Characterization of xylanase production by a local isolate of Penicillium janthinellum

Milagres, Adriane M. F.; Lacis, Lynda S.; Prade, Rolf A.

doi:10.1016/0141-0229(93)90145-r

Cited by 42 publications

(19 citation statements)

References 27 publications

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“…Although pure commercial xylan is not suitable for large-scale enzyme production, it has been established as the most used carbon source and the best inducer of xylanolytic enzymes (29). As in other fungi, xylose acts as a weak inducer of ␤-xylosidase production in T. amestolkiae (30), but glucose did not induce ␤-xylosidase production (30,31).…”

Section: Discussionmentioning

confidence: 99%

Novel pH-Stable Glycoside Hydrolase Family 3 β-Xylosidase from Talaromyces amestolkiae: an Enzyme Displaying Regioselective Transxylosylation

Nieto-Domínguez

Eugenio

Barriuso

et al. 2015

Appl Environ Microbiol

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This paper reports on a novel ␤-xylosidase from the hemicellulolytic fungus Talaromyces amestolkiae. The expression of this enzyme, called BxTW1, could be induced by beechwood xylan and was purified as a glycoprotein from culture supernatants. We characterized the gene encoding this enzyme as an intronless gene belonging to the glycoside hydrolase gene family 3 (GH3). BxTW1 exhibited transxylosylation activity in a regioselective way. This feature would allow the synthesis of oligosaccharides or other compounds not available from natural sources, such as alkyl glycosides displaying antimicrobial or surfactant properties. Regioselective transxylosylation, an uncommon combination, makes the synthesis reproducible, which is desirable for its potential industrial application. BxTW1 showed high pH stability and Cu 2؉ tolerance. The enzyme displayed a pI of 7.6, a molecular mass around 200 kDa in its active dimeric form, and K m and V max values of 0.17 mM and 52.0 U/mg, respectively, using commercial p-nitrophenyl-␤-D-xylopyranoside as the substrate. The catalytic efficiencies for the hydrolysis of xylooligosaccharides were remarkably high, making it suitable for different applications in food and bioenergy industries. P lant biomass represents the most abundant renewable energy resource available on earth. It is composed mainly of cellulose and hemicellulose, two polysaccharides that constitute the raw material for the so-called second-generation (2G) bioethanol industry. The production of this biofuel has received special attention in recent years because it is based on the use of nonfood sources of cellulosic biomass (1). It has been pointed out that energy crops should be restricted to metal-contaminated soils in order to avoid cultivation competition against the food industry (2, 3).In order to make the production of this biofuel economically viable, many modifications have been introduced into the industrial process in recent years. Among them, the strategy of combining enzymatic hydrolysis of lignocellulose with ethanol fermentation in a single process known as simultaneous saccharification and fermentation (SSF) is a significant step forward, but reduced production costs and improved yields are still necessary (1). Most studies have been using agricultural wastes as raw materials, usually after a physicochemical pretreatment to disrupt the lignocellulose structure to enhance cellulose and hemicellulose accessibility. Nevertheless, the industrial procedure currently used to produce 2G ethanol consists of fermenting glucose, which is enzymatically released from cellulose by using Saccharomyces cerevisiae as a biocatalyst (4). To increase process yields, hemicellulose hydrolysis and pentose fermentation are extremely relevant. Within this heterogeneous group of polysaccharides, xylans are most abundant in hardwoods and grass. They are composed of a backbone of ␤-1,4-linked D-xylopyranosyl units highly substituted with arabinofuranose, glucose, glucuronic or methyl-glucuronic acid, and acetyl side groups. The enz...

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Section: Discussionmentioning

confidence: 99%

Novel pH-Stable Glycoside Hydrolase Family 3 β-Xylosidase from Talaromyces amestolkiae: an Enzyme Displaying Regioselective Transxylosylation

Nieto-Domínguez

Eugenio

Barriuso

et al. 2015

Appl Environ Microbiol

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“…In fact, most endo-1,4--D-xylanases from Penicillium spp. have been reported to have an optimal pH in the range of 4.5 to 6.0, [17][18][19] with the exception of those from Penicillium purpurogenum 19) and Penicillium sp., 20) which were optimally active at pH 7.0 and 2.0, respectively. Moreover, most endo-1,4--D-xylanases from Aspergillus spp.…”

Section: Resultsmentioning

confidence: 99%

“…Similarly, endo-1,4--D-xylanase from P. purpurogenum 19) and the xylanolytic system from P. canescens 34) were mostly active at 50 to 60 C; however, lower optimum temperatures of 30 and 40 C have been reported for -D-xylosidase from P. herquei 23) and for endo-1,4--D-xylanases from P. chrysogenum 17) and Penicillium janthinellum, 18) respectively. Regarding endo-1,3-1,4--D-glucanase, its optimum temperature of 60 to 65 C (Fig.…”

