Author
G. Rónaszéki
Bio: G. Rónaszéki is an academic researcher. The author has contributed to research in topics: Kluyveromyces. The author has an hindex of 2, co-authored 3 publications receiving 13 citations.
Topics: Kluyveromyces
Papers
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TL;DR: Eighteen strains, of thermophilic fungus Thermomyces lanuginosus were screened for amylolytic activities and three strains were selected for detailed studies on their production of glucoamylase and α-amyl enzyme.
Abstract: Eighteen strains, of thermophilic fungus Thermomyces lanuginosus were screened for amylolytic activities. All of them produced extracellular amylolytic enzymes. Three strains were selected for detailed studies on their production of glucoamylase and α-amylase. The optimum conditions for the assays of amylolytic activities were selected. The optimum parameters were found to be the following: 70 °C and pH 4.6 for glucoamylase and 70 °C and pH 5.0 for α-amylase.
6 citations
Journal Article•
TL;DR: In this article, the optimum conditions for the assays of amylolytic activities of thermophilic fungus Thermomyces lanuginosus were selected and the optimum parameters were found to be the following: 70 °C and pH 4.6 for glucoamylase and pH 5.0 for α amylase.
Abstract: Eighteen strains, of thermophilic fungus Thermomyces lanuginosus were screened for amylolytic activities. All of them produced extracellular amylolytic enzymes. Three strains were selected for detailed studies on their production of glucoamylase and α-amylase. The optimum conditions for the assays of amylolytic activities were selected. The optimum parameters were found to be the following: 70 °C and pH 4.6 for glucoamylase and 70 °C and pH 5.0 for α-amylase.
5 citations
2 citations
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TL;DR: Amylolytic enzymes from Thermomyces lanuginosus ATCC 34626 were purified to electrophoretic homogeneity and almost complete homology with the α-amylase from Aspergillus oryzae and Emericella nidulans was observed.
158 citations
TL;DR: Amo acid sequence alignment of N-terminal sequence data allows the α-galactosidase from Thermomyces lanuginosus to be classified in glycosyl hydrolase family 36.
48 citations
TL;DR: A three-stage bioethanol bioprocess was developed, and amylases obtained from Rhizopus microsporus var.
12 citations
Journal Article•
TL;DR: The effects of various carbon and nitrogen sources on inulinase activity were investigated, and the best ones were found to be Jerusalem artichoke extract and peptone at the optimum fraction of 1.8 and 0.6 %, respectively.
Abstract: Summary The production of extracellular inulinase by eighteen Thermomyces lanuginosus strains was screened, and strain IMI 140524 was selected for further studies. The effects of various carbon and nitrogen sources on inulinase activity were investigated, and the best ones were found to be Jerusalem artichoke extract and peptone at the optimum fraction of 1.8 and 0.6 %, respectively. Effects of medium composition and fermentation conditions were also determined for the production of extracellular inulinase. The addition of 1 % (by volume) Tween 80 into fermentation medium enhanced the secretion of extracellular inulinase. In bench-scale fermentor, the age and amount of inoculum were also optimized and they were determined to be 40-hour-old culture and 5.0 % (by volume), respectively. The initial pH of the medium was adjusted to 6.5 and no further pH control was needed. Optimal aeration and agitation were 0.75 L/min and 150 rpm, respectively.
10 citations
TL;DR: Thermophilic Thermomyces lanuginosus strain TO3 was isolated from compost pile samples and was used for its ability to produce considerable glucoamylase activity when growing in liquid medium at 45oC with starch as the sole carbon source.
Abstract: Thermophilic Thermomyces lanuginosus strain TO3 was isolated from compost pile samples and was used for its ability to produce considerable glucoamylase activity when growing in liquid medium at 45oC with starch as the sole carbon source. Enzyme productivity was high in submerged fermentation (SmF) with maximum activity of 13 U/mL after 168 h of fermentation. Higher quantities of glucose were released when the substrate for enzyme was soluble starch than maltose or maltooligosaccharides were used. The distribution of glucoamylase between the extracellular and cell-associated fractions varied according to fermentation time. Glucoamylase produced from T. lanuginosus TO3 had optimum activity at 65 oC and good thermostability in the absence of substrate, with a half-life of 6 h at 60 oC. The enzyme was stable over a wide pH range (4.0-10.0).
3 citations