Characteristics of the Amylase and its Related Enzymes Produced by Ectomycorrhizal Fungus <i>Tricholoma matsutake</i>

Hur, Tae-Chul; Ka, Kang-Hyun; Joo, Seon-Tea; Terashita, Takao

doi:10.1080/12298093.2001.12015785

Cited by 15 publications

(16 citation statements)

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“…Terashita et al (2000b) reported that the amylase activity of T. matsutake was higher in starch that originated from barley grains than that which originated from other sources. Then, Hur et al (2001) reported amylase production and the enzymatic properties of partially purified amylases from T. matsutake. There are several reports about the purification procedures of the enzymes and some properties of glucoamylase and α-glucosidase from wood-rotting mushrooms such as Schizophyllum commune Fr.…”

Section: Discussionmentioning

confidence: 99%

“…However, in practice it is very difficult to cultivate large amounts of mycelia using monosaccharides in a pure culture because of the osmotic pressure in the medium (Ohta 1997). In particular, the most serious barrier for the artificial cultivation of the mushroom is that the mycelium of T. matsutake grows so slowly on the artificial media (about 2 cm/month) and has low capability to decompose polysaccharides (Hur et al 2001). Little research has been conducted on hydrolytic enzymes of mycorrhizal mushrooms.…”

Section: Discussionmentioning

confidence: 99%

“…Lee et al (1998) reported that the fungus had relatively high amylase activity among the extracellular enzymes. Hur et al (2001) also reported that amylase activities were variable among isolated T. matsutake.…”

Section: Introductionmentioning

confidence: 94%

“…Therefore, for artificial cultivation of this fungus, starch-hydrolyzing ability (amylases) is very important because the fungus has previously not been known to use many other polysaccharides except starch (Hur et al 2001). However, no characterization of highly purified α-amylase from a mushroom origin involving a mycorrhizal fungus has been reported.…”

Section: Introductionmentioning

confidence: 99%

“…Furthermore, it was reported (Terashita et al 2000b) that amylase activities in the culture filtrate of T. matsutake had relatively high values at 80 days after inoculation. Hur et al (2001) characterized the amylases produced by T. matsutake and its related enzymes. However, these enzymes were only partially purified enzymes.…”

Section: Introductionmentioning

confidence: 99%

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Purification and some properties of α-amylase from an ectomycorrhizal fungus, Tricholoma matsutake

et al. 2003

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α-Amylase from a still culture filtrate of Tricholoma matsutake, an ectomycorrhizal fungus, was isolated and characterized. The enzyme was purified to a homogeneous preparation with Toyopearl-DEAE, gel filtration, and Mono Q column chromatography. The α-amylase was highly purified (3580 fold) with a recovery of 10.5% and showed a single protein band by SDS-PAGE. The enzyme was most active at pH 5.0-6.0 toward soluble starch and stable within the broad pH range 4.0-10.0. This α-amylase was a relatively thermostable enzyme (optimum temperature, 60°C; thermal stability, 50°C). The molecular mass was 34 kDa by size-exclusion chromatography and 46 kDa by SDS-PAGE. This enzyme was not inhibited by the Hg 2ϩ ion. Measurement of viscosity and TLC and HPLC analysis of the hydrolysates obtained from amylose showed that the amylase from T. matsutake is an endo-type (α-amylase). Substrate specificity was tested using amylose with different polysaccharides. This α-amylase readily hydrolyzed the α-1,4 glucoside bond in soluble starch and amylose A (MW, 2900), but did not hydrolyze the α-1,6 bond and cyclic polysaccharides such as α-and -cyclodextrin.

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 94%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 3 more Smart Citations