Hydrolytic properties of two cellulases of Trichoderma reesei expressed in yeast

MJ Bailey, M. Siika‐aho, A. Valkeajarvi, ME Penttila

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53 Citations (Scopus)

Abstract

Two cellulases of the filamentous fungus Trichoderma reesei, cellobiohydrolase II (CBHII, EC 3.2.1.91) and endoglucanase I (EGI, EC 3.2.1.4), produced in recombinant strains of the yeast Saccharomyces cerevisiae, were tested in the hydrolysis of cellulose, xylan and other polymeric substrates. Both enzymes were active against unsubstituted, insoluble cellulose. CBHII had greater activity than EGI against crystalline cellulose, whereas in the case of amorphous substrate the order was reversed. Evidence for synergism was obtained when mixtures of the two enzymes were used with a constant total protein dosage. The EGI was also active against soluble substituted cellulose derivatives, whereas the activity of CBHII against these substrates was insignificant. Both enzymes were active against barley (1–>3,1–>4)‐beta‐glucan, but were inactive against (1–>3,1–>6)‐beta‐glucan (laminarin). An apparent low mannan‐degrading activity of EGI against locust‐bean (Ceratonia siliqua) gum galactomannan was not confirmed when homopolymeric mannan was used as substrate in a prolonged hydrolysis test. EGI exhibited considerably greater activity against insoluble, unsubstituted hardwood xylan than against amorphous cellulose. Soluble 4‐O‐methyl‐glucuronoxylan was also attacked by EGI, although to a somewhat lesser extent than the unsubstituted xylan. By comparison with two purified xylanases of T. reesei, EGI produced xylo‐oligosaccharides with a longer mean chain length when acting on both substituted and unsubstituted xylan substrates. CBHII was inactive against xylan. 1993 The Swiss Political Science Review

Original languageEnglish
Pages (from-to)65-76
Number of pages12
JournalBiotechnology and Applied Biochemistry
Volume17
Issue number1
DOIs
Publication statusPublished - 1 Jan 1993
MoE publication typeA1 Journal article-refereed

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Cellulases
Xylans
Trichoderma
Cellulose
Yeast
Yeasts
Substrates
Enzymes
Hydrolysis
Cellulose 1,4-beta-Cellobiosidase
Cellulose derivatives
Mannans
Hardwoods
Gingiva
Hordeum
Fungi
Chain length
Fabaceae
Saccharomyces cerevisiae
Crystalline materials

Cite this

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title = "Hydrolytic properties of two cellulases of Trichoderma reesei expressed in yeast",
abstract = "Two cellulases of the filamentous fungus Trichoderma reesei, cellobiohydrolase II (CBHII, EC 3.2.1.91) and endoglucanase I (EGI, EC 3.2.1.4), produced in recombinant strains of the yeast Saccharomyces cerevisiae, were tested in the hydrolysis of cellulose, xylan and other polymeric substrates. Both enzymes were active against unsubstituted, insoluble cellulose. CBHII had greater activity than EGI against crystalline cellulose, whereas in the case of amorphous substrate the order was reversed. Evidence for synergism was obtained when mixtures of the two enzymes were used with a constant total protein dosage. The EGI was also active against soluble substituted cellulose derivatives, whereas the activity of CBHII against these substrates was insignificant. Both enzymes were active against barley (1–>3,1–>4)‐beta‐glucan, but were inactive against (1–>3,1–>6)‐beta‐glucan (laminarin). An apparent low mannan‐degrading activity of EGI against locust‐bean (Ceratonia siliqua) gum galactomannan was not confirmed when homopolymeric mannan was used as substrate in a prolonged hydrolysis test. EGI exhibited considerably greater activity against insoluble, unsubstituted hardwood xylan than against amorphous cellulose. Soluble 4‐O‐methyl‐glucuronoxylan was also attacked by EGI, although to a somewhat lesser extent than the unsubstituted xylan. By comparison with two purified xylanases of T. reesei, EGI produced xylo‐oligosaccharides with a longer mean chain length when acting on both substituted and unsubstituted xylan substrates. CBHII was inactive against xylan. 1993 The Swiss Political Science Review",
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Hydrolytic properties of two cellulases of Trichoderma reesei expressed in yeast. / Bailey, MJ; Siika‐aho, M.; Valkeajarvi, A.; Penttila, ME.

In: Biotechnology and Applied Biochemistry, Vol. 17, No. 1, 01.01.1993, p. 65-76.

Research output: Contribution to journalArticleScientificpeer-review

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AU - Bailey, MJ

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AU - Valkeajarvi, A.

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AB - Two cellulases of the filamentous fungus Trichoderma reesei, cellobiohydrolase II (CBHII, EC 3.2.1.91) and endoglucanase I (EGI, EC 3.2.1.4), produced in recombinant strains of the yeast Saccharomyces cerevisiae, were tested in the hydrolysis of cellulose, xylan and other polymeric substrates. Both enzymes were active against unsubstituted, insoluble cellulose. CBHII had greater activity than EGI against crystalline cellulose, whereas in the case of amorphous substrate the order was reversed. Evidence for synergism was obtained when mixtures of the two enzymes were used with a constant total protein dosage. The EGI was also active against soluble substituted cellulose derivatives, whereas the activity of CBHII against these substrates was insignificant. Both enzymes were active against barley (1–>3,1–>4)‐beta‐glucan, but were inactive against (1–>3,1–>6)‐beta‐glucan (laminarin). An apparent low mannan‐degrading activity of EGI against locust‐bean (Ceratonia siliqua) gum galactomannan was not confirmed when homopolymeric mannan was used as substrate in a prolonged hydrolysis test. EGI exhibited considerably greater activity against insoluble, unsubstituted hardwood xylan than against amorphous cellulose. Soluble 4‐O‐methyl‐glucuronoxylan was also attacked by EGI, although to a somewhat lesser extent than the unsubstituted xylan. By comparison with two purified xylanases of T. reesei, EGI produced xylo‐oligosaccharides with a longer mean chain length when acting on both substituted and unsubstituted xylan substrates. CBHII was inactive against xylan. 1993 The Swiss Political Science Review

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