factor (SCF) (Doheny et al., 1999; Boraston et al., 2001) were also expressed as CBD-fused proteins. All these studies established the fact, that CBDs can be employed as high-capacity purification tags for the isolation of biologically active target peptides, at relatively low cost. Matrix-assisted refolding of recombinant proteins is one of the approaches taken in order to prevent the aggregation of protein during the course of renaturation. At the present, only histidine and arginine tags have been found to be suitable for this process as they maintain their matrix binding ability under denaturing conditions (Stempfer et al., 1996; Glansbeek et al., 1998) Recently, a CBD derived from Clostridium thermocellum was used as a tag for matrix-assisted refolding of a single-chain antibody expressed in Escherichia coli. This CBD binds to cellulose in the presence of 6 M urea. The method was shown to provide a threefold increase in protein yields when compared to standard refolding procedures (Berdichevsky et al., 1999a). Phage display technology is a proven tool for isolating biologically active molecules (Cortese et al., 1996; Forrer et al., 1999; Johnsson and Ge, 1999; Rodi and Makowski, 1999; Gaskin et al., 2001). One of the limitations preventing extensive implementation of this technology is the relatively high proportion of clones that lack insertions within the library. In a recent study, CBD from Clostridium thermocellum was fused to a single-chain antibody (scFv) and expressed as scFv–CBD phage display library. The CBD tag allowed for rapid recovery of phages that displayed functional inserts, thus increasing the efficiency of the screening process for recombinant antibodies (Berdichevsky et al., 1999b). Direct passive coating of proteins to plastic can result in partial or total denaturation of the adsorbed molecule. This can be attributed to hydrophobic interaction between the protein and the solid phase. (Suter and Butler, 1986; Schwab and Bosshard, 1992). Recently, Levy and Shoseyov (2002) used phage display of a random peptide library to screen for peptides that enable indirect immobilization of proteins to a solid surface via CBD. It was demonstrated that the affinity between the four amino acids tag and a CBD could be employed to immobilize horseradish peroxidase (HRP) on CBD-precoated cellulosic surfaces. This technique enables researches to tailor-make fusion tags that will mediate indirect noncovalent immobilization of proteins to solid matrixes. The binding of CBD to cellulose can be classified as reversible (Family I) or irreversible (Families II and III). When Family I CBD is used as an immobilizing tag, a low-rate column leakage is often observed (Linder et al., 1996). In order to overcome this problem, Linder et al. (1998) constructed a chimerical protein that was composed of CBDHII and CBHI from T. reesei, and a single-chain antibody. A significant decrease in protein leakage was observed
tions, can be improved by increasing their affinity to the textile substrate. This can be achieved by fusion to CBDs (von der Osten et al., 2000b). Additional substances can also be targeted to cellulosic fabrics. Fragrance-bearing particles, conjugated to CBD, can be added to laundry powder hence reducing the amount of fragrance needed in the product (Berry et al., 2001). Threads are exposed to considerable mechanical strain during the weaving process and in order to prevent tearing, they are reinforced by gelatinous substances by a process termed ‘‘sizing.’’ The most popular material used for this procedure is starch, but substances such as PVA, PVP, PAA or other cellulose derivatives such as CMC, hydroxyethyl–cellulose, hydroxypropyl–cellulose, and methylcellulose are also employed. A contradictory effect of the sizing agents is that fabrics are not able to absorb finishing agents, such as dyes, that are frequently dissolved in water. In order to improve the enzymatic ‘‘desizing’’ process, target enzymes can be fused to CBD, in this manner increasing the affinity of enzymes to the cellulosic fabric (von der Osten et al., 2000a). Antimicrobial agents can be targeted to polysaccharide materials. Emerson et al. (1998) proposed the targeting of aromatic aldehydes or alcohols to cellulose-containing materials. Aromatic aldehydes and alcohols, including benzaldehyde, acetaldehyde cinnamaldehyde, piperonal, and vanillin, are known to be effective disinfectants for bacteria, fungi, and viruses and are nontoxic to humans or animals. Targeting can be attained with the assistance of CBD and may be useful for directly impregnating surfaces such as paper or wood (Emerson et al., 1998). Another interesting application is oral care products. Fuglsang and Tsuchiya (2001) applied CBD to orally present polysaccharides (fructan and glucan) that are known to be involved in dental plaque. They found that CBD disperses oral polysaccharides thereby removing and preventing plaque formation. In addition, they established that CBD could be fused to enzymes that are capable of dental plaque polysaccharide degradation and that they could be employed safely in improved plaque removal. Research carried out by Fuglsang and Tsuchiya (2001) concluded that CBD, on its own or combined with other ingredients when used in conventional oral hygiene, will remove existing plaque or prevent its formation. Cellulases are employed in the degradation of gums that are part of the dough structure in breads. The process must be mild, since excess activity can damage dough structure and lower the quality of the final product. Enzymatic activity of Trichoderma cellulase is too aggressive; consequently, Aspergillus cellulase is used in its place (Godfrey, 1996). Fuglsang and Jorgensen (1998) demonstrated another use for CBDs in the baking industry. An antistaling enzyme such as amylolytic enzymes was fused to CBD and used to retard staling and aging of baked bread.
