Production of GH11 xylanase for bakery industry by solid state fermentation

Tekkol, Gizem Ezgi; Sargın, Sayıt; Karaçanci, Sevket; Pembeci, Ceyda; Mandaci, Sevnur; Akgün, İsmail Hakkı; Altinel, Burak; Öngen, Gaye

doi:10.1016/j.jbiotec.2017.06.985

Cited by 2 publications

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“…Use of xylanase enzymes was previously shown to enhance the enzymatic hydrolysis of lignocellulosic substrates [ 52 ]. In addition, xylanases are used in bread making to increase volume of the bread and contribute to improved bread quality, faster baking times and increased yields [ 25 ]. Wheat flour is treated with xylanase to break down hemicellulose, increasing the binding of water to the flour, allowing it to become softer and more elastic [ 53 ].…”

Section: Discussionmentioning

confidence: 99%

“…The microalgal permeate fraction was processed for mass spectrometry analysis using the Preomics Phoenix Cleanup Kit (96×), (Preomics, D-82152 Planegg/Martinsried, Germany) in accordance with the manufacturers’ instructions and described previously [ 25 ]. The sample was acidified and hydrophobic and hydrophilic contaminants removed using a series of wash steps and peptides eluted from the cartridge and prepared in loading buffer for LC-MS analysis.…”

Section: Methodsmentioning

confidence: 99%

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Identification of Bioactive Peptides from Nannochloropsis oculata Using a Combination of Enzymatic Treatment, in Silico Analysis and Chemical Synthesis

Hayes

Lucáková

2022

Biomolecules

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In vitro ACE-1 inhibitory peptides were characterised previously from a number of microalgal species including Spirulina platensis (peptide IAPG), Chlorella vulgaris (peptides FDL, AFL, VVPPA), Isochrysis galbana (peptide YMGLDLK), Chlorella sorokiniana (peptides IW and LW) and indeed Nannochloropsis oculata (peptides GMNNLTP and LEQ). The isolation of protein from Nannochloropsis oculata using a combination of ammonium salt precipitation and xylanase treatment of resulting biomass combined with molecular weight cut off filtration to produce a permeate and characterisation of bioactive peptides is described. The Angiotensin-1-converting enzyme (ACE-1) IC50 value for the generated permeate fraction was 370 µg/mL. Ninety-five peptide sequences within the permeate fraction were determined using mass spectrometry and eight peptides were selected for chemical synthesis based on in silico analysis. Synthesized peptides were novel based on a search of the literature and relevant databases. In silico, simulated gastrointestinal digestion identified further peptides with bioactivities including ACE-1 inhibitory peptides and peptides with antithrombotic and calcium/calmodulin-dependent kinase II (CAMKII) inhibition. This work highlights the potential of Nannochloropsis oculata biomass as both a protein and bioactive peptide resource, which could be harnessed for use in the development of functional foods and feeds.

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Section: Discussionmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

Identification of Bioactive Peptides from Nannochloropsis oculata Using a Combination of Enzymatic Treatment, in Silico Analysis and Chemical Synthesis

Hayes

Lucáková

2022

Biomolecules

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“…In bread making, xylanases are used with other enzymes because they have the potential benefit of enhancing the volume of the bread and contributing to its improved quality and they allow faster baking times and increase yields ( Tekkol et al, 2017 ). Wheat flour is treated with xylanase to break down hemicellulose, increasing the binding of water to the flour, allowing it to become softer and more elastic ( Dahiya and Singh, 2019 ).…”

Section: Biotechnological Application Of Thermostable Cellulases and Xylanasesmentioning

confidence: 99%

Thermostable Cellulases / Xylanases From Thermophilic and Hyperthermophilic Microorganisms: Current Perspective

Ajeje¹,

Hu²,

Song³

et al. 2021

Front. Bioeng. Biotechnol.

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The bioconversion of lignocellulose into monosaccharides is critical for ensuring the continual manufacturing of biofuels and value-added bioproducts. Enzymatic degradation, which has a high yield, low energy consumption, and enhanced selectivity, could be the most efficient and environmentally friendly technique for converting complex lignocellulose polymers to fermentable monosaccharides, and it is expected to make cellulases and xylanases the most demanded industrial enzymes. The widespread nature of thermophilic microorganisms allows them to proliferate on a variety of substrates and release substantial quantities of cellulases and xylanases, which makes them a great source of thermostable enzymes. The most significant breakthrough of lignocellulolytic enzymes lies in lignocellulose-deconstruction by enzymatic depolymerization of holocellulose into simple monosaccharides. However, commercially valuable thermostable cellulases and xylanases are challenging to produce in high enough quantities. Thus, the present review aims at giving an overview of the most recent thermostable cellulases and xylanases isolated from thermophilic and hyperthermophilic microbes. The emphasis is on recent advancements in manufacturing these enzymes in other mesophilic host and enhancement of catalytic activity as well as thermostability of thermophilic cellulases and xylanases, using genetic engineering as a promising and efficient technology for its economic production. Additionally, the biotechnological applications of thermostable cellulases and xylanases of thermophiles were also discussed.

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Production of GH11 xylanase for bakery industry by solid state fermentation

Cited by 2 publications

References 0 publications

Identification of Bioactive Peptides from Nannochloropsis oculata Using a Combination of Enzymatic Treatment, in Silico Analysis and Chemical Synthesis

Identification of Bioactive Peptides from Nannochloropsis oculata Using a Combination of Enzymatic Treatment, in Silico Analysis and Chemical Synthesis

Thermostable Cellulases / Xylanases From Thermophilic and Hyperthermophilic Microorganisms: Current Perspective

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