Production and characterization of β-1,4-glucosidase from a strain of Penicillium pinophilum

Joo, Ah-Reum; Jeya, Marimuthu; Lee, Kyoung-Mi; Lee, Kyoung-Min; Moon, Hee-Jung; Kim, Yeong-Suk; Lee, Jung-Kul

doi:10.1016/j.procbio.2010.02.005

Cited by 50 publications

(23 citation statements)

References 43 publications

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“…Demirkan (2011) has reported that tryptone was found to be better for amylase production by the parental and mutant strains in comparison to other nitrogen sources. Daroit et al (2007); Barbosa et al (2010) and Joo et al (2010) have indicated that the production level of β-glucosidase was decreased when potassium nitrate was used as the nitrogen source. Aiyer (2004) and Felix et al (1996) have reported that (NH 4 ) 2 HPO 4 was found to be the best nitrogen source for amylase production.…”

Section: Resultsmentioning

confidence: 99%

Development of a β-glucosidase hyperproducing mutant by combined chemical and UV mutagenesis

2012

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The extracellular β-glucosidase from microorganisms is generally produced in low levels. Therefore, in this study, a β-glucosidase hyperproducing mutant was developed by multiple exposures of ethyl methyl sulfonate (EMS) and ultraviolet (UV) radiation (both individually and jointly) to Bacillus subtilis strain (PS). The developed mutants were screened, selected and characterized. The mutant, PS-UM1 developed after UV exposure alone, indicated a small increase in β-glucosidase production (718 U/l) in comparison to the wild-type strain, PS (675 U/l). The mutant, PS-CM5 developed after EMS exposure alone, displayed a slightly better production (762 U/l) than both the above strains. However, after exposure of the wild-type strain to both UV and EMS mutagens jointly, a better mutant (PS-CM5-UM3) was developed with 1.2-fold increase in production (806 U/l). Further, optimization of culture conditions by classical “one-variable-at-a-time” approach was done to determine the optimum, pH, temperature and nitrogen sources. The selected mutant (PS-CM5-UM3) produced up to 1,797 U/l enzyme and was found to be stable for ten generations. The β-glucosidase from the selected mutant (PS-CM5-UM3) was concentrated and purified using ammonium sulfate, dialysis and size-exclusion chromatography. The enzyme displayed maximal activity at 60 °C and it was found to be fairly stable at temperatures up to 70 °C for 30 min. Its molecular weight was determined to be around 60 kDa by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE).

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Section: Resultsmentioning

confidence: 99%

Development of a β-glucosidase hyperproducing mutant by combined chemical and UV mutagenesis

2012

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“…6a, b). Based on these results, β-glucosidase from P. janthinellum can be classified as broad substrate specific, active against both aryl β-glucosidase and cellobiose [27]. The purified β-glucosidase exhibited K m and V max of 3.3 mM and 444.4 μmol min −1 mg protein −1 against pNPG, respectively.…”

Section: Substrate Specificity and Enzyme Kineticsmentioning

confidence: 91%

Penicillium janthinellum: a Source of Efficient and High Levels of β-Glucosidase

Kaur

Chadha

2014

Appl Biochem Biotechnol

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Penicillium janthinellum strain isolated from leaf litters of oak trees from montane alpine forests of Shivalik hills (India) produced high levels of β-glucosidase both during solid-state fermentation (796 units/gds) and shake flask cultures (65.3 units/ml). The peptide mass fingerprinting of the secretome showed a variety of glycosyl hydrolases. β-Glucosidase was purified and characterized to be a GH3 family member that had a molecular weight (M r) of 101 kDa and pI of 4.5. β-Glucosidase was optimally active at 60 °C at pH 5.0 but showed appreciable activity and thermostability under alkaline conditions (pH 9.0) also. β-Glucosidase activity was positively modulated in the presence of Mn(2+) ions. The enzyme preferentially catalyzed the hydrolysis of p-nitrophenol-β-D-glucopyranoside (pNPG) but also recognized cellobiose as substrates. K m and V max for the hydrolysis of pNPG by β-glucosidase were calculated as 3.3 mM and 444 μmol min(-1) mg protein(-1). Purified β-glucosidase showed transglycosylation activity in the presence of methanol as an acceptor molecule.

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“…In addition, some microorganisms, such as bacteria, molds and yeasts can produce this enzyme (Riou et al 1998;Spagna et al 2002a;Wallecha and Mishra 2003;Rodriguez et al 2004Rodriguez et al , 2007Barbagallo et al 2004;Arevalo Villena et al 2005;Hernandez-Orte et al 2009;Joo et al 2010). However, the efficiency of hydrolysis of monoterpenyl b-D-glucosides by various plants and microorganisms was found to be dependent on the structure of the aglycon and the origin of the enzyme (Günata et al 1990).…”

Section: Introductionmentioning

confidence: 99%

Characterization of β-glucosidases from Hanseniaspora sp. and Pichia anomala with potentially aroma-enhancing capabilities in juice and wine

Swangkeaw

Vichitphan

Butzke

et al. 2010

World J Microbiol Biotechnol

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The properties of intracellular b-glucosidases produced from two yeast isolates identified as Hanseniaspora sp. BC9 and Pichia anomala MDD24 were characterized. b-Glucosidase from Hanseniaspora sp. BC9 was not inhibited by both 20% w/v fructose and 20% w/v sucrose and was slightly inhibited by glucose ([ 40% relative b-glucosidase activity with 10% w/v glucose). b-Glucosidase from P. anomala MDD24 was inhibited by glucose, fructose and sucrose. In the presence of 4-12% v/v ethanol, b-glucosidase from P. anomala MDD24 was stimulated in range 110-130% relative activity whereas b-glucosidase from Hanseniaspora sp. BC9 was substantially inhibited in the presence of ethanol. Finally, juice and wine of the Muscat-type grape variety, Traminette, were selected to determine sugar-bound volatile aroma release, particularly terpenes, by the activity of those b-glucosidases. The results showed that high concentration of free aroma compounds were detected from Traminette juice treated with b-glucosidase from Hanseniaspora sp. BC9and Traminette wine treated with b-glucosidase from P. anomala MDD24. The preliminary results with proposed an application of these enzymes in commercial wine production lead to more efficient of b-glucosidase from Hanseniaspora sp. BC9 in releasing desirable aromas during an early stage of alcoholic fermentation while b-glucosidase from P. anomala MDD24 is suitable at the final stage of alcoholic fermentation.

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Production and characterization of β-1,4-glucosidase from a strain of Penicillium pinophilum

Cited by 50 publications

References 43 publications

Development of a β-glucosidase hyperproducing mutant by combined chemical and UV mutagenesis

Development of a β-glucosidase hyperproducing mutant by combined chemical and UV mutagenesis

Penicillium janthinellum: a Source of Efficient and High Levels of β-Glucosidase

Characterization of β-glucosidases from Hanseniaspora sp. and Pichia anomala with potentially aroma-enhancing capabilities in juice and wine

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