The purification and characterization of a dextranase from <i>Lipomyces starkeyi</i>

Koenig, David W.; Day, Donal F.

doi:10.1111/j.1432-1033.1989.tb14908.x

Cited by 27 publications

(25 citation statements)

References 12 publications

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“…Enzymes that specifically hydrolyse dextran are therefore employed to overcome some of the problems associated with the removal of dextran 6 . Dextranase (EC 3.2.1.11, α-1,6 glucan 6-glucanohydrolase) is an inducible enzyme that specifically hydrolyses the α-1,6-glucosidic linkages within the dextran molecule to release smaller oligosaccharides 7 . As this process reversibly reduces the stickiness caused by dextran, it has been suggested as a mean to solve the problem of microbe-produced dextran in the cane sugar industry 8 .…”

Section: Introductionmentioning

confidence: 99%

Cloning, characterization, and heterologous expression of a dextranase gene from Penicillium pinophilum SMCU3-14

Rerngsamran¹,

Temjitpukdee²,

Assavasirijinda³

et al. 2014

ScienceAsia

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A DNA fragment encoding dextranase was cloned from Penicillium pinophilum SMCU3-14 using the genome walking approach. Sequence analysis of the gene (SMCU-DEX) revealed a putative CAAT box at −165 (CCAAT), a putative TATA box at −93 (TATAA) in the 5 -noncoding region, and a polyadenylation signal (AATAAG) in the 3 -noncoding region. A cDNA sequence analysis revealed no evidence of introns. The deduced open reading frame is 1824 bp in length and encodes a predicted protein of 608 amino acids (molecular weight (MW) of ∼66 kDa), with a putative N-terminal 20-amino acid signal peptide, giving a predicted mature protein of 588 amino acids (MW of ∼64 kDa) that belongs to glycosyl hydrolase family 49, as with other fungal dextranases. This is the first report of a dextranase gene sequence from P. pinophilum. The cDNA was cloned and expressed in Escherichia coli, and the transformants showed dextranase activity on a dextran-containing agar medium. Crude extracts from the transformants analysed by sodium dodecyl sulphate polyacrylamide gel electrophoresis containing blue dextran revealed a distinct specific band of dextranase activity at an MW of approximately 66 kDa. This recombinant dextranase is likely to have valuable and cost-effective applications in medicine and industry.

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Section: Introductionmentioning

confidence: 99%

Cloning, characterization, and heterologous expression of a dextranase gene from Penicillium pinophilum SMCU3-14

Rerngsamran¹,

Temjitpukdee²,

Assavasirijinda³

et al. 2014

ScienceAsia

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“…Interestingly, the optimum pH of dextranase fermentation is similar to that of recombinant dextranase that is expressed in Pichia pastoris [11,12]. And also, the growth rate and dextranase production of L. starkeyi KCTC 17343 varied depending on the initial culture temperature ( ported in previous study [10,11]. As mentioned above, the optimum pH of dextranase fermentation is similar to that of enzyme activity.…”

Section: Resultsmentioning

confidence: 74%

“…At previous research, Lipomyces strains have been reported to have optimal growth at around 5.0 [11]. Interestingly, the optimum pH of dextranase fermentation is similar to that of recombinant dextranase that is expressed in Pichia pastoris [11,12]. And also, the growth rate and dextranase production of L. starkeyi KCTC 17343 varied depending on the initial culture temperature ( ported in previous study [10,11].…”

Section: Resultsmentioning

confidence: 90%

“…Dextranase yields and specific productions at pH 3 were over 3 times lower than those at pH 4 to 5. At previous research, Lipomyces strains have been reported to have optimal growth at around 5.0 [11]. Interestingly, the optimum pH of dextranase fermentation is similar to that of recombinant dextranase that is expressed in Pichia pastoris [11,12].…”

Section: Resultsmentioning

confidence: 99%

“…Lipomyces starkeyi, ascosporogeneous yeast, produces dextranase which selectively hydrolyzes the α-(1 6) glycosidic → bond present in dextrans to produce oligodextrans [10,11].…”

Section: Introductionmentioning

confidence: 99%

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Optimization of an Extracellular Dextranase Production from Lipomyces starkeyi KCTC 17343 and Analysis of Its Dextran Hydrolysates

Chang¹,

Yeom²,

Jung³

et al. 2009

Journal of Life Science

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W e optimized dextranase culture conditions by batch fermentation using Lipomyces starkeyi KCTC 17343. Furthermore, dextranase was purified by an ultra-membrane, and then dextran hydrolyzates were characterized. Cell growth and dextranase production varied depending on the initial culture pH and temperature. The conditions of optimal dextranase production were met in a pH range of 4-5 and temperature between 25-30 o C. At optimal fermentation conditions, total enzyme activity and specific enzyme activity were about 4.85 IU/ml and 0.79 IU/g cells, respectively. The specific growth rate was examined to be 0.076 hr-1 . The production of dextranase in culture broth was very stably maintained after mid-log phase of growth. The enzyme hydrolyzed dextran into DP (degree of polymerization) 2 to 8 oligodextran series. Analysis of the composition of hydrolysates suggested that the enzyme produced is an endo-dextranase.

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Cloning and characterization of a dextranase gene from Lipomyces starkeyi and its expression in Saccharomyces cerevisiae

Kang

Kim²,

Park

et al. 2005

Yeast

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The open reading frame encodes a 608 amino acid polypeptide (LSD1) with a 67.6 kDa predicted molecular mass. There was a 77% deduced amino acid sequence identity between the LSD1 dextranase and the dextranase from Penicillium minioluteum. The primary structure of LSD1 dextranase exhibits distant similarity with the enzymes of the glycosyl hydrolase family 49 that comprises Penicillium dextranase. The optimum pH of LSD1 was 6.0 and the optimum temperature was 37 • C. LSD1 dextranase activity was substantially abolished by exposure to 1 mM Hg 2+ , Ag 3+ and Mn 2+ . LSD1 exhibited high hydrolysing activity towards dextran (100%), soluble starch (22%) and mutan (8%).

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The purification and characterization of a dextranase from Lipomyces starkeyi

Cited by 27 publications

References 12 publications

Cloning, characterization, and heterologous expression of a dextranase gene from Penicillium pinophilum SMCU3-14

Cloning, characterization, and heterologous expression of a dextranase gene from Penicillium pinophilum SMCU3-14

Optimization of an Extracellular Dextranase Production from Lipomyces starkeyi KCTC 17343 and Analysis of Its Dextran Hydrolysates

Cloning and characterization of a dextranase gene from Lipomyces starkeyi and its expression in Saccharomyces cerevisiae

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