nach oben

Cellulose

Erschienen in:

01.02.2010

Reducing end-specific fluorescence labeled celluloses for cellulase mode of action

verfasst von: Riin Velleste, Hele Teugjas, Priit Väljamäe

Erschienen in: Cellulose | Ausgabe 1/2010

Einloggen

Aktivieren Sie unsere intelligente Suche, um passende Fachinhalte oder Patente zu finden.

search-config

KI-gestützte Suche

Aus

Abstract

Cellobiohydrolases (CBH-s) attack primarily from the cellulose chain ends. It is known that CBH-s can differ in their chain end preference. Here the cellulose reducing end-specific fluorescence labeling was studied with the aim to find the most suitable labeled cellulose for easy determination of CBH-s chain end preference. Anthranilic acid (AA) was used as fluorescence label. Bacterial cellulose, amorphous Avicel and filter paper were subjected to the labeling. Suitability of modified bicincoic acid method for determination of reducing groups on cellulose was also confirmed. AA labeled celluloses were hydrolysed with family 7 and 6 CBH-s from Trichoderma reesei and Phanerochaete chrysosporium. Hydrolysis data were plotted as released label (%) versus total degradation (%) (progress curves). Most characteristic progress curves were obtained with AA labeled regenerated amorphous Avicel where the family 6 CBH-s produced clearly upward curved progress curves confirming their preference for non-reducing ends.

Vorheriger Artikel Composition of lignocellulosic surfaces: comments on the interpretation of XPS spectra

Nächster Artikel Structure elucidation of uniformly 13C-labeled bacterial celluloses from different Gluconacetobacter xylinus strains

Sie haben noch keine Lizenz? Dann Informieren Sie sich jetzt über unsere Produkte:

Springer Professional "Technik"

Online-Abonnement

Mit Springer Professional "Technik" erhalten Sie Zugriff auf:

über 67.000 Bücher
über 390 Zeitschriften

aus folgenden Fachgebieten:

Automobil + Motoren
Bauwesen + Immobilien
Business IT + Informatik
Elektrotechnik + Elektronik
Energie + Nachhaltigkeit
Maschinenbau + Werkstoffe

Jetzt Wissensvorsprung sichern!

Jetzt informieren

Springer Professional "Wirtschaft+Technik"

Online-Abonnement

Mit Springer Professional "Wirtschaft+Technik" erhalten Sie Zugriff auf:

über 102.000 Bücher
über 537 Zeitschriften

aus folgenden Fachgebieten:

Automobil + Motoren
Bauwesen + Immobilien
Business IT + Informatik
Elektrotechnik + Elektronik
Energie + Nachhaltigkeit
Finance + Banking
Management + Führung
Marketing + Vertrieb
Maschinenbau + Werkstoffe
Versicherung + Risiko

Jetzt Wissensvorsprung sichern!

Jetzt informieren

Nur mit Berechtigung zugänglich

Anthon GE, Barrett DM (2002) Determination of reducing sugars with 3-methyl-2-benzothiazolinonehydrazone. Anal Biochem 305:287–289CrossRef

Anumula KR (1994) Quantitative determination of monosaccharides in glycoproteins by high performance liquid chromatography with highly sensitive fluorescence detection. Anal Biochem 220:275–283CrossRef

Anumula KR (2006) Advances in fluorescence derivatization methods for high-performance liquid chromatographic analysis of glycoprotein carbohydrates. Anal Biochem 350:1–23CrossRef

Arai M, Sakamoto R, Murao S (1989) Different action of two avicelases from Aspergillus aculeatus. Agric Biol Chem 5:1411–1412

Aronson NN, Halloran BA, Alexyev MF, Amable L, Madura JD, Pasupulati L, Worth C, van Roey P (2003) Family 18 chitinase–oligosaccharide substrate interaction: subsite preference and anomer selectivity of Serratia marcescens chitinase A. Biochem J 376:87–95CrossRef

Barr BK, Hsieh Y-L, Ganem B, Wilson DB (1996) Identification of two functionally different classes of exocellulases. Biochemistry 35:586–592CrossRef

