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

193 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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