Acid protease from Trichoderma reesei : limited proteolysis of fungal carbohydrases

Eneyskaya, Elena V.; Kulminskaya, Anna A.; Savel'ev, Andrew N.; Savel'eva, N. V.; Shabalin, Konstantin A.; Neustroev, Kirill N.

doi:10.1007/s002530051513

Cited by 34 publications

(19 citation statements)

References 14 publications

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“…2). Furthermore, ≥70% activity remained after 24 hours of incubation at room temperature at pH ranges of 2.0-4.0, in conformity with the results reported by Li [27], Jose [23], Eneyslaya [28], Yin [24], and Chen [25]. According to the studies conducted by Hsiao [29], Kumar [11], Li [33] and Xu [35], the optimal pH values of extracellular acid protease from Rhizopus oryzae, and Aspergillus spp.…”

Section: Results and Disscusionsupporting

confidence: 70%

Partial Characterization of an Acidic Protease from Rhizopus stolonifer RN-11

Liu¹,

Huang²

2015

TOBIOTJ

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Abstract:The present study characterises an acidic protease purified from the Rhizopus stolonifer strain, RN-11. The acidic protease with a 70 kDa molecular weight, was stable within pH 2-4 at temperatures 40-50℃. The temperature and pH value conducive to optimal catalytic activity were pH 2.5 and 50℃, respectively. Treatment with 5 mmol metal ions showed that the acidic protease was activated by Na . It was proposed that the studied acidic protease might represent a previously uncharacterised type of acidic protease produced by the Rhizopus stolonifer RN-11 strain.

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Section: Results and Disscusionsupporting

confidence: 70%

Partial Characterization of an Acidic Protease from Rhizopus stolonifer RN-11

Liu¹,

Huang²

2015

TOBIOTJ

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“…To understand the mechanism of the fungal growth inhibition by ATBI, we have investigated the role of two essential hydrolytic enzymes, xylanase and aspartic protease, which are crucial for the growth of phytopathogenic fungal strains and, thus, in their biosynthetic pathway. The productions of xylanase and aspartic protease are well documented in A. oryzae (11,41) and in T. reesei (5,18). The growth of T. reesei and A. oryzae on the synthetic agar medium containing xylan or casein was inhibited by ATBI (Fig.…”

Section: Resultsmentioning

confidence: 92%

Novel Bifunctional Inhibitor of Xylanase and Aspartic Protease: Implications for Inhibition of Fungal Growth

Dash

Ahmad

Nath

et al. 2001

Antimicrob Agents Chemother

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A novel bifunctional inhibitor (ATBI) from an extremophilic Bacillus sp. exhibiting an activity against phytopathogenic fungi, including Alternaria, Aspergillus, Curvularia, Colletotricum, Fusarium, and Phomopsis species, and the saprophytic fungus Trichoderma sp. has been investigated. The 50% inhibitory concentrations of ATBI ranged from 0.30 to 5.9 g/ml, whereas the MIC varied from 0.60 to 3.5 g/ml for the fungal growth inhibition. The negative charge and the absence of periodic secondary structure in ATBI suggested an alternative mechanism for fungal growth inhibition. Rescue of fungal growth inhibition by the hydrolytic products of xylanase and aspartic protease indicated the involvement of these enzymes in cellular growth. The chemical modification of Asp or Glu or Lys residues of ATBI by 2,4,6-trinitrobenzenesulfonic acid and Woodward's reagent K, respectively, abolished its antifungal activity. In addition, ATBI also inhibited xylanase and aspartic protease competitively, with K i values 1.75 and 3.25 M, respectively. Our discovery led us to envisage a paradigm shift in the concept of fungal growth inhibition for the role of antixylanolytic activity. Here we report for the first time a novel class of antifungal peptide, exhibiting bifunctional inhibitory activity.The primary current means for the identification of new antifungal agents are represented by screening of the vast biodiversity prevalent in natural resources such as soil samples, marine waters, insects, and tropical plants (6,8). The need for safe and effective antifungal agents has triggered considerable interest in the isolation of new compounds from biological resources. The rapid emergence of fungal pathogens resistant to currently available antibiotics has further compounded the dearth of novel antifungal agents. The past decade has witnessed a dramatic growth in knowledge of natural peptides from plants, animals, and microorganisms. These peptides play an important role in the protection of plants from invasive infection and could prove to be useful tools for the genetic engineering of fungal resistance in transgenic plants (40).Antifungal peptides are classified into two classes based on their mode of action (17). The first group acts by lysis, which occurs via several mechanisms (34). Lytic peptides may be amphipathic, having two faces, with one being positively charged and the other being neutral and hydrophobic. The second class of peptide interferes with the cell wall synthesis or the biosynthesis of essential components (14). The biological activities of a large number of peptide toxins have been rationalized in terms of the peptides' having the ability to adopt amphiphilic ␣-helical structures (15,16,21). Peptides are expected to have value as alternative agents in the fight against new resistant microbial strains as they have modes of action different from those of classical antibiotics. The characterization of such new antifungal and antimicrobial peptides and the design of analogues with improved activities have allowed better ...

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“…awamori using a non-native A. niger glucoamylase signal peptide was lost after 72 h of cultivation due to protease degradation [42]. In addition to their undesired influence on cellulase yields, intracellular proteases are hypothesized to positively control enzyme release, activity, stability and posttranslational modifications, resulting in the production of enzyme isoforms [105,106,108], and the type and extent of these proteolytic modifications might vary in different heterologous hosts [109].…”

Section: Proteolytic Degradation Of Heterologously Expressed Cellobiomentioning

confidence: 99%

Heterologous expression of cellobiohydrolases in filamentous fungi – An update on the current challenges, achievements and perspectives

Zoglowek

Lübeck

Ahring

et al. 2015

Process Biochemistry

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Acid protease from Trichoderma reesei : limited proteolysis of fungal carbohydrases

Cited by 34 publications

References 14 publications

Partial Characterization of an Acidic Protease from Rhizopus stolonifer RN-11

Partial Characterization of an Acidic Protease from Rhizopus stolonifer RN-11

Novel Bifunctional Inhibitor of Xylanase and Aspartic Protease: Implications for Inhibition of Fungal Growth

Heterologous expression of cellobiohydrolases in filamentous fungi – An update on the current challenges, achievements and perspectives

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