nach oben

Biomass Conversion and Biorefinery

Erschienen in:

06.04.2022 | Original Article

Extracellular enzyme production by different species of Trichoderma fungus for lemon peel waste bioconversion

verfasst von: Ramin Gooruee, Mohammad Hojjati, Behrooz Alizadeh Behbahani, Samira Shahbazi, Hamed Askari

Erschienen in: Biomass Conversion and Biorefinery | Ausgabe 2/2024

Einloggen

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

search-config

KI-gestützte Suche

Aus

Abstract

In this study, extracellular enzyme production by different species of Trichoderma fungus (T. aureoviride NAS106, T. afroharzianum NAS107, T. ghanense NAS108, T. pleuroticola NAS109, T. harzianum NAS110, and T. lixii NAS114) were investigated under submerged fermentation conditions using lemon peel waste as a substrate at 28 °C, pH 5, and fermentation time of 48 h. Extracellular protein concentration, cellulose (exoglucanase, endoglucanase, β-glucosidase, and total cellulase), xylanase, and pectinase enzyme activity were also assayed. This study also examined the effect of different fermentation times on extracellular protein production and enzymatic activity in a superior strain of Trichoderma. The molecular weight of extracellular proteins was studied using SDS-PAGE. The results showed that the highest extracellular protein concentration and exoglucanase, endoglucanase, beta-glucosidase, total cellulase, xylanase, and pectinase activity were produced in T. afroharzianum NAS107. It was also revealed that the major activity of the total cellulase enzyme was due to the synergistic function of endoglucanases and cellulohydrolases. In addition, the electrophoretic pattern of protein bands of this species showed the ability to produce enzymes of xylanase (Xyl I), exoglucanase (Cel 6A (CBH II) and Cel7A (CBH I)), endoglucanases (Cel 5A (EG II), and Cel 12A (EG III), β-glucosidase (Cel3A (BGL I) and Cel 1A (BGL II)), polygalacturonase I and II, pectin lyase, and pectin esterase I and II, with the highest enzymatic activity during the fermentation period of 96 to 120 h due to the synergistic activity of exoglucanase, endoglucanase, beta-glucosidase, and xylanase enzymes. The findings of this study showed that T. afroharzianum is a suitable producer of extracellular enzymes cellulase, xylanase, and pectinase. Thus, it can be used as a biological substance or an enzyme source for saccharification of citrus conversion industry wastes such as lemon peel.

Vorheriger Artikel Fabrication of biochar@Cu-Ni nanocatalyst for reduction of aryl aldehyde and nitroarene compounds

Nächster Artikel Process optimisation for improvement of crystallinity index of cellulose nanofibre from Imperata cylindrica by Taguchi methodology

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

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

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

Bilal M, Iqbal HM, Hu H, Wang W, Zhang X (2018) Metabolic engineering and enzyme-mediated processing: a biotechnological venture towards biofuel production–a review. Renew Sustain Energy Rev 82:436–447. https://doi.org/10.1016/j.rser.2017.09.070CrossRef

FN Niyonzima 2021 Detergent-compatible fungal cellulases Folia microbiologica 66 25 40 https://doi.org/10.1007/s12223-020-00838-w

Buenrostro-Figueroa J, de la Garza-Toledo H, Ibarra-Junquera V, Aguilar CN (2010) Juice extraction from mango pulp using an enzymatic complex of Trichoderma sp. produced by solid-state fermentation. Food Sci Biotechnol 19:1387–1390. https://doi.org/10.1007/s10068-010-0197-5CrossRef

Sun J, Lu J, Xie G (2018) Secretome analysis of Trichoderma reesei CICC41495 for degradation of arabinoxylan in malted barley. J Inst Brew 124:352–358. https://doi.org/10.1002/jib.505CrossRef

Verma N, Kumar V, Bansal MC (2018) Utility of Luffa cylindrica and Litchi chinensis peel, an agricultural waste biomass in cellulase production by Trichoderma reesei under solid state cultivation. Biocatal Agric Biotechnol 16:483–492. https://doi.org/10.1016/j.bcab.2018.09.021CrossRef