Bhat KM, Hay AJ, Claeyssens M, Wood TM (1990) Study of the mode of action and site-specificity of the endo-(1–4)-β-D-glucanases of the fungus Penicillium pinophilum with normal, 1–3H-labelled, reduced and chromogenic cello-oligosaccharides. Biochem J 266:371–378

Bhikhabhai R, Johansson G, Pettersson G (1984) Isolation of cellulolytic enzymes from Trichoderma reesei QM 9414. J Appl Biochem 6:336–345

Biely P, Vrsanska M, Claeyssens M (1993) Mode of action of Trichoderma reesei β-1,4-glucanases on cellooligosaccharides. In: Suominen P, Reinikainen T (eds) Proceedings of the second TRICEL symposium of Trichoderma reesei. Cellulases and other hydrolases, Espoo, pp 99–108

Boisset C, Fraschini C, Schülein M, Henrissat B, Chanzy H (2000) Imaging the enzymatic digestion of bacterial cellulose ribbons reveals the endo character of the cellobiohydrolase Cel6A from Humicola insolens and its mode of synergy with cellobiohydrolase Cel7A. Appl Environ Microbiol 66:1444–1452CrossRef

Boraston AB, Bolam DN, Gilbert HJ, Davies GJ (2004) Carbohydrate-binding modules: fine-tuning polysaccharide recognition. Biochem J 382:769–781CrossRef

Carrard G, Koivula A, Söderlund H, Beguin P (2000) Cellulose-binding domains promote hydrolysis of different sites on crystalline cellulose. Proc Natl Acad Sci USA 97:10342–10347CrossRef

Chanzy H, Henrissat B (1985) Undirectional degradation of Valonia cellulose microcrystals subjected to cellulase action. FEBS Lett 184:285–288CrossRef

Claeyssens M, van Tilbeurgh H, Tomme P, Wood TM, McRae SI (1989) Fungal cellulase systems. Comparison of the specificities of the cellobiohydrolases isolated from Penicillum pinophilum and Trichoderma reesei. Biochem J 261:819–825

Gilkes NR, Kwan E, Kilburn DG, Miller RC, Antony R, Warren J (1997) Attack of carboxymethylcellulose at opposite ends by two cellobiohydrolases from Cellulomonas fimi. J Biotechnol 57:83–90CrossRef

Gill SC, von Hippel PH (1989) Calculation of protein extinction coefficients from amino acid sequence data. Anal Biochem 182:319–326CrossRef

Gruno M, Väljamäe P, Pettersson G, Johansson G (2004) Inhibition of the Trichoderma reesei cellulases by cellobiose is strongly dependent on the nature of substrate. Biotechnol Bioeng 86:503–511CrossRef

Harjunpää V, Teleman A, Koivula A, Ruohonen L, Teeri TT, Teleman O, Drakenberg T (1996) Cello-oligosaccharide hydrolysis by cellobiohydrolase II from Trichoderma reesei. Association and rate constants derived from an analysis of progress curves. Eur J Biochem 240:584–591CrossRef

Hildén L, Väljamäe P, Johansson G (2005) Surface character of pulp fibres studied using endoglucanases. J Biotechnol 118:386–397CrossRef

Himmel ME, Ding S-Y, Johnson DK, Adney WS, Nimlos MR, Brady JW, Foust TD (2007) Biomass recalcitrance: engineering plants and enzymes for biofuels production. Science 315:804–807CrossRef

Honda Y, Taniguchi H, Kitaoka M (2008) A reducing-end-acting chitinase from Vibrio proteolyticus belonging to glycoside hydrolase family 19. Appl Microbiol Biotechnol 78:627–634CrossRef

Hörmann H, Gollwitzer R (1962) Bestimmung von hexosen in trypofan-haltigen eiweisskörpern. Ann Chem 655:178–188

Horn SJ, Eijsink VGH (2004) A reliable reducing end assay for chito-oligosaccharides. Carbohydr Polym 56:35–39CrossRef