- Cell immobilization
Cell immobilization technology has many applications in biotechnology. The applications range from ethanol production and phenol degradation (Mordoccoa et al., 1999; Nigam,
- to mammalian cell attachment (Yamada, 1983; Kleinman et al., 1987), and whole-cell
diagnostics (Gunneriusson et al., 1996; Stahl and Uhlen, 1997; Samuelson et al., 2000). Several industrial technologies have been developed to immobilize cells; however, they have serious drawbacks. Hollow fibers are expensive and undergo a steady decline in filtration rate (Kang et al., 1990). Covalent immobilization results in loss of cell viability (Jirku, 1999) while cell entrapment is affected by a high degree of mass transfer resistance between the cell and its surroundings (Pilkington et al., 1998). Whole-cell immobilization to cellulosic material was first demonstrated when E. coli surface-anchored CBD, derived from C. fimi, was attached to cellulose (Francisco et al., 1993). In this study, recombinant E. coli cells expressed surface-exposed CBD that enabled high affinity and specific immobilization onto the cellulose surface. Subsequently, it was shown that immobilization via CBDCex derived from C. fimi provided a monolayer of cells on different cellulosic supports. The cells bound tightly to cellulose at a wide range of pHs and the extent of immobilization was dependent on the amount of surface-exposed CBD (Wang et al., 2001). In a different study, Staphylococcus carnosus was chosen to display CBDCel6A from T. reesei on its cell surface and the addition of the CBD predisposed the anchoring of bacterial cells to cotton fibers (Lehtio et al., 2001). A different strategy for cell immobilization was demonstrated by fusing the cell attachment peptide, RGD, to CBDCenA from C. fimi. This novel approach enabled cell immobilization without the need for expensive attachment factors (Wierzba et al., 1995). Recently, it has been demonstrated that stem cell factor immobilized onto cellulose via CBDCex from C. fimi is more potent in stimulating the proliferation of factor-dependent cell lines when compared to the soluble unbound growth factor (Doheny et al., 1999). Surface-exposed CBD is an efficient means of whole-cell immobilization. The process is uncomplicated, mild, and inexpensive. Furthermore, this CBD technology provides an enhanced method for growth factor and cytokine presentation in primary cell cultures.