Al-Maqtari QA, Waleed A-A, Mahdi AA (2019) Microbial enzymes produced by fermentation and their applications in the food industry-a review. Int J Agric Innov Res 8:62–82

Carvalho EA, dos Santos Góes LM, Uetanabaro APT, da Silva EGP, Rodrigues LB, Pirovani CP, da Costa AM (2017) Thermoresistant xylanases from Trichoderma stromaticum: application in bread making and manufacturing xylo-oligosaccharides. Food Chem 221:1499–1506. https://doi.org/10.1016/j.foodchem.2016.10.144CrossRef

Schuster A, Schmoll M (2010) Biology and biotechnology of Trichoderma. Appl Microbiol Biotechnol 87:787–799. https://doi.org/10.1007/s00253-010-2632-1CrossRef

AC Costa da GF Cavalheiro ER Queiroz Vieira de JR Gandra e BuschinelliRHdT, da Paz MF, Fonseca GG, Leite RSR, 2019 Catalytic properties of xylanases produced by Trichoderma piluliferum and Trichoderma viride and their application as additives in bovine feeding Biocatal Agric Biotechnol 19 101161 https://doi.org/10.1016/j.bcab.2019.101161

10.

N Srivastava M Srivastava A Alhazmi T Kausar S Haque R Singh PW Ramteke PK Mishra M Tuohy M Leitgeb 2021 Technological advances for improving fungal cellulase production from fruit wastes for bioenergy application: a review Environ Pollut 117370 https://doi.org/10.1016/j.envpol.2021.117370

11.

Arora N, Banerjee AK, Mutyala S, Murty US (2009) Comparative characterization of commercially important xylanase enzymes. Bioinformation 3:446. https://doi.org/10.6026/97320630003446CrossRef

12.

Prasanna H, Ramanjaneyulu G, Reddy BR (2016) Optimization of cellulase production by Penicillium sp. 3 Biotech 6: 1–11. https://doi.org/10.1007/s13205-016-0483-x

13.

Bansal N, Tewari R, Soni R, Soni SK (2012) Production of cellulases from Aspergillus niger NS-2 in solid state fermentation on agricultural and kitchen waste residues. Waste Manage 32:1341–1346. https://doi.org/10.1016/j.wasman.2012.03.006CrossRef

14.

Liu J, Yang J, Wang R, Liu L, Zhang Y, Bao H, Jang JM, Wang E, Yuan H (2020) Comparative characterization of extracellular enzymes secreted by Phanerochaete chrysosporium during solid-state and submerged fermentation. Int J Biol Macromol 152:288–294. https://doi.org/10.1016/j.ijbiomac.2020.02.256CrossRef

15.

Kunamneni A, Plou FJ, Alcalde M, Ballesteros A (2014) Trichoderma enzymes for food industries. in: Biotechnology and biology of Trichoderma. Elsevier, pp 339–344. https://doi.org/10.1016/B978-0-444-59576-8.00024-2

16.

Burkert J, Maugeri F, Rodrigues M (2004) Optimization of extracellular lipase production by Geotrichum sp. using factorial design. Biores Technol 91:77–84. https://doi.org/10.1016/S0960-8524(03)00152-4CrossRef

17.

N Verma V Kumar 2020 Utilization of bottle gourd vegetable peel waste biomass in cellulase production by Trichoderma reesei and Neurosporacrassa Biomass Convers Biorefine 1–10 https://doi.org/10.1007/s13399-020-00727-9

18.

Zehra M, Syed MN, Sohail M (2020) Banana peels: a promising substrate for the coproduction of pectinase and xylanase from Aspergillus fumigatus MS16. Polish journal of microbiology 69: 19–26. https://doi.org/10.33073/pjm-2020-002

19.

Irfan M, Bakhtawar J, Sadia S, Shakir HA, Khan M, Ali S (2020) Utilization of fruit wastes for enzyme production in submerged fermentation. International Journal of Biology and Chemistry 13: 88–95. https://doi.org/10.26577/ijbch.2020.v13.i2.11

20.

