Protein engineering of GH10 family xylanases for gaining a resistance to cereal proteinaceous inhibitors

Denisenko, Yury A.; Gusakov, Alexander V.; Рожкова, А. М.; Зоров, И. Н.; Bashirova, Anna V.; Matys, V. Yu.; Немашкалов, В. А.; Sinitsyn, A. P.

doi:10.1016/j.bcab.2019.01.042

Cited by 15 publications

(8 citation statements)

References 30 publications

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“…GH10 bacterial xylanases and fungal Aspergillus aculeatus AaXyl2 have two amino acid insertions in the primary structure with respect to AnidXlnC xylanase, which explains their resistance to XIP-type inhibitors. Confirming this hypothesis, all fungal xylanases resistant to the XIP inhibition have two similar insertions [ 92 ]. Interestingly, XIP-I shows structural homology with some type III chitinases belonging to the GH18 family classified into the PR-8 class, although XIP-I has no chitinase activity.…”

Section: Structural Properties Of Xylanase-xi Interactionmentioning

confidence: 75%

“…The genetic engineering approach is an attractive strategy to increase the variability and functionality of xylanases used for industrial applications ( Table 2 ). Heterologous expression of the GH10 xylanases PcXylA from Penicillium canescens and TrXyn3 from Trichoderma reesei, with an insertion of 5 amino acid residues into the peptide loop forming the active site cleft, reduced the inhibition of recombinant xylanases by the XIs from rye compared to corresponding wild-type xylanases [ 92 ]. On the other hand, the authors detected a moderate decrease in thermostability and in specific activity against glucuronoxylan for PcXylA-ins and TrXyn3-ins because of the insertion.…”

Section: Strategies To Reduce the Effect Of Xis In Food Processing An...mentioning

confidence: 99%

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Xylanase Inhibitors: Defense Players in Plant Immunity with Implications in Agro-Industrial Processing

Tundo

Mandalà

Sella

et al. 2022

IJMS

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Xylanase inhibitors (XIs) are plant cell wall proteins largely distributed in monocots that inhibit the hemicellulose degrading activity of microbial xylanases. XIs have been classified into three classes with different structures and inhibition specificities, namely Triticum aestivum xylanase inhibitors (TAXI), xylanase inhibitor proteins (XIP), and thaumatin-like xylanase inhibitors (TLXI). Their involvement in plant defense has been established by several reports. Additionally, these inhibitors have considerable economic relevance because they interfere with the activity of xylanases applied in several agro-industrial processes. Previous reviews highlighted the structural and biochemical properties of XIs and hypothesized their role in plant defense. Here, we aimed to update the information on the genomic organization of XI encoding genes, the inhibition properties of XIs against microbial xylanases, and the structural properties of xylanase-XI interaction. We also deepened the knowledge of XI regulation mechanisms in planta and their involvement in plant defense. Finally, we reported the recently studied strategies to reduce the negative impact of XIs in agro-industrial processes and mentioned their allergenicity potential.

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Section: Structural Properties Of Xylanase-xi Interactionmentioning

confidence: 75%

Section: Strategies To Reduce the Effect Of Xis In Food Processing An...mentioning

confidence: 99%

Xylanase Inhibitors: Defense Players in Plant Immunity with Implications in Agro-Industrial Processing

Tundo

Mandalà

Sella

et al. 2022

IJMS

View full text Add to dashboard Cite

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“…Debyser, Derdelinckx, and Delcour (1997a) first reported that wheat ( Triticum aestivum ) contained proteinaceous xylanase inhibitor which inhibited the xylanolytic system of malted barley. So far, three proteinaceous xylanase inhibitors have been purified and characterized from cereals, including Triticum aestivum xylanase inhibitor (TAXI) (Leys, De Bondt, Schreurs, & Courtin, 2019), thaumatin‐like xylanase inhibitor (TLXI) (Denisenko et al, 2019), and xylanase‐inhibiting protein (XIP) (Liu, Zhang, Wei, Chen, & Jia, 2017). The reported proteinaceous xylanase inhibitors hereto in cereals are active toward microbial xylanases, and no proteins have been reported to have the ability to inhibit the catalytic activity of the cereal endogenous xylanases (Denisenko et al, 2019).…”

