Microbial Xylanases: Sources, Types, and Their Applications

Enshasy, Hesham Ali El; Kandiyil, S K; Malek, Roslinda Abd; Othman, Norasikin

doi:10.1007/978-3-319-43679-1_7

Cited by 13 publications

(10 citation statements)

References 263 publications

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“…Most molds can grow well at a wide pH, for instance, in the pH range of 3.0-8.5, and have an optimum pH of 5.0-7.0. 46,47 Therefore, pH of the substrate is crucial for the growth of fungi because certain enzymes will only break down a substrate according to its activity at a certain pH level.…”

Section: Discussionmentioning

confidence: 99%

Production of Amylase by Aspergillus subflavus and Aspergillus fumigatus from flamevine flower (Pyrostegia venusta (Ker-Gawl.) Miers): A Tropical Plant in Bedugul Botanical Garden, Bali, Indonesia

Sukmawati¹,

Dellanerra²,

Fikriyyah³

et al. 2022

J. Pure Appl. Microbiol.

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Pyrostegia venusta is known as an ornamental plant with its source of antioxidants, cytotoxic, anti-inflammatory, and anti-HIV compounds. Ephypitic molds are potentially co-existed on the surface of this flower since it contains essential nutrients which support their growth. On the other hand, molds produce several enzymes that might involve flower growth. The presence of ephypitic molds on this flower provides information about its ability to produce amylase. This study successfully isolated molds from August flower (P. venusta) originating from Taman Nasional Bedugul, Bali, Indonesia. The study aimed to isolate potential amylase producer strains and optimize the enzyme production using Solid-State Fermentation (SSF) method. Ten mold isolates belonging to Universitas Negeri Jakarta Culture Collection (UNJCC) were selected according to their amylolytic index (IA) values, morphological identification, and colony count number. Selected strains were optimized for its growth to produce amylase using the SSF method under different temperatures (30, 40, 50°C) and pH (6, 7, 8) with a wheat brain fermentation medium. Results showed that UNJCC F100 (6.53 × 108 CFU/ml) and UNJCC F106 (9.83 x 108 CFU/ml) are the two isolates with the highest IA values of 1.34 ± 0.1 and 1.08 ± 0.12 among all isolates. Based on molecular identification using ITS region, UNJCC F100 and UNJCC F106 were identified as A. subflavus (97% homology) and A. fumigatus (99.52% homology), respectively. This study exhibited that both isolate UNJCC F100 and isolate UNJCC F106 have optimal amylase production conditions at 30°C and pH 6. The enzyme produced was 19.99 U/ml at 30°C and 34.33 U/ml at pH 6 for isolate UNJCC F100, and for isolate UNJCC F106 is 28.55±3.80 U/ml. The two isolates are potentially used for amylase production, referring to the specific environmental condition. However, to generate a higher amount with amylase activity, other external variables such as medium used, inoculum concentration, and fermentation method are important to consider further for a larger application.

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Section: Discussionmentioning

confidence: 99%

Production of Amylase by Aspergillus subflavus and Aspergillus fumigatus from flamevine flower (Pyrostegia venusta (Ker-Gawl.) Miers): A Tropical Plant in Bedugul Botanical Garden, Bali, Indonesia

Sukmawati¹,

Dellanerra²,

Fikriyyah³

et al. 2022

J. Pure Appl. Microbiol.

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“…The catalytic mechanisms of GH10 and GH11 xylanases have been thoroughly studied during the past decades [3,4,45,53,54]. The main difference between xylanases from these two families is the lower specificity of most GH10 xylanases towards xylan, combined with their ability to hydrolyze branched xylans, producing oligosaccharides with substituents at the nonreducing end.…”

Section: Discussionmentioning

confidence: 99%

“…Endo-β-xylanases (EC 3.2.1.8) are major hemicellulases involved in the bioconversion of xylans present in plant biomass, are widespread in nature, and are produced by numerous organisms [1]. The majority of xylanases characterized to date are of fungal or bacterial origin, and operate at approximately 40-60°C, and a pH range of 4.0-7.0 [1][2][3][4][5]. In most cases, acid-tolerant endo-1,4-β-xylanases are produced by fungi [4,5].…”

Section: Introductionmentioning

confidence: 99%

“…The majority of xylanases characterized to date are of fungal or bacterial origin, and operate at approximately 40-60°C, and a pH range of 4.0-7.0 [1][2][3][4][5]. In most cases, acid-tolerant endo-1,4-β-xylanases are produced by fungi [4,5]. These are of particular interest for biotechnological applications, such as in the food and feed industry [6,7].…”