Ruiz HA, Rodríguez-Jasso RM, Rodríguez R, Contreras-Esquivel JC, Aguilar CN (2012) Pectinase production from lemon peel pomace as support and carbon source in solid-state fermentation column-tray bioreactor. Biochem Eng J 65:90–95. https://doi.org/10.1016/j.bej.2012.03.007CrossRef

21.

Mukherjee R, Paul T, Soren JP, Halder SK, Mondal KC, Pati BR, Mohapatra PKD (2019) Acidophilic α-amylase production from Aspergillus niger RBP7 using potato peel as substrate: a waste to value added approach. Waste biomass valoriz 10:851–863. https://doi.org/10.1007/s12649-017-0114-8CrossRef

22.

Mamma D, Kourtoglou E, Christakopoulos P (2008) Fungal multienzyme production on industrial by-products of the citrus-processing industry. Biores Technol 99:2373–2383. https://doi.org/10.1016/j.biortech.2007.05.018CrossRef

23.

Li P-J, Xia J-L, Shan Y, Nie Z-Y, Su D-L, Gao Q-R, Zhang C, Ma Y-L (2015) Optimizing production of pectinase from orange peel by Penicillium oxalicum PJ02 using response surface methodology. Waste Biomass Valoriz 6:13–22. https://doi.org/10.1007/s12649-014-9317-4CrossRef

24.

FAO (2019) Food and Agriculture Organization Citrus production data. http://www.fao.org. 10 Aug 2021

25.

Al-Qudah TS, Zahra U, Rehman R, Majeed MI, Sadique S, Nisar S, Tahtamouni R, Tahtamouni RW (2018) Lemon as a source of functional and medicinal ingredient: a review. Int J Chem Biochem Sci 14:55–61

26.

Sharma H, Singh I, Misra JP (2019) Mechanical and thermal behaviour of food waste (Citrus limetta peel) fillers–based novel epoxy composites. Polym Polym Compos 27:527–535. https://doi.org/10.1177/0967391119851012CrossRef

27.

Gómez-Mejía E, Rosales-Conrado N, León-González ME, Madrid Y (2019) Citrus peels waste as a source of value-added compounds: Extraction and quantification of bioactive polyphenols. Food Chem 295:289–299. https://doi.org/10.1016/j.foodchem.2019.05.136CrossRef

28.

Garcia-Castello EM, Rodriguez-Lopez AD, Mayor L, Ballesteros R, Conidi C, Cassano A (2015) Optimization of conventional and ultrasound assisted extraction of flavonoids from grapefruit (Citrus paradisi L.) solid wastes. LWT-Food Sci Technol 64:1114–1122. https://doi.org/10.1016/j.lwt.2015.07.024CrossRef

29.

Bagde PP, Dhenge S, Bhivgade S (2017) Extraction of pectin from orange peel and lemon peel. Int J Eng Technol Sci Res 4:1–7

30.

AOAC (2000) Official methods of analysis Seventeenth edn. Association of Official Analytical Chemists, Gaithersburg

31.

Shahbazi S, Askari H (2018) Investigating of the influence of cellulase enzymes from mutated isolates of Trichoderma harzianum and T. viride on biodegradation of cellulose Iα, Iβ and III. Agric Biotechnol https://doi.org/10.22084/AB.2018.7877.1249

32.

Shahbazi S, Askari H, Mojerlou S (2016) The impact of different physicochemical parameters of fermentation on extracellular cellulolytic enzyme production by Trichoderma harzianum. J Crop Protect 5: 397–412. https://doi.org/10.18869/modares.jcp.5.3.397

33.

Bradford MM (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72:248–254. https://doi.org/10.1016/0003-2697(76)90527-3CrossRef

34.

Gama F, Mota M (1998) Cellulases for oligosaccharide synthesis: a preliminary study. Carbohyd Polym 37:279–281. https://doi.org/10.1016/S0144-8617(98)00071-XCrossRef

35.

Laemmli UK (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. nature 227: 680–685. https://doi.org/10.1038/227680a0

36.