- Protein engineering with CBD
Protein engineering, using CBDs, is an emerging field. High-level expression vectors have been designed for the production of CBD-fused proteins. Graham et al. (1995) and Hasenwinkle et al. (1997) constructed an expression vector for C- or N-terminal CBD-fused proteins (pTugA and pTugK) based on CBD (^) Cex from C. fimi. Other studies have shown that expressing foreign proteins fused to CBD, for the most part, resulted in high expression levels (Shpigel et al., 1998b, 1999, 2000; Doheny et al., 1999; Rechter et al., 1999; Richins et al., 2000; Kauffmann et al., 2000; Levy and Shoseyov, 2001; Rotticci-Mulder et al., 2001; Boraston et al., 2001). Based on these developments, Novagen has utilized this technology to add to their pET expression vector panel, a group of expression vectors (pET34–38) that incorporate CBDs as their fusion tags (Novy et al., 1997). The beneficial effect that CBD has on the expression of proteins was demonstrated in several studies. Replacing the CBD of endo-1,4-b-glucanase from Bacillus subtilis (Ben) with the CBD of exoglucanase I (Texl) from T. viride resulted in high expression levels in E. coli (Kim et al., 1998). Similar results were reported by Otomo et al. (1999). Segmental isotope
cellulolyticum. The designed chimerical cellulosomes exhibited enhanced synergistic action on crystalline cellulose (Fierobe et al., 2001). It seems evident that CBD has the potential of being used as a molecular scaffold (Shoseyov and Doi, 1990; Doi et al., 1994; Beguin and Alzari, 1998; Bayer et al., 1998a,b). The characteristics of motifs that bind to GroEL were analyzed using affinity panning of immobilized GroEL chaperonin for a phage display library of randomized fungal CBD. This study revealed that GroEL could bind a wide range of structures with exposed side chains; a finding that further substantiates the unfolding activity of GroEL by binding extended conformation of the substrate (Chatellier et al., 1999).
- Diagnostics
Biosensors have enormous potential in the analysis of complex systems due to the high specificity and sensitivity of biomolecules (Hill and Davis, 1999; Turner, 2000; Scheller et al., 2001). In bioprocesses such as fermentation, optimization can only be achieved if the different components in the bioreactor are monitored and controlled. In order to address this problem, Phelps et al. (1994) harnessed CBDs as a tool for glucose biosensing. This novel approach is based on the reversible immobilization of chemically conjugated CBD–glucose oxidase (CBDCex from C. fimi) that can be repeatedly loaded onto a cellulose probe. The binding of CBDCex is reversible and consequently when the enzyme activity deteriorates, the sensor can be regenerated by eluting the original bound enzyme and substituting it with a fresh source (Phelps et al., 1994, 1995; Turner et al., 1997). Staphylococcal Protein A is a cell wall protein consisting of five specific Fc IgG-binding domains which, when bound to the antibody, do not interfere with antigen binding ability (Moks et al., 1986). Protein A was fused to the Clostridium cellulovorans CBD and was used for antibody purification on a cellulose column. It was further demonstrated that this bifunctional protein could be employed in combination with cellulosic microtiter plates as an attractive diagnostic matrix for antigen immobilization. Prot A–CBD complex could also be used as a signal-amplification reagent based on the ability of Prot A–CBD to link prestained cellulose particles to primary antibodies in a Western blot technique (Shoseyov et al., 1999; Shpigel et al., 2000). In recent years, the demand for rapid microbial testing has steadily increased. Various detection methods have been developed that are based on nucleic acid hybridization and immunological assays. An important factor that guides the development of these systems, is the shortening of the time required for pathogen detection. These methods require a high pathogen to cell concentration and therefore, an enrichment step is needed prior to the detection stage (Swaminathan and Feng, 1994; Blackburn et al., 1994). PCR-based detection assays have also been developed that increase detection sensitivity owing to high-specific pathogen detection competence in the presence of large bacterial background. Even so, when pathogen levels are less then 10^3 CFU/g, an additional 6–8 h enrichment step is require (Swaminathan and Feng, 1994). Recently Shoseyov (1998) and Siegel and Shoseyov (2001) developed a system based on CBD, which enables rapid detection of pathogenic microbes in
food samples (illustrated in Fig. 2). In this method, CBD is conjugated to a bacteria-binding protein such as an epitope specific monoclonal antibody and is loaded on to a cellulosic matrix (e.g., cotton gauze) that acts as a bacterial cell concentrator (Fig. 2A). The structure of the cotton gauze enables passage of relatively large volumes of liquids so sufficient bacteria can be isolated, even from dilute samples. The bacteria can then be further enriched with a short growing period (Fig. 2B) or eluted from the loaded matrix, all the while maintaining a very low bacterial background (Fig. 2C) (Shoseyov, 1998; Siegel and Shoseyov, 2001). The eluted bacteria can be utilized for enumeration and/or classification. The advantage of CBDs in diagnostics can be attributed to the wealth of different cellulosic matrices that possess very low nonspecific binding to proteins.