Section: Introductionmentioning

confidence: 99%

“…So far, three proteinaceous xylanase inhibitors have been purified and characterized from cereals, including Triticum aestivum xylanase inhibitor (TAXI) (Leys, De Bondt, Schreurs, & Courtin, 2019), thaumatin‐like xylanase inhibitor (TLXI) (Denisenko et al, 2019), and xylanase‐inhibiting protein (XIP) (Liu, Zhang, Wei, Chen, & Jia, 2017). The reported proteinaceous xylanase inhibitors hereto in cereals are active toward microbial xylanases, and no proteins have been reported to have the ability to inhibit the catalytic activity of the cereal endogenous xylanases (Denisenko et al, 2019). Proteinaceous xylanase inhibitors seriously affect the catalytic activity of microbial xylanases in cereal processing (Denisenko et al, 2019; Leys et al, 2019).…”

Section: Introductionmentioning

confidence: 99%

“…The reported proteinaceous xylanase inhibitors hereto in cereals are active toward microbial xylanases, and no proteins have been reported to have the ability to inhibit the catalytic activity of the cereal endogenous xylanases (Denisenko et al, 2019). Proteinaceous xylanase inhibitors seriously affect the catalytic activity of microbial xylanases in cereal processing (Denisenko et al, 2019; Leys et al, 2019).…”

Section: Introductionmentioning

confidence: 99%

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Barley α‐amylase/subtilisin inhibitor shows inhibitory activity against endogenous xylanase isozyme I of malted barley: A novel protein function

Sun

2020

J Food Biochem

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Mashing process had little influence on the arabinoxylan content in the finished wort. In this paper, a protein with inhibitory activity against the endogenous xylanase isozyme I (X‐I) of malted barley was extracted and purified using a combination of ion‐exchange and size‐exclusion chromatography. The protein was identified as barley α‐amylase/subtilisin inhibitor (BASI). According to the amino acid sequence analysis, BASI was completely different from the previous reported xylanase inhibitors. BASI showed dosage‐dependent inhibitory activity. BASI exhibited a maximum inhibitory activity at 50°C and pH 6.0. BASI inhibited X‐I as a competitive manner. Practical applications A protein with inhibitory activity against the major endogenous xylanase isozyme I (X‐I) of malted barley was extracted, purified, and characterized, which was identified as barley α‐amylase/subtilisin inhibitor (BASI). The results help brewers to achieve a better understanding of the mechanism of arabinoxylan degradation during mashing. BASI can be used as an indicator to screen microbial xylanases. The microbial xylanases insensitive to BASI would have obvious advantages in the degradation of arabinoxylan polymers and filterability improvement during mashing.

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The Role of Microbial Diversity in Lignocellulosic Biomass Degradation: A Biotechnological Perspective

Rasool,

Irfan

2024

ChemBioEng Reviews

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Lignocellulosic biomass, such as plant residues and agricultural waste, holds immense potential as a renewable resource for the production of biofuels, chemicals, and animal feed. However, the efficient degradation of lignocellulose into fermentable sugars remains a significant challenge. Recent research has highlighted the critical role of microbial diversity in lignocellulosic biomass degradation, offering new insights from a biotechnological perspective. The comprehension and utilization of microbial diversity are crucial for developing efficient biotechnological strategies for lignocellulosic biomass degradation. By uncovering the intricate relationships between microbial communities and their enzymatic machinery, researchers can optimize degradation processes, enhance biofuel production, and contribute to a more sustainable bio‐based economy. Microorganisms, including bacteria, fungi, and archaea, possess diverse enzymatic capabilities, allowing them to secrete a plethora of lignocellulolytic enzymes. Microbial organisms inhabiting extreme environments, such as the rumen, hot and cold springs, deep sea trenches, and acidic and alkaline pH environments, exhibit significant potential in generating enzymes, including hemicellulolytic and lignocellulolytic enzymes, which possess superior biochemical properties essential for industrial bioconversion applications. This review explores the ability of lignocellulosic enzymes from microbial sources to efficiently break down the lignocellulosic biomass and their potential applications in industrial biotechnology.

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Protein engineering of GH10 family xylanases for gaining a resistance to cereal proteinaceous inhibitors

Cited by 15 publications

References 30 publications

Xylanase Inhibitors: Defense Players in Plant Immunity with Implications in Agro-Industrial Processing

Xylanase Inhibitors: Defense Players in Plant Immunity with Implications in Agro-Industrial Processing

Barley α‐amylase/subtilisin inhibitor shows inhibitory activity against endogenous xylanase isozyme I of malted barley: A novel protein function

The Role of Microbial Diversity in Lignocellulosic Biomass Degradation: A Biotechnological Perspective

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