Section: )mentioning

confidence: 96%

Properties of Selected Hemicellulases of a Multi-Enzymatic System fromPenicillium funiculosum

Karboune¹,

L’Hocine²,

Anthoni³

et al. 2009

Bioscience, Biotechnology, and Biochemistry

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A multi-enzymatic system from Penicillium funiculosum displayed -L-arabinofuranosidase, endo-1,4--Dxylanase, -D-xylosidase and endo-1,3-1,4--D-glucanase activities at high levels over a wide acidic pH range of 2.0 to 5.5. Moreover, the pH stability was particularly extended over the wide range of pH of 2.0 to 8.0 with endo-1,3-1,4--D-glucanase and endo-1,4--D-xylanase; however, -L-arabinofuranosidase and -D-xylosidase exhibited higher stability in the pH range of 2.0 to 5.5. The results indicate that the optimal temperature of -L-arabinofuranosidase (65 C) and -D-xylosidase (70 C) as well as their thermal stability were higher than those of endo-1,3-1,4--D-glucanase (60 C) and endo-1,4--D-xylanase (50 C). Although V maxapp of -Dxylosidase and endo-1,4--D-xylanase was higher than that of -L-arabinofuranosidase and endo-1,3-1,4--Dglucanase, respectively, their catalytic efficiency was lower. High levels of ferulolyl esterase, -D-galactosidase, -D-mannosidase and endo-1,4--D-mannanase activities were also detected in the multi-enzymatic system. The overall features of the multi-enzymatic system from P. funiculosum reveal its potential for degrading and modifying plant cell walls from a variety of food and feedstuffs.

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“…Preparation of cellulase-free xylanases can be obtained through several, not ahvays cost effective Inethods, like relTIoval by purification or enzynultic inactivation of cellulases, or by production fro111 InicroorguniSI'IlS that fail to produce detectable aillounts of cellulase activity (Biely e/ al., 1980: (JoInes et al., 1993: Milagres, Lacis andPrade~1993). Selective induclion using chenlically defined inducers (Biely, Vrsanka and Kratky, 1980; J-Inl1ov~i, Petnikova nnd Biely, 1991)~ production by cellulase negative mutants (Eriksson and Goodell, 1974;Mondou et al, 1986) and production by genetically engineered strains can also be used.…”

Section: The Xylanase Marketplacementioning

confidence: 99%

Xylanases: from Biology to BioTechnology

Prade

1996

Biotechnology and Genetic Engineering Reviews

223

137

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SummaryXylan is the tnain carbohydrate found in the henlicellulosic fraction of plant tissues and accounls for one third of all renewable organic carbon aV'lilable on earlh.Xylanase, the rnajor cOluponent of an enzyillatic consortiUl11, acts in nature by depo(ynlerizing xylan JTIolecules into ITIonomeric penlosan units that are used by bacterial and fungal populations as a primary carbon source. Xylanase producers have been isolated fr0I11 all ecological niches where plant Inaterial is deposited, and nlicfoorganislTIs often contain lTIultiple loci encoding overlapping xylanolytic funct ions. The nUlllcrical excess of genes and the extensive sharing of structural features \vilhin f3-glycanase fcunilies suggests that extensive gene dupIicalion and conversion events have occurred during xyJanase evolution. Hydrolysis of J3-glycosidic linkages is sponsored by ,1 general acid catalytic reaclion conlnlon (0 all glycanases, whereas subslrale recognition is specified by subsites that interaCl \vith adjacent glycosyJ units. Under natural conditions xylanases are inducible by the products of their own action and subject to carbon catabolile repression. Bleaching paper pulps with xylanases is the first successful cOlnrnercial application for these cnzYlnes. The recovery of cellulosic textile fibers is the next logical application and bioconvcrsion of biomass into fuels and chemicals~renlains the ultitnate target Recent developInents have sho\vll that Jnetabolic path\\1ays can be transferred frOln one organiSI1110 another and proteins can be Jnodified to gain confonnational stability. suggesting that naturally occurring systclns can be clistOJn engineered to the situation in the fennentation tank. Thus, biotechnologies developed to tranSfOrIll bionulss into Inarketable products that gradually substitute Inaterials derived froIII non-rene\vablc resources are becolning cOJTIluercially worthwhile.

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Characterization of xylanase production by a local isolate of Penicillium janthinellum

Cited by 42 publications

References 27 publications

Novel pH-Stable Glycoside Hydrolase Family 3 β-Xylosidase from Talaromyces amestolkiae: an Enzyme Displaying Regioselective Transxylosylation

Novel pH-Stable Glycoside Hydrolase Family 3 β-Xylosidase from Talaromyces amestolkiae: an Enzyme Displaying Regioselective Transxylosylation

Properties of Selected Hemicellulases of a Multi-Enzymatic System fromPenicillium funiculosum

Xylanases: from Biology to BioTechnology

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