Purification and Characterisation of a Fungal beta-Mannanase.

Eriksson, Karl‐Erik; Winell, Margareta

doi:10.3891/acta.chem.scand.22-1924

Cited by 50 publications

(17 citation statements)

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“…Di-and trioligosaccharides, along with minor amounts of monosaccharide were the main reaction products. A similar pattern of formation of fl-mannan degradation products has been observed for A. niger (Eriksson and Winell 1968) and P. purpurogenum (Kusakabe et al 1988). The latter two fungal enzymes have been classified as endofl-mannanases (Eriksson et al 1990).…”

Section: Properties Of the Purified Fl-mannanasesupporting

confidence: 57%

Purification, and characterization of a β-mannanase of Trichoderma reesei C-30

Arisan-Atac

Hodits

Kristufek

et al. 1993

Appl Microbiol Biotechnol

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Trichoderma reesei was studied for its ability to produce fl-mannanase activity on a variety of carbon sources. The highest fl-mannanase activity was produced on cellulose, whereas fl-mannan-containing carbon sources (such as konjac powder or locust bean gum) gave lower enzyme titres. The enzyme responsible for the major fl-mannanolytic activity from T. reesei was purified to physical homogeneity by preparative chromatofocusing and anion exchange fast protein liquid chromatography. This fl-mannanase is a glycoprotein, with a molecular mass of 46 (+ 2) kDa and an isoelectric point of 5.2. It has an optimal pH at 5.0 and broad pH stability (2.5-7.0). It is stable for 60 min at 55 ° C, and has an optimal temperature for activity at 75 ° C. During incubation with locust bean gum, the enzyme releases mainly tri-and disaccharides.

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Section: Properties Of the Purified Fl-mannanasesupporting

confidence: 57%

Purification, and characterization of a β-mannanase of Trichoderma reesei C-30

Arisan-Atac

Hodits

Kristufek

et al. 1993

Appl Microbiol Biotechnol

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“…The presence of galactose residues on the mannan backbone significantly hinders the activity of ␤-mannanase (252), but this effect is small if the galactose residues in the vicinity of the cleavage point are all on the same side of the main chain (251). ␤-Mannanases release predominantly mannobiose and mannotriose from mannan, confirming that they are true endohydrolases (4,64,105,306). It has been shown that A. niger ␤-mannanase binds to four mannose residues during catalysis (249).…”

Section: Degradation Of the Galacto(gluco)mannan Backbonementioning

confidence: 70%

AspergillusEnzymes Involved in Degradation of Plant Cell Wall Polysaccharides

Vries

Visser

2001

Microbiol Mol Biol Rev

877

585

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SUMMARY Degradation of plant cell wall polysaccharides is of major importance in the food and feed, beverage, textile, and paper and pulp industries, as well as in several other industrial production processes. Enzymatic degradation of these polymers has received attention for many years and is becoming a more and more attractive alternative to chemical and mechanical processes. Over the past 15 years, much progress has been made in elucidating the structural characteristics of these polysaccharides and in characterizing the enzymes involved in their degradation and the genes of biotechnologically relevant microorganisms encoding these enzymes. The members of the fungal genus Aspergillus are commonly used for the production of polysaccharide-degrading enzymes. This genus produces a wide spectrum of cell wall-degrading enzymes, allowing not only complete degradation of the polysaccharides but also tailored modifications by using specific enzymes purified from these fungi. This review summarizes our current knowledge of the cell wall polysaccharide-degrading enzymes from aspergilli and the genes by which they are encoded.

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“…Activity was measured at pH 5 because of the high enzyme stability, and previous reports for other mannanases indicated that this value was close to the optimal. 13,27 Reported optimal pHs for mannanases produced by fungi range from 3.2 for one puri®ed from Sclerotium rolfsii, 30 one having two optima (3.0 and 3.8) puri®ed from Aspergillus sp, 13 to 5.4 for one produced by Trichoderma reesei. 27 The optimal pH found here is therefore higher than other reported optima and allows high b-mannanase activity at nearneutral pH values.…”

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confidence: 99%

“…31 Other optima are in between, such as 72 and 74°C for two mannanases of Sclerotium rolfsii when glucomannan was used as inducer, 30 and one from Aspergillus sp (65°C). 13 The optimal temperature of a b-mannanase from Aspergillus tamarii was not fully evaluated, but its maximum stability was at 37°C. 32 Thus our puri®ed b-mannanase has one of the lowest reported optimal temperatures and could be used ef®ciently in processes where relatively low temperatures are required, such as viscosity reduction of concentrated liquid coffee extract to reduce energy costs in instant coffee manufacture.…”

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confidence: 99%