Mechanism of action of the <i>endo</i>‐(1 → 3)‐α‐glucanase MutAp from the mycoparasitic fungus <i>Trichoderma harzianum</i>

Grün, Christian H.; Dekker, Natashe Lemos; Nieuwland, Alexander A.; Klis, Frans M.; Kamerling, Johannis P.; Vliegenthart, Johannes F.G.; Hochstenbach, Frans

doi:10.1016/j.febslet.2006.05.062

Cited by 30 publications

(22 citation statements)

References 42 publications

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“…According to the literatures [20][21][22][23][24], two anomeric signals for typical ␣-glycosidic configurations appeared at 101.0 and 100.5 ppm in 13 C NMR spectrum (Fig. 2), consistent with the value of specific rotation and FT-IR spectrum.…”

Section: Isolation and Structure Characterization Of Akpsupporting

confidence: 86%

Structure elucidation and antioxidant activity of a novel α-(1→3),(1→4)-d-glucan from Aconitum kusnezoffii Reichb.

Gao

et al. 2010

International Journal of Biological Macromolecules

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Section: Isolation and Structure Characterization Of Akpsupporting

confidence: 86%

Structure elucidation and antioxidant activity of a novel α-(1→3),(1→4)-d-glucan from Aconitum kusnezoffii Reichb.

Gao

et al. 2010

International Journal of Biological Macromolecules

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“…Gradient conditions for HPLC analysis were as follows: time at 0 min (t = 0), 100% solvent A (0.8 ml/min); at 6 min, 86% solvent A (0.8 ml/min); at 35 min, 54.7% solvent A (0.8 ml/min); at 37 min, 5% solvent A (1 ml/min); at 41 min, 86% solvent A (1 ml/min); at 42 min, 86% solvent A (1.2 ml/min); and at 55 min, 86% solvent A (0.8 ml/min). (1,3)-α-Glucan oligosaccharides were purified as described in Grün et al (2006) and used as a standard.…”

Section: Product Analysismentioning

confidence: 99%

Role of the α‐glucanase Agn2p in ascus‐wall endolysis following sporulation in fission yeast

Dekker

Rijssel

Distel

et al. 2007

Yeast

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During sporulation in the ascomyceteous fungus Schizosaccharomyces pombe, diploid cells undergo differentiation into asci containing four haploid ascospores, which are highly resistant to environmental stresses. Although the morphogenetic processes involved in ascospore formation have been studied extensively, little is known about the molecular mechanism that ensures the release of mature ascospores from the ascus, allowing their dispersal into the environment. Recently, we identified Agn2p as the paralogue of the characterized endo-(1,3)-α-glucanase Agn1p, and observed that asci deleted for agn2 are defective in ascospore dispersal. Here, we focus on the cellular and biochemical functions of Agn2p. By placing agn2 under the control of an inducible promoter, we show that expression of agn2 is required for the efficient release of ascospores from their asci. Furthermore, we characterize the enzyme activity of purified recombinant Agn2p and show that Agn2p, like Agn1p, is an endo-(1,3)-α-glucanase that produces predominantly (1,3)-α-glucan pentasaccharides. Finally, we demonstrate that exogenous addition of purified Agn2p liberated the ascospores from asci deleted for agn2. We propose that Agn2p participates in the endolysis of the ascus wall by hydrolysing its (1,3)-α-glucan, thereby assisting in the release of ascospores.

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“…It is likely that similar findings were observed wherein α-glucanase from Trichoderma harzianum cleaved α-1,3-linkages in some insolu- ble glucans of streptococci. 10,11) Thus, the present mutanase from fermented food should be able to hydrolyze and solubilize glucans in biofilms formed by cariogenic streptococci in vivo. 12) …”

Section: Mutanase Hydrolyzed Insoluble Glucans Which Were Synthesizementioning

confidence: 99%

Substrate Specificity of Mutanase of Paenibacillus humicus from Fermented Food

Tsumori

Shimamura

Sakurai

et al. 2011

JOURNAL OF HEALTH SCIENCE

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Mutanase, α-1,3-glucanase, catalyzes the hydrolysis of α-1,3-glucans, and is expected for preventive medicine, since the enzyme has an ability for hydrolysis of insoluble glucans that are synthesized by cariogenic streptococci. We previously isolated the mutanase of Paenibacillus humicus from fermented soybeans. In the present study, Paenibacillus mutanase was characterized with respect to its hydrolysis efficiency of insoluble glucans, and mode of action on α-1,3-glucan oligosaccharides. Recombinant mutanase hydrolyzed insoluble glucans of cariogenic streptococci efficiently. Enzymatic reaction on hydrolysis of mutan, we assumed that the enzyme cleaved the substrate in an endo-catalytic manner. The hydrolysis of α-1,3-glucan oligosaccharides gave α-1,3-glucan tetrasaccharide as the primary final product but α-1,3-glucan pentasaccharide was the minimal size of substrate on which the enzyme catalyzed. Mutanase hydrolyzed borohydride-treated α-1,3-glucan hexasaccharide into the tetrasaccharide and the disaccharide-alditol. Thus, the enzyme cleaved the fourth α-1,3-glucosidic linkage from the non-reducing end of the oligosaccharides. Mutanase in fermented food should be capable of removing streptococcal insoluble glucans that can induce dental caries.

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Mechanism of action of the endo‐(1 → 3)‐α‐glucanase MutAp from the mycoparasitic fungus Trichoderma harzianum

Cited by 30 publications

References 42 publications

Structure elucidation and antioxidant activity of a novel α-(1→3),(1→4)-d-glucan from Aconitum kusnezoffii Reichb.

Structure elucidation and antioxidant activity of a novel α-(1→3),(1→4)-d-glucan from Aconitum kusnezoffii Reichb.

Role of the α‐glucanase Agn2p in ascus‐wall endolysis following sporulation in fission yeast

Substrate Specificity of Mutanase of Paenibacillus humicus from Fermented Food

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