- Fiber modification
Din et al. (1991) reported that CBDCenA from C. fimi endoglucanase A is capable of nonhydrolytic disruption activity of cellulose fibers that results in small particle release. In addition, it was shown that CBDCenA could prevent the flocculation of microcrystalline
Fig. 2. CBD-based pathogen detection system. The method involves conjugation of CBD to a bacteria-binding protein that is subsequently loaded onto a cellulosic matrix column (e.g., cotton gauze). This column acts as a bacterial cell concentrator (A). If the anticipated concentration is insufficient, brief growth period prior to elution from the loaded matrix can be applied to increase bacterial count (B). The resultant isolated bacterial flora contains a very low undesirable background (C). The eluted bacteria can be further analyzed quantitatively or classified into types by means of ELISA, lateral flow detection, or plating onto selective or differential media (D).
the binding sites in CCP are attached to the cellulosic surface and this results in improved mechanical properties (Fig. 4A). At high CCP concentrations, most of the binding sites on the cellulose are occupied by single CBD moieties; consequently, the second CBD moiety (the nonbound moiety) of CCP exposes a hydrophobic surface and in this manner increases surface hydrophobicity (Fig. 4B). Applying CBD to cellulose fibers has a potential for use in paper recycling. It has been demonstrated that the application of CBD on secondary fibers, such as old paperboard containers, results in increased tensile and burst indexes as well as improvement in pulp drainage (Pala et al., 2001). Another study demonstrated that polysaccharide structure modification could be achieved using isolated CBDs. In this study, the surface area of a polysaccharide (ramie cotton fibers) was roughened after treatment with CBD (CBD (^) CenA from C. fimi). It was proposed that these treatments could be used in order to alter dyeing characteristics of cellulose fibers (Gilkes et al., 1998). Cavaco-Paulo et al. (1999) demonstrated the effect of CBD on the dye affinity to cotton fibers. The treated fibers demonstrated increased levels of dye affinity following treatments with Family II CBD from C. fimi. This was especially notable with acid dyes. Bjorkquist et al. (2001) employed a different approach. They demonstrated that an amino acid sequence of less then 30 amino acids can mimic the high affinity of CBD for cellulose (‘‘mimic CBD’’). They proposed that a hybrid protein, composed of a ‘‘mimic CBD’’ and ‘‘benefit agents’’ could be used in fiber care. The benefit agents could be enzymes, perfumes,
Fig. 3. Interfacial contact angle between CCP-treated filter paper and water. Water droplets (20 ml) were onto CCP- treated paper or on nontreated filter papers and pictures were taken in time laps of 25 ms. The nontreated paper frame was taken 25 ms after the water came in contact with the paper, whereas the CCP-treated frame was taken 2 min after the water came in contact with the paper. In order to prevent paper wetting, the paper surface must present low energy on which the initial contact angle of a drop of water is higher than 90°. When the contact angle is less then 90°, wetting, spreading, and penetration occur (Spence, 1987). From the picture, it is clear that the CCP-treated paper wetting angle is higher then 90°; therefore, this paper possesses a hydrophobic surface (Levy et al., 2002b).
xyloglucan adopts a rigid conformation in all probability aligned with the cellulose chain, whereas, the remainder is more mobile. The xyloglucan, when present during cellulose synthesis in the A. xylinum model system, causes the cellulose to become more amorphous and increases its tensile strength (Brett, 2000). When CBD was present, it was shown that CBD could compete with xyloglucan for binding to cellulose (Shpigel et al., 1998a). These findings support the hypothesis that, at least part of the effect of CBD on the plant cell wall is via cellulose–xyloglucan interactions. Shoseyov et al. (2001) have shown that CBD can modulate plant growth of transgenic plants. Introduction of the Family III CBD gene from C. cellulovorans under the control of the elongation-specific cel1 promoter into transgenic poplar plants led to a significant increase in biomass production in selected clones when compared with wild-type control plants (Fig. 5). Analysis of wood characteristics from transgenic poplar trees showed a significant increase in fiber cell length as well as an increase in the average degree of
Fig. 5. Transgenic poplar (Populus tremula) plants expressing CBD. Poplar trees were transformed with cbd (^) Clos gene, fused to cel1 signal peptide under the control of Arabidopsis thaliana elongation specific promotor (cel 1 promoter, Shani, 2000; Shani et al., 1997, 2000). Transgenic plants displayed faster growth rates, thicker stems, and significant increase in wood volume (Shani, 2000).
polymerization of cellulose. In addition, a significant decrease in microfibril angle (MFA) was observed. All these new properties resulted in increased burst, tear, and tensile indices of paper prepared from these fibers (Shoseyov et al., 2001; Levy et al., 2001, 2002b).
