Fungal β-mannanases: Mannan hydrolysis, heterologous production and biotechnological applications

Zyl, Willem H. van; Rose, Shaunita H.; Trollope, Kim M.; Görgens, Johann F.

doi:10.1016/j.procbio.2010.05.011

Cited by 160 publications

(120 citation statements)

References 123 publications

(137 reference statements)

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“…Both the signal peptidases target the protein to the secretory pathway. The presence of signal peptide is supportive with the fact that the native protein is to be secreted to the extracellular environment in order to degrade organic matters that are used as carbon sources for their growth [2,4].…”

Section: Nucleotide and Amino Acids Sequence Analysismentioning

confidence: 97%

“…In hemicellulose, there are two major components which are xylan and mannan [1]. These components posed various economical values such as in the feedstock for foods and feeds [2]. Mannan can be a branched or linear polymer divided into four subclasses, namely linear mannan, glucomannan, galactomannan and galactoglucomannan [3,4].…”

Section: Introductionmentioning

confidence: 99%

“…and Trichoderma sp. are well-known for producing hemicellulases, mainly xylanase and mannanases [1,2]. Mannan-degrading enzymes are one of the major hemicellulase being studied.…”

Section: Introductionmentioning

confidence: 99%

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In silico analysis of β-mannanases and β-mannosidase from Aspergillus flavus and Trichoderma virens UKM1

Yee

Murad²,

Bakar³

2013

AIP Conference Proceedings

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Abstract.A gene encoding an endo--1,4-mannanase from Trichoderma virens UKM1 (manTV) and Aspergillus flavus UKM1 (manAF) was analysed with bioinformatic tools. In addition, A. flavus NRRL 3357 genome database was screened for a -mannosidase gene and analysed (mndA-AF). These three genes were analysed to understand their gene properties. manTV and manAF both consists of 1,332-bp and 1,386-bp nucleotides encoding 443 and 461 amino acid residues, respectively. Both the endo--1,4-mannanases belong to the glycosyl hydrolase family 5 and contain a carbohydrate-binding module family 1 (CBM1). On the other hand, mndA-AF which is a 2,745-bp gene encodes a protein sequence of 914 amino acid residues. This -mannosidase belongs to the glycosyl hydrolase family 2. Predicted molecular weight of manTV, manAF and mndA-AF are 47.74 kDa, 49.71 kDa and 103 kDa, respectively. All three predicted protein sequences possessed signal peptide sequence and are highly conserved among other fungalmannanases and -mannosidases.

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Section: Nucleotide and Amino Acids Sequence Analysismentioning

confidence: 97%

Section: Introductionmentioning

confidence: 99%

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In silico analysis of β-mannanases and β-mannosidase from Aspergillus flavus and Trichoderma virens UKM1

Yee

Murad²,

Bakar³

2013

AIP Conference Proceedings

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“…For example, the increased availability and high specifi city of β-mannanases have been used for numerous applications, such as production of manno-oligosaccharides, pharmaceutical applications, instant coffee production, animal feeds, paper and pulp production, detergent formulations etc. ( VAN ZYL et al, 2010;LU et al, 2014). β-Mannanase could be generally produced by various Aspergillus species ( VAN ZYL et al, 2010) and the activity of the produced enzymes can differ from species to species.…”

mentioning

confidence: 99%

“…( VAN ZYL et al, 2010;LU et al, 2014). β-Mannanase could be generally produced by various Aspergillus species ( VAN ZYL et al, 2010) and the activity of the produced enzymes can differ from species to species. Also, other microorganisms have been evaluated for β-mannanase productions.…”

mentioning

confidence: 99%

Enhanced β-mannanase production from alternative sources by recombinant Aspergillus sojae