Imai T, Boisset C, Samejima M, Igarashi K, Sugiyama J (1998) Undirectional processive action of cellobiohydrolase Cel7A on Valonia cellulose microcrystals. FEBS Lett 432:113–116CrossRef

Kipper K, Väljamäe P, Johansson G (2005) Processive action of cellobiohydrolase Cel7A from Trichoderma reesei is revealed as `burst′ kinetics on fluorescent polymeric model substrates. Biochem J 385:527–535CrossRef

Knill CJ, Kennedy JF (2003) Degradation of cellulose under alkaline conditions. Carbohydr Polym 51:281–300CrossRef

Kongruang S, Penner MH (2004) Borhydride reactivity of cellulose reducing ends. Carbohydr Polym 58:131–138CrossRef

Kongruang S, Han MJ, Breton CIG, Penner MH (2004) Quantitative analysis of cellulose reducing ends. Appl Biochem Biotechnol 113:213–232CrossRef

Lynd LR, Weimer PJ, van Zyl WH, Pretorius IS (2002) Microbial cellulose utilization: fundamentals and biotechnology. Microbiol Mol Biol Rev 66:506–577CrossRef

Lynd LR, Laser MS, Bransby D, Dale BE, Davison B, Hamilton R, Himmel M, Keller M, McMillan JD, Sheehan J, Wyman CE (2008) How biotech can transform biofuels. Nat Biotechnol 26:169–172CrossRef

Martinez D, Larrondo LF, Putnam N, Gelpke MDS, Huang K, Chapman J, Helfenbein KG, Ramaiya P, Detter JC, Larimer F, Coutinho PM, Henrissat B, Berka R, Cullen D, Rokhsar D (2004) Genome sequence of the lignocellulose degrading fungus Phanerochaete chrysosporium strain RP78. Nat Biotechnol 22:695–700CrossRef

Martinez D et al (2008) Genome sequencing and analysis of the biomass-degrading fungus Trichoderma reesei (syn. Hypocrea jecorina). Nat Biotechnol 26:553–560CrossRef

Nimlos MR, Matthews JF, Crowley MF, Walker RC, Chukkapalli G, Brady JW, Adney WS, Cleary JM, Zhong L, Himmel ME (2007) Molecular modeling suggests induced fit of family I carbohydrate–binding modules with a broken-chain cellolose surface. Protein Eng Des Sel 20:179–187CrossRef

Nutt A, Sild V, Pettersson G, Johansson G (1998) Progress curves. A mean for functional classification of cellulases. Eur J Biochem 258:200–206CrossRef

Pace CN, Vajdos F, Fee L, Grimsley G, Gray T (1995) How to measure and predict the molar absorption coefficient of a protein. Protein Sci 4:2411–2423CrossRef

Ragauskas AJ, Williams CK, Davison BH, Britovsek G, Cairney J, Eckert CA, Frederick WJ Jr, Hallet JP, Leak DJ, Liotta CL, Mielenz JR, Murphy R, Templer R, Tschaplinski T (2006) The path forward for biofuel and biomaterials. Science 311:484–489CrossRef

Röhrling J, Potthast A, Rosenau T, Lange T, Ebner G, Sixta H, Kosma P (2002) A novel method for the determination of carbonyl groups in cellulosics by fluorescence labeling. 1. Method development. Biomacromolecules 3:959–968CrossRef

Schou C, Rasmussen G, Kaltoft M-B, Henrissat B, Schülein M (1993) Stereochemistry, specificity and kintics of the hydrolysis of reduced cellodextrins by nine cellulases. Eur J Biochem 21:947–953CrossRef

Sugiyama J, Boisset C, Hashimoto M, Watanabe T (1999) Molecular directionality of β-chitin biosynthesis. J Mol Biol 286:247–255CrossRef

Teeri TT (1997) Crystalline cellulose degradation: new insight into the function of cellobiohydrolases. Trends Biotechnol 15:160–167CrossRef