Chinedu SN, Okochi V, Omidiji O (2011) Cellulase production by wild strains of Aspergillus niger, Penicillium chrysogenum and Trichoderma harzianum grown on waste cellulosic materials. IFE J Sci 13:57–62

37.

Durand H, Clanet M, Tiraby G (1988) Genetic improvement of Trichoderma reesei for large scale cellulase production. Enzyme Microb Technol 10:341–346. https://doi.org/10.1016/0141-0229(88)90012-9CrossRef

38.

Askari H, Shahbazi S (2018) Improvement of cellulose degrading enzymes activity by mutagenesis in Trichoderma reesei fungi. Agricultural Biotechnology 9:41–50

39.

Shahbazi S, Askari H, Ebrahimi A, Safaeie M, Karimi M (2015) Increasing the efficiency of sugar beet pulp saccharification by Trichoderma reesei superior mutants for bioethanol production. Journal of Sugar Beet 31 :61–76. https://doi.org/10.22092/JSB.2015.101498.

40.

Wood TM, Bhat KM (1988) Methods for measuring cellulase activities. Methods Enzymol 160:87–112. https://doi.org/10.1016/0076-6879(88)60109-1CrossRef

41.

van Tilbeurgh H, Claeyssens M, de Bruyne CK (1982) The use of 4-methylumbelliferyl and other chromophoric glycosides in the study of cellulolytic enzymes. FEBS Lett 149:152–156. https://doi.org/10.1016/0014-5793(82)81092-2CrossRef

42.

H Tilbeurgh van G Pettersson R Bhikabhai H Boeck de CLAEYSSENS M, 1985 Studies of the cellulolytic system of Trichoderma reesei QM 9414: reaction specificity and thermodynamics of interactions of small substrates and ligands with the 1, 4-β-glucan cellobiohydrolase II Eur J Biochem 148 329 334 https://doi.org/10.1111/j.1432-1033.1985.tb08843.x

43.

Väljamäe P, Sild V, Pettersson G, Johansson G (1998) The initial kinetics of hydrolysis by cellobiohydrolases I and II is consistent with a cellulose surface− erosion model. Eur J Biochem 253:469–475. https://doi.org/10.1046/j.1432-1327.1998.2530469.xCrossRef

44.

Srisodsuk M, Kleman-Leyer K, Keränen S, Kirk TK, Teeri TT (1998) Modes of action on cotton and bacterial cellulose of a homologous endoglucanase-exoglucanase pair from Trichoderma reesei. Eur J Biochem 251:885–892. https://doi.org/10.1046/j.1432-1327.1998.2510885.xCrossRef

45.

Nidetzky B, Claeyssens M (1994) Specific quantification of Trichoderma reesei cellulases in reconstituted mixtures and its application to cellulase–cellulose binding studies. Biotechnol Bioeng 44:961–966. https://doi.org/10.1002/bit.260440812CrossRef

46.

Medve J, Ståhlberg J, Tjerneld F (1994) Adsorption and synergism of cellobiohydrolase I and II of Trichoderma reesei during hydrolysis of microcrystalline cellulose. Biotechnol Bioeng 44:1064–1073. https://doi.org/10.1002/bit.260440907CrossRef

47.

Klyosov AA (1990) Trends in biochemistry and enzymology of cellulose degradation. Biochemistry 29:10577–10585. https://doi.org/10.1021/bi00499a001CrossRef

48.

Shoemaker S, Brown Jr R (1978) Characterization of endo-1, 4-β-d-glucanases purified from Trichoderma viride. Biochimica et Biophysica Acta (BBA)-Enzymology 523: 147–161. https://doi.org/10.1016/0005-2744(78)90017-7

49.

Zhang YHP, Lynd LR (2004) Toward an aggregated understanding of enzymatic hydrolysis of cellulose: noncomplexed cellulase systems. Biotechnol Bioeng 88:797–824. https://doi.org/10.1002/bit.20282CrossRef

50.

Teeri T, Koivula A (1995) Cellulose degradation by native and engineered fungal cellulases. Carbohydr Eur 12:28–33

51.