Yatmaz¹,

Karahalil²,

Germeç³

et al. 2016

Acta Alimentaria

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β-mannanases can degrade galactomannans to mannose and it has been used in various application areas. The aim of this study was to produce the β-mannanase from carob pod extract including different nitrogen sources. The best operation values for fermentation were determined to be 8% initial sugar concentration with 0.5% yeast extract, 100 r.p.m., and 7% inoculation rate, which yielded the maximum β-mannanase activity as 423.60 U ml -1 . Effects of nitrogen sources on β-mannanase activity were also studied and it reached 695.6 U ml -1 by using 0.5% of ammonium nitrate as the nitrogen source at the determined optimum conditions. Results also showed that meat bone meal and soybean meal could be used as cost effective nitrogen sources based on achieved β-mannanase activity.Keywords: β-mannanase, recombinant Aspergillus sojae, carbon sources, nitrogen sourcesMicrobial mannanase has gained signifi cant attention, since it degrades the complex polysaccharides of plant tissues into simple small molecules such as manno-oligosaccharides and mannose. For example, the increased availability and high specifi city of β-mannanases have been used for numerous applications, such as production of manno-oligosaccharides, pharmaceutical applications, instant coffee production, animal feeds, paper and pulp production, detergent formulations etc. ( VAN ZYL et al., 2010;LU et al., 2014). β-Mannanase could be generally produced by various Aspergillus species ( VAN ZYL et al., 2010) and the activity of the produced enzymes can differ from species to species. Also, other microorganisms have been evaluated for β-mannanase productions. CHEN and coworkers (2007) expressed Aspergillus sulphures β-mannanase gene in Pichia pastoris and the specifi c activity was found to be 366 U ml -1 in locust bean gum. OZTURK and co-workers (2010) used recombinant Aspergillus sojae ATCC11906 (AsT1) for β-mannanase production from molasses and found the highest activity value as 363 U ml -1. WANG and co-workers (2010) have found that Pantoea agglomerans A021 could produce β-mannanase from konjac powder and the maximum activity of purifi ed Man26P was 514 U mg -1. WU and co-workers (2011) used Aspergillus niger E-30 to produce the β-mannanase from peeled potato and the maximum β-mannanase activity value was 1067.5 U mg -1 by purifi ed enzyme solution

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Biofuels: Fungal, Bacterial and Insect Degraders of Lignocellulose

Sethi

Scharf

2013

Encyclopedia of Life Sciences

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Lignocellulose is the main structural component of plant cell walls and can be degraded into simple sugars with the help of hydrolytic enzymes. Lignocellulose is composed of three polymers: cellulose, hemicellulose and lignin. Certain fungi, bacteria and insects have evolved the ability to degrade lignocellulose. Cellulose is degraded to glucose by the synergistic action of three distinct classes of enzymes: endoglucanases, exoglucanases and β‐glucosidases. Owing to its variable structure and organisation, hemicellulose degradation requires various enzymes with diverse modes of action, which include endoxylanases, endomannanases, β‐xylosidases, β‐mannosidases, β‐galactosidases, α‐glucuronidases, α‐arabinofurnosidases, α‐galactosidases, acetyl xylan esterases, feruloyl esterases and glucuronyl esterases. Lignin degradation is much more difficult due to its complex structure and bonding to carbohydrate complexes. It requires oxidative enzymes, such as lignin peroxidases, manganese peroxidases, versatile peroxidases, laccases, and several other auxiliary enzymes. Commercial biofuel production from lignocellulosic materials can be achieved by artificially producing these cellulases, hemicellulases and lignases in recombinant form. Key Concepts: Lignocellulose is the most abundant renewable resource of energy on the Earth. Lignocellulose is a general term referring to a natural complex of three biopolymers: cellulose, hemicellulose and lignin. Simple sugar can be released from lignocellulose using three categories of enzymes: cellulases, hemicellulase and lignases. Released sugars from lignocellulose can be fermented into biofuel (ethanol). Wood‐rotting fungi such as white‐rot, brown‐rot and soft‐rot fungi can degrade lignocellulose. Aerobic and anaerobic bacteria such as Bacillus, Streptomyces, Cellulomonas and Clostridium possess lignocellulose‐degrading enzymes. Wood and plant‐feeding insects such termites, roaches, longhorn beetles and grasshoppers are rich sources of novel lignocellulases genes. Lignocellulases of fungal, bacterial and insect origin can be artificially/recombinantly produced in various protein expression systems. Fungal, bacterial and insect lignocellulases are expected to play important roles in the development of successful lignocellulose conversion technologies.

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Fungal β-mannanases: Mannan hydrolysis, heterologous production and biotechnological applications

Cited by 160 publications

References 123 publications

In silico analysis of β-mannanases and β-mannosidase from Aspergillus flavus and Trichoderma virens UKM1

In silico analysis of β-mannanases and β-mannosidase from Aspergillus flavus and Trichoderma virens UKM1

Enhanced β-mannanase production from alternative sources by recombinant Aspergillus sojae

Biofuels: Fungal, Bacterial and Insect Degraders of Lignocellulose

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