Tuohy MG, Walsh DJ, Murray PG, Claeyssens M, Cuffe MM, Savage AV, Coughlan MP (2002) Kinetic parameters and mode of action of the cellobiohydrolases produced by Talaromyces emersonii. Biochim Biophys Acta 1596:366–380

Uzcategui E, Ruiz A, Montesino R, Johansson G, Pettersson G (1991) The 1, 4-β-D-glucan cellobiohydrolases from Phanerochaete crysosporium. I. A system of synergistically acting enzymes homologous to Trichoderma reesei. J Biotechnol 19:271–286CrossRef

Varrot A, Schülein M, Davies GJ (1999) Structural changes of the active site tunnel of Humicola insolens cellobiohydrolase, Cel6A, upon oligosaccharide binding. Biochemistry 38:8884–8891CrossRef

von Ossowski I, Ståhlberg J, Koivula A, Piens K, Becker D, Boer H, Harle R, Harris M, Divne C, Mahdi S, Zhao Y, Driguez H, Claeyssens M, Sinnot ML, Teeri TT (2003) Engineering the exo-loop of Trichoderma reesei cellobiohydrolase, Cel7A. A comparison with Phanerochaete chrysosporium Cel7D. J Mol Biol 333:817–829CrossRef

Vrsanska M, Biely P (1992) The cellobiohydrolase I from Trichoderma reesei QM 9414: action on cello-oligosaccharides. Carbohydr Res 227:19–27CrossRef

Watanabe K, Takemura H, Tabuchi M, Tahara N, Toyosaki H, Morinaga Y, Tsuchida T, Yano H, Yoshinaga F (2000) Cellulose-producing bacteria. US Patent 6140105

Zhang Y-HP, Lynd LR (2005) Determination of the number average degree of polymerization of cellodextrins and cellulose with application to enzymatic cellulose hydrolysis. Biomacromolecules 6:1510–1515CrossRef

Zhang Y-HP, Himmel ME, Mielenz JR (2006a) Outlook for cellulase improvement: screening and selection strategies. Biotechnol Adv 24:452–481CrossRef

Zhang Y-HP, Cui J-B, Lynd LR, Kuang LR (2006b) A transition from cellulose swelling to cellulose dissolution by o-phosphoric acid: evidence from enzymatic hydrolysis and supramolecular structure. Biomacromolecules 7:644–648CrossRef

Zverlov VV, Velikodvorskaya GA, Schwarz WH (2002) A newly described cellulosomal cellobiohydrolase, CelO from Clostridium thermocellum: investigation of exo-mode of hydrolysis, and binding capacity to crystalline cellulose. Microbiology 148:247–255

Titel: Reducing end-specific fluorescence labeled celluloses for cellulase mode of action
verfasst von: Riin Velleste
Hele Teugjas
Priit Väljamäe
Publikationsdatum: 01.02.2010
Verlag: Springer Netherlands
Erschienen in: Cellulose / Ausgabe 1/2010
Print ISSN: 0969-0239
Elektronische ISSN: 1572-882X
DOI: https://doi.org/10.1007/s10570-009-9356-3

Springer Professional

Abstract

Bitte loggen Sie sich ein, um Zugang zu Ihrer Lizenz zu erhalten.

Sie haben noch keine Lizenz? Dann Informieren Sie sich jetzt über unsere Produkte:

Springer Professional "Technik"

Springer Professional "Wirtschaft+Technik"

Weitere Artikel der Ausgabe 1/2010

ABA- and BAB-triblock cooligomers of tri-O-methylated and unmodified cello-oligosaccharides: syntheses and structure-solubility relationship

Properties of superhydrophobic paper treated with rapid expansion of supercritical CO2 containing a crystallizing wax

Dissolution mechanisms of wood cellulose fibres in NaOH–water

Evaluation of molten inorganic salt hydrates as reaction medium for the esterification of cellulose

Glucomannan composite films with cellulose nanowhiskers

Structure elucidation of uniformly 13C-labeled bacterial celluloses from different Gluconacetobacter xylinus strains