Purification and characterization of two β-mannanases from Trichoderma reesei

Henrik Stålbrand, Matti Siika-aho (Corresponding Author), Maija Tenkanen, Liisa Viikari

Research output: Contribution to journalArticleScientificpeer-review

188 Citations (Scopus)

Abstract

Five enzymes with mannanase activity were separated from Trichoderma reesei culture filtrate using analytical isoelectric focusing and subsequently detected with the zymogram technique. The crude enzymes had isoelectric points in the range of 3.6–6.5. Two of the mannanases with pI values of 4.6 and 5.4 were purified using ion-exchange chromatography, affinity chromatography and chromatofocusing. The molecular weights determined with SDS-PAGE were 51 000 (mannanase pI 4.6) and 53 000 (mannanase pI 5.4). The two enzymes had similar properties with respect to pH optimae and pH stabilities. Both mannanases hydrolyzed ivory nut mannan mainly to mannotriose and mannobiose. The specific activities (against locust bean gum) of the purified enzymes were 1860 and 1430 nkat mg−1 for the pI 4.6 and pI 5.4 mannanases, respectively.

Original languageEnglish
Pages (from-to)229 - 242
Number of pages14
JournalJournal of Biotechnology
Volume29
Issue number3
DOIs
Publication statusPublished - 1993
MoE publication typeA1 Journal article-refereed

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Trichoderma
Purification
Enzymes
Affinity chromatography
Mannans
Nuts
Ion Exchange Chromatography
Isoelectric Point
Isoelectric Focusing
Chromatography
Affinity Chromatography
Polyacrylamide Gel Electrophoresis
Ion exchange
Molecular Weight
Molecular weight

Cite this

Stålbrand, Henrik ; Siika-aho, Matti ; Tenkanen, Maija ; Viikari, Liisa. / Purification and characterization of two β-mannanases from Trichoderma reesei. In: Journal of Biotechnology. 1993 ; Vol. 29, No. 3. pp. 229 - 242.
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Purification and characterization of two β-mannanases from Trichoderma reesei. / Stålbrand, Henrik; Siika-aho, Matti (Corresponding Author); Tenkanen, Maija; Viikari, Liisa.

In: Journal of Biotechnology, Vol. 29, No. 3, 1993, p. 229 - 242.

Research output: Contribution to journalArticleScientificpeer-review

TY - JOUR

T1 - Purification and characterization of two β-mannanases from Trichoderma reesei

AU - Stålbrand, Henrik

AU - Siika-aho, Matti

AU - Tenkanen, Maija

AU - Viikari, Liisa

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AB - Five enzymes with mannanase activity were separated from Trichoderma reesei culture filtrate using analytical isoelectric focusing and subsequently detected with the zymogram technique. The crude enzymes had isoelectric points in the range of 3.6–6.5. Two of the mannanases with pI values of 4.6 and 5.4 were purified using ion-exchange chromatography, affinity chromatography and chromatofocusing. The molecular weights determined with SDS-PAGE were 51 000 (mannanase pI 4.6) and 53 000 (mannanase pI 5.4). The two enzymes had similar properties with respect to pH optimae and pH stabilities. Both mannanases hydrolyzed ivory nut mannan mainly to mannotriose and mannobiose. The specific activities (against locust bean gum) of the purified enzymes were 1860 and 1430 nkat mg−1 for the pI 4.6 and pI 5.4 mannanases, respectively.

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