Production of extracellular debranching activity by amylolytic yeasts

Mot, René De; Oudendijck, E. Van; Verachtert, Hubert

doi:10.1007/bf00135686

Cited by 26 publications

(10 citation statements)

References 16 publications

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“…On the other hand, its low-molecular-mass homologue, acarbose, was a potent selective inhibitor of the Candida glucoamylase. A pronounced inhibitory effect of acarbose has also been reported for a few other glucoamylases [3,27,88,901. According to Clarke and Svensson [91], two specific tryptophanyl residues were involved in the strong binding of acarbose to the glucoamylase of A. niger resulting in a typical ultraviolet difference spectrum between 260 nm and 320 nm.…”

Section: Inhihitionmentioning

confidence: 95%

“…Indeed, neutral carbohydrate (as mannose) was present in both the C. antarctica a-amylase (2.4%) and glucoamylase (7.4%0), which was confirmed by their staining with the periodic acid/Schiff s base reagent after electrophoresis. The glycoprotein nature of extracellular yeast amylases has been reported by several authors [3,11,27,32,33,[43][44][45]. A 300-kDa glucoamylase from S. diastaticus with an extremely high carbohydrate content (8O0/,) was recently characterized by Modena et al…”

Section: Physicochemical Characteristicsmentioning

confidence: 98%

“…3 C). The optimum for glucoamylase is within the usual range for yeast glucoamylases (SO -60°C), but the value for a-amylase is considerably higher than for most other yeasts (not higher than 50°C) [3,4,27]. However, an a-amylase with optimum at 70°C is secreted by L. starkeyi [60].…”

Section: Physicochemical Characteristicsmentioning

confidence: 99%

“…As specific extracellular debranching enzymes, such as pullulanase or isoamylase, are usually not produced by moulds or yeasts [2], the glucoamylase debranching activity is essential to enable extensive starch hydrolysis by these microorganisms. Indeed, the most active amylolytic yeasts display such activity [3,11,27,44,45,56,651. However, the debranching activity of S. diustaticus glucoamylases is extremely low, if detectable [33,35,461.…”

Section: Substrate Specificitymentioning

confidence: 99%

“…Glucoamylase was also more acidstable but, unlike a-amylase, its stability rapidly decreased at alkaline pH ( Fig.2A). Mould and other yeast amylases usually also have pH optima between 4 and 6 [3,4,27,31,.…”

Section: Physicochemical Characteristicsmentioning

confidence: 99%

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Purification and characterization of extracellular α‐amylase and glucoamylase from the yeast Candida antarctica CBS 6678

Mot

Verachtert

1987

European Journal of Biochemistry

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An a-amylase and a glucoamylase were purified to homogeneity from the culture fluid of /3-cyclodextringrown Candida antarctica CBS 6678 by protamine sulfate treatment, ammonium sulfate precipitation, gel filtration (Sephadex G-75 sf, Ultrogel AcA 54), DEAE-Sephacel chromatography, hydroxyapatite chromatography and affinity chomatography on acarbose -AH-Sepharose 4B.Both enzymes were monomeric glycoproteins with fairly different amino acid compositions. Their apparent relative molecular mass, sedimentation coefficient (s&, , ), isoelectric point, absorption coefficient (280 nm), pH and temperature optima were estimated as 48500, 4.7 S, 10.1, 1.74 cm2 mg-', 4.2 and 57"C, respectively, for glucoamylase and as 50000, 4.9 S, 10.3, 1.53 cm2 mg-l, 4.2 and 62"C, respectively, for a-amylase.Kinetic analyses indicated that both enzymes preferentially hydrolyzed high-molecular-mass substrates, including some raw starches. a-Amylase was active on cyclodextrins, whereas debranching activity was demonstrated for glucoamylase. Trestatins were potent inhibitors of both a-amylase (Ki < 1 pM) and glucoamylase (Ki < 0

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Section: Inhihitionmentioning

confidence: 95%

Section: Physicochemical Characteristicsmentioning

confidence: 98%

Section: Physicochemical Characteristicsmentioning

confidence: 99%

Section: Substrate Specificitymentioning

confidence: 99%

Section: Physicochemical Characteristicsmentioning

confidence: 99%

See 3 more Smart Citations