- Concluding remarks
Cellulose is by far the most abundant biopolymer on earth. Its excellent chemical and physical properties made it a practical product for infinite applications since the origin of civilization. Today, we are surrounded by numerous products that are composed of cellulose. The capability to govern the binding of biomolecules and cellulose-containing biopolymers to cellulose during the biosynthesis products is an actuality owing to the abundance of CBDs. It is only our imagination that limits their applications.
References
Andersen LN, Schulein M, Lange NEK, Bjørnvad ME, Møller SOS, Glad SOS, Kauppinen MS, Schnorr K, Kongsbak L. Pectate lyases. US patent 6,187,580, 2001. Askling C, Wagberg L, Rigdahl M. The effect of additives on the mechanical properties of dry-formed fiber networks. J Mater Sci 1998;33:1997 – 2003. Atalla RH, Hackney JM, Uhlin I, Thompson NS. Hemicelluloses as structure regulators in the aggregation of native cellulose. Int J Biol Macromol 1993;15:109 – 12. Banka RR, Mishra S, Ghose TK. Fibril formation from cellulose by a novel protein from Trichoderma reesei: a non-hydrolytic cellulolytic component? World J Microbiol Biotechnol 1998;14:551 – 8. Bayer EA, Morag E, Lamed R. The cellulosome a treasure-trove for biotechnology. Trends Biotechnol 1994;12:379 – 86. Bayer EA, Shimon LJ, Shoham Y, Lamed R. Cellulosomes—structure and ultrastructure. J Struct Biol 1998a;124:221 – 34. Bayer EA, Chanzy H, Lamed R, Shoham Y. Cellulose, cellulases and cellulosomes. Curr Opin Struct Biol 1998b;8:548 – 57. Beguin P, Aubert JP. The biological degradation of cellulose. FEMS Microbiol Rev 1994;13:25 – 58. Beguin P, Alzari PM. The cellulosome of Clostridium thermocellum. Biochem Soc Trans 1998;26:178 – 85. Benziman M, Haigler CH, Brown RMJ, White AR, Cooper KM. Cellulose biogenesis: polymerization and crystallization are coupled processes in Acetobacter xylinum. Proc Natl Acad Sci USA 1980;77:6678 – 82. Berdichevsky Y, Lamed R, Frenkel D, Gophna U, Bayer EA, Yaron S, Shoham Y, Benhar I. Matrix-assisted refolding of single- chain Fv-cellulose binding domain fusion proteins. Protein Expression Purif 1999a;17:249 – 59. Berdichevsky Y, Ben-Zeev E, Lamed R, Benhar I. Phage display of a cellulose binding domain from Clostridium thermocellum and its application as a tool for antibody engineering. J Immunol Methods 1999b;228:151 – 62. Berry MJ, Davis PJ, Gidley MJ. Conjugated polysaccharide fabric detergent and conditioning products. US patent 6,225,462,
Bjorkquist DW, Smets J, Siegel DP, Boyer SL. Mimic cellulose binding domain (WO01/32848A1, PCT). Bjornvad M, Pedersen S, Schulein M, Bisg Rd-Fratzen H. Alpha-amylase fused to cellulose binding domain, for starch degradation (WO98/16633A1, PCT). Blackburn CW, Curtis LM, Humpheson L, Petitt SB. Evaluation of the vitek immunodiagnostic assay system (VIDAS) for the detection of Salmonella in foods. Lett Appl Microbiol 1994;19:32 – 6. Bolam DN, Ciruela A, McQueen-Mason S, Simpson P, Williamson MP, Rixon JE, Boraston A, Hazlewood GP, Gilbert HJ. Pseudomonas cellulose-binding domains mediate their effects by increasing enzyme substrate proximity. Biochem J 1998;331:775 – 81. Boraston A, Bray M, Burn E, Creagh AL, Gilkes N, Guarna M, Jervis E, Johnson P, Kormos J, McIntosh L, McLean B, Sandercock L, Tomme P, Haynes C, Warren A, Kilburn D. The structure and function of cellulose binding domains. In: Claeyssen M, Nerinkx W, Piens K, editors. Carbohydrate from Trichoderma reesei and other microorganisms. Cambrige, UK: The Royal Society of Chemistry, 1998. p. 139 – 46.
