Secretion of α-amylase and multiple forms of glucoamylase by the yeast <i>Trichosporon pullulans</i>

Mot, René De; Verachtert, Hubert

doi:10.1139/m86-009

Cited by 34 publications

(6 citation statements)

References 19 publications

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“…The optimal pH for the enzyme activity (5.5) was similar to that found for α‐amylases from a variety of yeast strains [5,7]. The optimal pH for yeast α‐amylase activity is usually in the range of 4.0 and 6.0 [5–10,16]. The optimum temperature for the enzyme activity was found to be 50°C at pH 5.5 (Table 2), and it is in agreement with the data for the α‐amylases from for S. alluvius ATCC 26074, S. alluvius UCD 54‐83, L. kononenkoae , and C. antarctica CBS 6678 [6,7,9].…”

Section: Resultssupporting

confidence: 84%

“…These results suggest that the enzyme does not require calcium for its activity and/or stability. The enzyme activity was greatly inhibited in the presence of Hg 2+ , Fe 2+ and Cu 2+ , these ions have also been reported to inhibit other α‐amylases produced by yeasts [5–10,16]. The inhibition by mercuric ions may indicate the importance of indole amino acid residues in enzyme function as has been demonstrated for other microbial α‐amylases [1].…”

Section: Resultsmentioning

confidence: 64%

“…These results suggested that the amylase purified from C. flavus was a glycoprotein and the ratio of sugar was approximately 50% in weight. The existence of glycoprotein with α‐amylase activity has been well documented for several yeasts, including those produced by T. pullulans , L. kononenkoae , C. antarctica CBS 6678 and S. alluvius ATCC 26074 [5,6,8,9]. It is known that in certain glycoproteins produced by filamentous fungi and yeasts the carbohydrate moiety is indispensable for secretion or increasing stability against thermal and chemical denaturation [17,18].…”

Section: Resultsmentioning

confidence: 99%

“…4). α‐Amylases attack the α‐(1–4) glucosidic linkages of starch in a random endoamylolytic fashion [1], and has often been reported in many fungi, including some produced by yeasts [1,5–10,16].…”

Section: Resultsmentioning

confidence: 99%

“…Although there have been many papers dealing with α‐amylase‐producing yeasts such as Lipomyces kononenkoae [5], Schwanniomyces alluvius [6,7], Trichosporon pullulans [8] and Candida antarctica [9], only limited research has been directed towards the amylases produced by the Cryptococcus genus [10]. In the present report we investigate the amylolytic activities of C. flavus and describe some of the biochemical properties of the α‐amylase purified from the culture broth.…”

Section: Introductionmentioning

confidence: 98%

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Biochemical characterization of Î±-amylase from the yeastCryptococcus flavus

Wanderley

Torres

Moraes

et al. 2004

FEMS Microbiology Letters

110

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During our screening of amylolytic microorganisms from Brazilian fruits, we isolated a yeast strain classified as Cryptococcus flavus. When grown on starch-containing medium this strain exhibited the highest amylase production after 24 h of cultivation. The extracellular amylase from C. flavus was purified from the culture broth by a single step using chromatography on a Sephacryl S-100 column. The enzyme was purified 16.14-fold with a yield of 50.21% of the total activity. The purified enzyme was a glycoprotein with an apparent molecular mass of 75 and 84.5 kDa as estimated by sodium dodecyl sulfate^polyacrylamide gel electrophoresis and gel filtration, respectively. The enzyme lost approximately 50% of the molecular mass after treatment with glycosidases. The major end products of starch, amylose, amylopectin, pullulan and glycogen were maltose and maltotriose. The K m value for the pure enzyme was 0.056 mg ml 31 with soluble starch as the substrate. Enzyme activity was optimal at pH 5.5 and 50 ‡C. The enzyme retained 90% of the activity after incubation at 50 ‡C for 60 min and was inhibited by Cu 2þ , Fe 2þ and Hg 2þ .

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Section: Resultssupporting

confidence: 84%

Section: Resultsmentioning

confidence: 64%