Section: Introductionmentioning

confidence: 99%

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A novel acid‐tolerant β‐xylanase fromScytalidium candidum3C for the synthesis ofo‐nitrophenyl xylooligosaccharides

et al. 2020

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Endo‐β‐xylanases are hemicellulases involved in the conversion of xylans in plant biomass. Here, we report a novel acidophilic β‐xylanase (ScXynA) with high transglycosylation abilities that was isolated from the filamentous fungus Scytalidium candidum 3C. ScXynA was identified as a glycoside hydrolase family 10 (GH10) dimeric protein, with a molecular weight of 38 ± 5 kDa per subunit. The enzyme catalyzed the hydrolysis of different xylans under acidic conditions and was stable in the pH range 2.6–4.5. The kinetic parameters of ScXynA were determined in hydrolysis reactions with p‐nitrophenyl‐β‐d‐cellobioside (pNP‐β‐Cel) and p‐nitrophenyl‐β‐d‐xylobioside (pNP‐β‐Xyl2), and kcat/Km was found to be 0.43 ± 0.02 (s·mM)−1 and 57 ± 3 (s·mM)−1, respectively. In the catalysis of the transglycosylation o‐nitrophenyl‐β‐d‐xylobioside (oNP‐β‐Xyl2) acted both as a donor and an acceptor, resulting in the efficient production of o‐nitrophenyl xylooligosaccharides, with a degree of polymerization of 3–10 and o‐nitrophenyl‐β‐d‐xylotetraose (oNP‐β‐Xyl4) as the major product (18.5% yield). The modeled ScXynA structure showed a favorable position for ligand entry and o‐nitrophenyl group accommodation in the relatively open −3 subsite, while the cleavage site was covered with an extended loop. These structural features provide favorable conditions for transglycosylation with oNP‐β‐Xyl2. The acidophilic properties and high transglycosylation activity make ScXynA a suitable choice for various biotechnological applications, including the synthesis of valuable xylooligosaccharides.

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“…The second category reserves the xylanases that are stable and active near the neutral pH range and known as neutrophilic xylanases and the third category consists of the alkaliphilic xylanases which have pH optimum at alkaline range. In most of the cases, the acidophilic xylanases are found to be produced by fungi (Enshasy et al 2016). These acid-stable xylanases have many industrial values (Tenkanen et al 1997;Pokhrel et al 2013;Chen et al 2016).…”

Section: Introductionmentioning

confidence: 99%

Molecular structure and catalytic mechanism of fungal family G acidophilic xylanases

Dey

Roy

2018

3 Biotech

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Industrial applications of xylanases have made this enzyme an important subject of applied research work. Function of this particular enzyme is to degrade or hydrolyze the plentiful polysaccharide xylan, an important component of hemicellulose. It mainly cleaves the backbone of xylan that is made up of a number of xylose residues connected with β-1,4-glycosidic linkages. Fungi with mycelia are regarded as the best producer of xylanases. These varied xylanases not only differ in their sizes and shapes but also differ in their physicochemical properties. Depending on the optimum pH in which they work best, they have been classified into (1) acidophilic xylanases active at low pH or acidic pH range, (2) alkaliphilic xylanases that are active at high or alkaline pH range and (3) neutral xylanases having pH optima in the neutral range between pH 5 and 7. Other researchers have classified the xylanases also on the basis of their structural properties, kinetic parameters, etc. This review discusses the molecular structures of some acidophilic xylanases and the molecular basis of low pH optima observed for their activities. It also discusses their unique catalytic mechanism and actual role of the catalytic residues found in them. Apart from these, the review also discusses different applications of these acidophilic xylanases in different industries. The article concludes with brief suggestions about how these acidophilic xylanases can be created employing the techniques of genetic engineering and concepts of synthetic evolution, using the traits of the known acidophilic xylanases discussed in the review.

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Microbial Xylanases: Sources, Types, and Their Applications

Cited by 13 publications

References 263 publications

Production of Amylase by Aspergillus subflavus and Aspergillus fumigatus from flamevine flower (Pyrostegia venusta (Ker-Gawl.) Miers): A Tropical Plant in Bedugul Botanical Garden, Bali, Indonesia

Production of Amylase by Aspergillus subflavus and Aspergillus fumigatus from flamevine flower (Pyrostegia venusta (Ker-Gawl.) Miers): A Tropical Plant in Bedugul Botanical Garden, Bali, Indonesia

A novel acid‐tolerant β‐xylanase fromScytalidium candidum3C for the synthesis ofo‐nitrophenyl xylooligosaccharides

Molecular structure and catalytic mechanism of fungal family G acidophilic xylanases

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