Fuglsang CC, Jorgensen OB. Use of a carbohydrate binding domain in baking (WO98/16112A1, PCT). Fuglsang CC, Tsuchiya R. Cellulose binding domains (CBDs) for oral care products. US patent 6,264,925, 2001. Gao PJ, Chen GJ, Wang TH, Zhang YS, Liu J. Non-hydrolytic disruption of crystalline structure of cellulose by cellulose binding domain and linker sequence of cellobiohydrolase I from Penicillium janthinellum. Acta Biochim Biophys Sin 2001;33:13 – 8. Gaskin DJ, Starck K, Turner NA, Vulfson EN. Phage display combinatorial libraries of short peptides: ligand selection for protein purification. Enzyme Microb Technol 2001;28:766 – 72. Gassan J, Bledzki AK. Alkali treatment of lute fibers: relationship between structure and mechanical properties. J Appl Polym Sci 1998;71:623 – 9. Giddings G. Transgenic plants as protein factories. Curr Opin Biotechnol 2001;12:450 – 4. Gilkes NR, Warren RA, Miller RJ, Kilburn DG. Precise excision of the cellulose binding domains from two Cellulomonas fimi cellulases by a homologous protease and the effect on catalysis. J Biol Chem 1988;263:10401 – 7. Gilkes NR, Henrissat B, Kilburn DG, Miller RJ, Warren RA. Domains in microbial beta-1,4-glycanases: sequence conservation, function, and enzyme families. Microbiol Rev 1991;55:303 – 15. Gilkes NR, Jervis E, Henrissat B, Tekant B, Miller RC, Warren RA, Kilburn DG. The adsorption of a bacterial cellulase and its two isolated domains to crystalline cellulose. J Biol Chem 1992;267:6743 – 9. Gilkes NR, Kilburn DG, Miller RC, Warren RA, Sugiyama J, Chanzy H, Henrissat B. Visualization of the adsorption of a bacterial endo-beta-1,4-glucanase and its isolated cellulose-binding domain to crystalline cellulose. Int J Biol Macromol 1993;15:347 – 51. Gilkes NR, Kilburn DG, Miller RC, Warren A. Methods and compositions for modification of polysaccharide characteristics. US patent 5,821,358, 1998. Glansbeek HL, van Beuningen HM, Vitters EL, van der Kraan PM, van den Berg WB. Expression of recombinant human soluble type II transforming growth factor-beta receptor in Pichia pastoris and Escherichia coli: two powerful systems to express a potent inhibitor of transforming growth factor-beta. Protein Expression Purif 1998;12:201 – 7. Godfrey T. Baking. In: Godfrey T, West S, editors. Industrial enzymology 2nd ed. London: Macmillan, 1996. p. 87 – 101. Goldstein MA, Takagi M, Hashida S, Shoseyov O, Doi RH, Segel IH. Characterization of the cellulose-binding domain of the Clostridium cellulovorans cellulose-binding protein A. J Bacteriol 1993;175:5762 – 8. Graham RW, Greenwood JM, Warren RA, Kilburn DG, Trimbur DE. The pTugA and pTugAS vectors for high-level expression of cloned genes in Escherichia coli. Gene 1995;158:51 – 4. Greenwood JM, Ong E, Gilkes NR, Warren RA, Miller RC, Kilburn DG. Cellulose-binding domains: potential for purification of complex proteins. Protein Eng 1992;5:361 – 5. Gunneriusson E, Samuelson P, Uhlen M, Nygren PA, Stahl S. Surface display of a functional single-chain Fv antibody on staphylococci. J Bacteriol 1996;178:1341 – 6. Hackney JM, Atalla RH, VanderHart DL. Modification of crystallinity and crystalline structure of Acetobacter xylinum cellulose in the presence of water-soluble beta-1,4-linked polysaccharides: 13C-NMR evidence. Int J Biol Macromol 1994;16:215 – 8. Haigler CH. Relationship between polymerization and crystallization in microfibril biogenesis. In: Haigler CH, Weimer