Purification and some properties of an .alpha.-L-arabinofuranosidase from Aspergillus niger. Action on grape monoterpenyl arabinofuranosylglucosides

Günata, Ziya; Brillouet, Jean‐Marc; Voirin, Stéphane G.; Baumes, Raymond; Cordonnier, Robert

doi:10.1021/jf00093a040

Cited by 56 publications

(19 citation statements)

References 13 publications

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“…Plant and microbial β-glucosidases hydrolyse β-glucosides of primary and secondary alcohols, while tertiary alcohol β-glycosides are preferred by fungal-derived enzymes. [47][48][49] In contrast, exoglycosidases and diglycosidases from grapes have much broader substrate specificity.…”

Section: Discussionmentioning

confidence: 99%

Flavour enhancement through the enzymatic hydrolysis of glycosidic aroma precursors in juices and wine beverages: a review

Pogorzelski

Wilkowska

2007

Flavour & Fragrance J

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Section: Discussionmentioning

confidence: 99%

Flavour enhancement through the enzymatic hydrolysis of glycosidic aroma precursors in juices and wine beverages: a review

Pogorzelski

Wilkowska

2007

Flavour & Fragrance J

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“…ABFs have been used in food production for antistaling and to improve quality of bread texture (Denli and Ercan, 2001;Jankiewicz and Michniewicz, 1987), to improve flavor and aromatic fragrance of wine (Gunata et al, 1990;Michlmayr et al, 2013;Spagna et al, 1998;Spagna, et al, 1998), and to increase solubility of precipitates and prevent haze formation in fruit juice (Whitaker, 1984). Although, no studies that apply GH62 ABFs in food and beverage production have been published it is not unthinkable that applications of GH62s can further improve the processing of cell wall derived hemicelluloses and hence the quality of the above-mentioned as well as other plantbased products.…”

Section: Food and Feedmentioning

confidence: 99%

GH62 arabinofuranosidases: Structure, function and applications

Wilkens

Andersen

Dumon

et al. 2017

Biotechnology Advances

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Motivated by industrial demands and ongoing scientific discoveries continuous efforts are made to identify and create improved biocatalysts dedicated to plant biomass conversion. --1,3 arabinofuranosyl specific -L-arabinofuranosidases (EC 3.2.1.55) are debranching enzymes catalyzing hydrolytic release -L-arabinofuranosyl residues, which decorate xylan or arabinan backbones in lignocellulosic and pectin constituents of plant cell walls. The CAZy database classifies -L-arabinofuranosidases in Glycoside Hydrolase (GH) families GH2, GH3, GH43, GH51, GH54 and GH62. Only GH62 contains exclusively -L-arabinofuranosidases and these are of fungal and bacterial origin. Twenty-two GH62 enzymes out of 223 entries in the CAZy database have been characterized and very recently new knowledge was acquired with regard to crystal structures, substrate specificities, and phylogenetics, which overall provides novel insights into structure/function relationships of GH62. Overall GH62 -L-arabinofuranosidases are believed to play important roles in nature by acting in synergy with several cell wall degrading enzymes and members of GH62 represent promising candidates for biotechnological improvements of biofuel production and in various biorefinery applications.3

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“…In recent years, interest in xylan degrading enzymes have been increased due to their applications in various agro-industrial processes, such as hemicellulosic biomass conversion to fuels and chemicals, paper pulp delignification, animal feedstock digestibility enhancement, xylo-oligosaccharide production, juices clarification, beer consistency improvement, fruit juices and wines aroma enhancement and pentose containing disaccharides synthesis (Rahman et al 2001, Makkonen et al 2005, Wong et al 1988, Gunata et al 1990, Spagna et al 1998, Rmond et al 2004). Thus, extensive l Institute of Transplantation and Gene Sciences, Baskent Univ.…”

Section: Introductionmentioning

confidence: 99%

Isolation of Endopyhtic and Xylanolytic Bacillus pumilus Strains from Zea mays

YAŞINOK¹,

Ayşegül;ŞAHİN²,

İffet;HABERAL³

et al. 2008

Tarım Bilimleri Dergisi

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In this study, two endophytic xylanolytic bacteria, named M1 and M2, were isolated from surface sterilized Zea mays stern and leaf, respectively. Isolates were identified as Bacillus pumilus. Microorganisims showed different morphology on agar plates. Xylanase production level and profile varied between isolates, as well. Maximum xylanase production level of 188.0 ± 20.0 and 5.6 ± 1.1 U/ml were achieved by Bacillus pumilus M1 and Bacillus pumilus M2 in a liquid medium containing 3% corn cobs as a sole carbon source and inducer, respectively. Isolates produced very low level of cellulase in crude enzyme extract. B. pumilus M1 xylanase was partially characterized. Enzyme had a maximum activity at pH 8.0 and 65°C, seemed proper for pulp and paper industry, and required further characterization. In conclusion, this study indicated that inside part of Zea mays is a novel and good source for isolating xylanase producers. After detailed characterization, such enzymes could be used in various applications in paper and pulp, textile, food and feed industries.Key Words: Bacillus pumilus, endopyhte, plant, xylan, xylanase producers. Zea mays'dan Endofitik ve Ksilanolitik Bacillus pumilus Suş ları n ı n İzolasyonuÖz: Bu çal ışmada, yüzey sterilizasyonu yap ı lm ış Zea mays gövde ve yapraklar ı ndan, s ı ras ı ile M1 ve M2 olarak isimlendirilen iki tane endofitik ksilanolitik bakteri izole edilmi ştir. Izolatlar Bacillus pumilus olarak tan ı mlanm ıştı r. Mikroorganizmalar agar üzerinde farkl ı morfoloji sergilemi ştir. Izolatlar aras ı nda, ksilanaz üretim seviyesi ve profilinde de farkl ı l ı klar bulunmaktad ı r. İçinde %3 m ı s ı r koçan ı n ı tek karbon kaynağı olarak bulunduran s ı v ı besi yerinde, Bacillus pumilus Mi ve Bacillus pumilus M2 s ı ras ı ile maksimum ksilanaz aktivitesi olan 188.0 ± 20.0 ve 5.6 t 1.1 U/mi değ erlerine ula şabilmi ştir. İzolatlar, kaba fermentasyon özütünde çok dü ş ük miktarda selülaz üretmi ştir. B. pumilus M1 ksilanaz ı k ı smi karakterize edilmi ştir. Enzim pH 8.0 ve 65°C'de maksimum aktivite götermi ş , ka ğı t beyazlatma endüstrisine uygun görülmü ş ve ileri derecede karakterizasyona ihtiyaç duymu ştur. Sonuç olarak, bu çal ış ma Zea mays' ı n iç k ı sm ı n ı n, ksilanaz üreticilerinin izolasyonu için yeni ve iyi bir kaynak oldu ğ unu göstermi ştir. Detayl ı tan ı mlama ard ı ndan bu enzimler, ka ğı t, tekstil, g ı da ve yem endüstrisinde çe ş itli uygulamalarda değerlendirilebilmesi mümkündür.

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Purification and some properties of an .alpha.-L-arabinofuranosidase from Aspergillus niger. Action on grape monoterpenyl arabinofuranosylglucosides

Cited by 56 publications

References 13 publications

Flavour enhancement through the enzymatic hydrolysis of glycosidic aroma precursors in juices and wine beverages: a review

Flavour enhancement through the enzymatic hydrolysis of glycosidic aroma precursors in juices and wine beverages: a review

GH62 arabinofuranosidases: Structure, function and applications

Isolation of Endopyhtic and Xylanolytic Bacillus pumilus Strains from Zea mays

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