Zhang S, Wolfgang DE, Wilson DB (1999) Substrate heterogeneity causes the nonlinear kinetics of insoluble cellulose hydrolysis. Biotechnol Bioeng 66:35–41. https://doi.org/10.1002/(SICI)1097-0290(1999)66:1CrossRef

52.

Zhang YHP, Lynd LR (2006) A functionally based model for hydrolysis of cellulose by fungal cellulase. Biotechnol Bioeng 94:888–898. https://doi.org/10.1002/bit.20906CrossRef

53.

Fortkamp D, Knob A (2014) High xylanase production by Trichoderma viride using pineapple peel as substrate and its apllication in pulp biobleaching. Afr J Biotech 13:2248–2259. https://doi.org/10.5897/AJB2013.13479CrossRef

54.

Lappalainen A, Siika-Aho M, Kalkkinen N, Fagerström R, Tenkanen M (2000) Endoxylanase II from Trichoderma reesei has several isoforms with different isoelectric points. Biotechnol Appl Biochem 31:61–68. https://doi.org/10.1042/BA19990066CrossRef

55.

Stålbrand H, Siika-aho M, Tenkanen M, Viikari L (1993) Purification and characterization of two β-mannanases from Trichoderma reesei. J Biotechnol 29:229–242. https://doi.org/10.1016/0168-1656(93)90055-RCrossRef

56.

Mohamed SA, Al-Malki AL, Kumosani TA (2009) Characterization of a polygalacturonase from Trichoderma harzianum grown on citrus peel with application for apple juice. Aust J Basic Appl Sci 3:2770–2777

57.

T Kobayashi K Koike T Yoshimatsu N HigakiSUzUMATSU A, OzAwA T, Hatada Y, Ito S, 1999 Purification and properties of a low-molecular-weight, high-alkaline pectate lyase from an alkaliphilic strain of Bacillus Biosci Biotechnol Biochem 63 65 72 https://doi.org/10.1271/bbb.63.65

58.

Semenova M, Grishutin S, Gusakov A, Okunev O, Sinitsyn A (2003) Isolation and properties of pectinases from the fungus Aspergillus japonicus. Biochem Mosc 68:559–569. https://doi.org/10.1023/A:1023959727067CrossRef

59.

LD Kluskens ALEBEEK G-JWv, Voragen AG, VOS WMd, OOST Jvd, 2003 Molecular and biochemical characterization of the thermoactive family 1 pectate lyase from the hyperthermophilic bacterium Thermotoga maritima Biochem J 370 651 659 https://doi.org/10.1042/bj20021595

Titel: Extracellular enzyme production by different species of Trichoderma fungus for lemon peel waste bioconversion
verfasst von: Ramin Gooruee
Mohammad Hojjati
Behrooz Alizadeh Behbahani
Samira Shahbazi
Hamed Askari
Publikationsdatum: 06.04.2022
Verlag: Springer Berlin Heidelberg
Erschienen in: Biomass Conversion and Biorefinery / Ausgabe 2/2024
Print ISSN: 2190-6815
Elektronische ISSN: 2190-6823
DOI: https://doi.org/10.1007/s13399-022-02626-7

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 "Wirtschaft+Technik"

Springer Professional "Technik"

Weitere Artikel der Ausgabe 2/2024

Preparation of bagasse pith-derived biochar for high-efficiency removal of Cr(VI) and further hydrogenation of furfural

Practical aspects of biowastes conversion to fertilizers

Strategic utilization of groundnut shell (Arachis hypogaea) immobilized bacterial consortium for enhanced 4-nitrophenol remediation: statistical optimization, kinetic modeling, and reusability

Enhanced production of bacterial hydrolytic endoglucanase enzyme using waste leaves of water hyacinth and its thermal stability under the influence of TiO2 nanoparticles

Zirconium-lignin hybrid catalyst for the Meerwein-Ponndorf-Verley reduction of biomass-derived 5-hydroxymethylfurfural to 2,5-bis(hydroxymethyl)furan

Study on the co-pyrolysis characteristics of sewage sludge and wood powder and kinetic analysis