PJ, editors. Biosynthesis and biodegradation of cellulose. New York: Marcel Dekker, 1991. p. 99 – 124. Harakas NK. Protein purification process engineering. Biospecific affinity chromatography. Bioprocess Technol 1994;18: 259 – 316. Hasenwinkle D, Jervis E, Kops O, Liu C, Lesnicki G, Haynes CA, Kilburn DG. Very high-level production and export in Escherichia coli of a cellulose binding domain for use in a generic secretion-affinity fusion system. Biotechnol Bioeng 1997;55:854 – 63. Hayashi T, Ohsumi C. Endo-1,4-b-glucanase in the cell wall of stems of auxin-treated pea seedling. Plant Cell Physiol 1994;35:419 – 24. Haynes CA, Tomme P, Kilburn DG. Two-phase partition affinity separation system and affinity separated cell-containing composition. US patent 6,048,715, 2000. Hefford MA, Laderoute K, Willick GE, Yaguchi M, Seligy VL. Bipartite organization of the Bacillus subtilis endo-beta-1,4- glucanase revealed by C-terminal mutations. Protein Eng 1992;5:433 – 9. Henrissat B. Cellulases and their interaction with cellulose. Cellulose 1994;1:169 – 96. Herbers K, Sonnewald U. Production of new/modified proteins in transgenic plants. Curr Opin Biotechnol 1999;10:163 – 8. Hill HA, Davis JJ. Biosensors: past, present and future. Biochem Soc Trans 1999;27:331 – 5. Hood EE, Jilka JM. Plant-based production of xenogenic proteins. Curr Opin Biotechnol 1999;10:382 – 6. Jervis EJ, Haynes CA, Kilburn DG. Surface diffusion of cellulases and their isolated binding domains on cellulose. J Biol Chem 1997;272:24016 – 23. Jiang M, Radford A. Exploitation of a cellulose-binding domain from Neurospora crassa. Enzyme Microb Technol 2000;27:434 – 42.
Jirku V. Whole cell immobilization as a means of enhancing ethanol tolerance. J Ind Microbiol Biotechnol 1999;22:147 – 51. Johnson PE, Joshi MD, Tomme P, Kilburn DG, McIntosh LP. Structure of the N-terminal cellulose-binding domain of Cellu- lomonas fimi CenC determined by nuclear resonance spectroscopy. Biochemistry 1996;35:14381 – 94. Johnsson K, Ge L. Phage display of combinatorial peptide and protein libraries and their applications in biology and chemistry. Curr Top Microbiol Immunol 1999;243:87 – 105. Kalum L, Andersen BK. Enzymatic treatment of denim. US patent 6,146,428, 2000. Kang WK, Shukla R, Sirkar KK. Ethanol-production in a microporous hollow-fiber-based extractive fermenter with immobilized yeast. Biotechnol Bioeng 1990;36:826 – 33. Kauffmann C, Shoseyov O, Shpigel E, Bayer EA, Lamed R, Shoham Y, Mandelbaum RT. A novel methodology for enzymatic removal of atrazine from water by CBD-fusion protein immobilized on cellulose. Environ Sci Technol 2000;34:1292 – 6. Kilburn DG, Miller RC, Warren RAJ, Gilkes NR. Polysaccharide binding fusion proteins and conjugates. US patent 5,962,289, 1999a. Kilburn DG, Miller RC, Gilkes NR, Warren RAJ. Conjugate of non-protein chemical moiety and polypeptide having cellulose binding region. US patent 5,928,917, 1999b. Kim H, Goto M, Jeong HJ, Jung KH, Kwon I, Furukawa K. Functional analysis of a hybrid endoglucanase of bacterial origin having a cellulose binding domain from a fungal exoglucanase. Appl Biochem Biotechnol 1998;75:193 – 204. Kim H, Jung KH, Pack MY. Molecular characterization of xynX, a gene encoding a multidomain xylanase with a thermo- stabilizing domain from Clostridium. Appl Microbiol Biotechnol 2000;54:521 – 7. Kleinman HK, Luckenbill-Edds L, Cannon FW, Sephel GC. Use of extracellular matrix