A family 11 xylanase from Penicillium funiculosum is strongly inhibited by three wheat xylanase inhibitors

Furniss, Caroline S.M.; Belshaw, Nigel J.; Alcocer, Marcos; Williamson, Gary; Elliott, Giles O.; Gebruers, Kurt; Haigh, Nigel P; Fish, Neville M.; Kroon, Paul A.

doi:10.1016/s0167-4838(02)00366-7

Cited by 40 publications

(27 citation statements)

References 23 publications

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“…The specific activity of the purified XYN11F63 was 7,988 Umg −1 , significantly higher than that of most Penicillium xylanases, such as XYNA from Penicillium sp. strain 40 (1,250 Umg −1 ) [9], XynA from P. citrinum (2,100 Umg −1 ) [7], and XYNC from P. funiculosum (2,830 Umg −1 ) [8]. The high level of expression would be further improved by optimizing the fermentation parameters.…”

Section: Discussionmentioning

confidence: 99%

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Gene Cloning, Overexpression, and Characterization of a Xylanase from Penicillium sp. CGMCC 1669

Liu

Shi

Chen

et al. 2009

Appl Biochem Biotechnol

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A xylanase-encoding gene, xyn11F63, was isolated from Penicillium sp. F63 CGMCC1669 using degenerated polymerase chain reaction (PCR) and thermal asymmetric interlaced (TAIL)-PCR techniques. The full-length chromosomal gene consists of 724 bp, including a 73-bp intron, and encodes a 217 amino acid polypeptide. The deduced amino acid sequence of xyn11F63 shows the highest identity of 70% to the xylanase from Penicillium sp. strain 40, which belongs to glycosyl hydrolases family 11. The gene was overexpressed in Pichia pastoris, and its activity in the culture medium reached 516 U ml(-1). After purification to electrophoretic homogeneity, the enzyme showed maximal activity at pH 4.5 and 40 degrees C, was stable at acidic buffers of pH 4.5-9.0, and was resistant to proteases (proteinase K, trypsin, subtilisin A, and alpha-chymotrypsin). The specific activity, K (m), and V (max) for oat spelt xylan substrate was 7,988 U mg(-1), 22.2 mg ml(-1), and 15,105.7 micromol min(-1) mg(-1), respectively. These properties make XYN11F63 a potential economical candidate for use in feed and food industrial applications.

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Section: Discussionmentioning

confidence: 99%

“…To date, several xylanase genes from Penicillium spp. have been cloned and expressed, such as Penicillium citrium XynA [7], Penicillium funiculosum XYNC [8], Penicillium sp. strain 40 XynA [9], Penicillium purpurogenum XynB [10], and Penicillium janthinellum NCIM [11].…”

Section: Introductionmentioning

confidence: 99%

Gene Cloning, Overexpression, and Characterization of a Xylanase from Penicillium sp. CGMCC 1669

Liu

Shi

Chen

et al. 2009

Appl Biochem Biotechnol

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“…soisson) as described previously (9,10). A. nidulans xylanase XLNC and P. funiculosum xylanase XYNC were overexpressed (14, 15) and purified as described earlier (10,11).…”

Section: Methodsmentioning

confidence: 99%

The Dual Nature of the Wheat Xylanase Protein Inhibitor XIP-I

Payan

Leone

Porciero

et al. 2004

Journal of Biological Chemistry

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118

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The xylanase inhibitor protein I (XIP-I) from wheatTriticum aestivum is the prototype of a novel class of cereal protein inhibitors that inhibit fungal xylanases belonging to glycoside hydrolase families 10 (GH10) and 11 (GH11). The crystal structures of XIP-I in complex with Aspergillus nidulans (GH10) and Penicillium funiculosum (GH11) xylanases have been solved at 1.7 and 2.5 Å resolution, respectively. The inhibition strategy is novel because XIP-I possesses two independent enzyme-binding sites, allowing binding to two glycoside hydrolases that display a different fold. Inhibition of the GH11 xylanase is mediated by the insertion of an XIP-I ⌸-shaped loop (L␣ 4 ␤ 5 ) into the enzyme active site, whereas residues in the helix ␣7 of XIP-I, pointing into the four central active site subsites, are mainly responsible for the reversible inactivation of GH10 xylanases. The XIP-I strategy for inhibition of xylanases involves substrate-mimetic contacts and interactions occluding the active site. The structural determinants of XIP-I specificity demonstrate that the inhibitor is able to interact with GH10 and GH11 xylanases of both fungal and bacterial origin. The biological role of the xylanase inhibitors is discussed in light of the present structural data.

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“…22) On the other hand, the K mapp value for endo-1,4--D-xylanase (9.2 mg/ml) is close to those reported for two isoenzymes of endo-1,4--Dxylanase from P. capsulatum using wheat straw xylan as a substrate (7.0 and 9.8 mg/ml), but lower than those obtained using oat spelt xylan as substrate (46.0 and 33.7 mg/l). 29) However, lower Km values of 3.4, 4.1 and 4.7 mg/ml have been obtained for other endo-1,4--D-xylanases from P. chrysogenum, 17) recombinant P. funiculosum 37) and P. canescens, 34) respectively. The apparent K mapp value (9.2 mg/ml) of endo-1,3-1,4--D- glucanase for -glucan was higher than that reported for the same enzyme from Orpinomyces sp.…”

Section: )mentioning

confidence: 98%

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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A family 11 xylanase from Penicillium funiculosum is strongly inhibited by three wheat xylanase inhibitors

Cited by 40 publications

References 23 publications

Gene Cloning, Overexpression, and Characterization of a Xylanase from Penicillium sp. CGMCC 1669

Gene Cloning, Overexpression, and Characterization of a Xylanase from Penicillium sp. CGMCC 1669

The Dual Nature of the Wheat Xylanase Protein Inhibitor XIP-I

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

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