components for cell culture. Anal Biochem 1987;166:1 – 13. Kroon PA, Williamson G, Fish NM, Archer DB, Belshaw NJ. A modular esterase from Penicillium funiculosum which releases ferulic acid from plant cell walls and binds crystalline cellulose contains a carbohydrate binding module. Eur J Biochem 2000;267:6740 – 52. Krull LH, Dintzis FR, Griffin HL, Baker FL. A microfibril-generating factor from the cellulase of Trichoderma reesei. Bio- technol Bioeng 1988;31:321 – 7. Kulkarni N, Shendye A, Rao M. Molecular and biotechnological aspects of xylanases. FEMS Microbiol Rev 1999;23:411 – 56. Le Nguyen D, Heitz A, Chiche L, Castro B, Boigegrain RA, Favel A, Coletti-Previero MA. Molecular recognition between serine proteases and new bioactive microproteins with a knotted structure. Biochimie 1990;72:431 – 5. Lee I, Evans BR, Woodward J. The mechanism of cellulase action on cotton fibers: evidence from atomic force microscopy. Ultramicroscopy 2000;82:213 – 21. Lehtio J, Teeri TT, Nygren PA. Alpha-amylase inhibitors selected from a combinatorial library of a cellulose binding domain scaffold. Proteins 2000;41:316 – 22. Lehtio J, Wernerus H, Samuelson P, Teeri TT, Stahl S. Directed immobilization of recombinant staphylococci on cotton fibers by functional display of a fungal cellulose-binding domain. FEMS Microbiol Lett 2001;195:197 – 204. Levy I, Shoseyov O. Expression, refolding and indirect immobilization of horseradish peroxidase (HRP) to cellulose via a phage- selected peptide and cellulose-binding domain (CBD). J Pept Sci 2002;7:50 – 7. Levy I, Nussinovitch A, Shoseyov A. Modification of polysaccharide containing materials, 2001 (WO01/34091A2, PCT). Levy I, Shani Z, Shoseyov O. Modification of polysaccharides and plant cell wall by endo-1,4-b-glucanase and cellulose-binding domains. Biomol Eng 2002a (In press). Levy I, Nussinovitch A, Shpigel E, Shoseyov O. Recombinant cellulose crosslinking protein: a novel paper-modification biomaterial. Cellulose 2002b (In press). Limon MC, Margolles-Clark E, Benitez T, Penttila M. Addition of substrate-binding domains increases substrate-binding capacity and specific activity of a chitinase from Trichoderma harzianum. FEMS Microbiol Lett 2001;198:57 – 63. Linder M, Lindeberg G, Reinikainen T, Teeri TT, Pettersson G. The difference in affinity between two fungal cellulose-binding domains is dominated by a single amino acid substitution. FEBS Lett 1995;372:96 – 8. Linder M, Salovuori I, Ruohonen L, Teeri TT. Characterization of a double cellulose-binding domain. Synergistic high affinity binding to crystalline cellulose. J Biol Chem 1996;271:21268 – 72. Linder M, Margolles-Clark E, Reinikainen T, Teeri TT. Trichoderma reesei cellobiohydrolase I with an endoglucanase cellulose- binding domain: action on bacterial microcrystalline cellulose. J Biotechnol 1997;57:49 – 57. Linder M, Nevanen T, Soderholm L, Bengs O, Teeri TT. Improved immobilization of fusion proteins via cellulose-binding domains. Biotechnol Bioeng 1998;60:642 – 7. Linder M, Nevanen T, Teeri TT. Design of a pH-dependent cellulose-binding domain. FEBS Lett 1999;447:13 – 6. Lowe CR. Combinatorial approaches to affinity chromatography. Curr Opin Chem Biol 2001;5:248 – 56. Lymar ES, Li B, Renganathan V. Purification and characterization of a cellulose-binding beta-glucosidase from cellulose- degrading cultures of Phanerochaete chrysosporium. Appl Environ Microbiol 1995;61:2976 – 80.
