Production, purification, and biochemical characterization of serine alkaline protease from Penicillium chrysogenium strain X5 used as excellent bio-additive for textile processing

Benmrad, Maroua Omrane; Moujehed, Emna; Elhoul, Mouna Ben; Mechri, Sondes; Béjar, Samír; Zouari, Riadh; Baffoun, Ayda; Jaouadi, Bassem

doi:10.1016/j.ijbiomac.2018.07.194

Cited by 40 publications

(17 citation statements)

References 44 publications

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“…This indicates that the SPPS enzyme acts on hydrophobic amino–acid residues attached to the carboxyl side of the cleavage sites of the chromogenic substrate. These characteristics, were in line with the other previously depicted subtilisins from bacterial [28, 32] and fungal [26, 33, 41, 42] origins. This indicated that the SPPS protease was slightly similar to subtilisins, not only in terms of specificity for position P1, but also with regard to the effects of amino-acids residues related to the cleavage site of the enzyme.…”

Section: Resultssupporting

confidence: 91%

Purification and biochemical characterization of a novel thermostable protease from the oyster mushroom Pleurotus sajor-caju strain CTM10057 with industrial interest

et al. 2019

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Background: Proteases are hydrolytic enzymes that catalyze peptide linkage cleavage reactions at the level of proteins and peptides with different degrees of specificity. This group draws the attention of industry. More than one protease in three is a serine protease. Classically, they are active at neutral to alkaline pH. The serine proteases are researched for industrial uses, especially detergents. They are the most commercially available enzyme group in the world market. Overall, fungi produced extracellular proteases, easily separated from mycelium by filtration. Results: A new basidiomycete fungus CTM10057, a hyperproducer of a novel protease (10,500 U/mL), was identified as Pleurotus sajor-caju (oyster mushroom). The enzyme, called SPPS, was purified to homogeneity by heattreatment (80°C for 20 min) followed by ammonium sulfate precipitation (35-55%)-dialysis, then UNO Q-6 FPLC ion-exchange chromatography and finally HPLC-ZORBAX PSM 300 HPSEC gel filtration chromatography, and submitted to biochemical characterization assays. The molecular mass was estimated to be 65 kDa by sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE), Native-PAGE, casein-zymography, and size exclusion by HPLC. A high homology with mushroom proteases was displayed by the first 26 amino-acid residues of the NH 2-terminal aminoacid sequence. Phenylmethanesulfonyl fluoride (PMSF) and diiodopropyl fluorophosphates (DFP) strongly inhibit SPPS, revealing that it is a member of the serine-proteases family. The pH and temperature optima were 9.5 and 70°C, respectively. Interestingly, SPPS possesses the most elevated hydrolysis level and catalytic efficiency in comparison with SPTC, Flavourzyme® 500 L, and Thermolysin type X proteases. More remarkably, a high tolerance towards organic solvent tolerance was exhibited by SPPS, together with considerable detergent stability compared to the commercial proteases Thermolysin type X and Flavourzyme® 500 L, respectively. Conclusions: This proves the excellent proprieties characterizing SPPS, making it a potential candidate for industrial applications especially detergent formulations.

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Section: Resultssupporting

confidence: 91%

Purification and biochemical characterization of a novel thermostable protease from the oyster mushroom Pleurotus sajor-caju strain CTM10057 with industrial interest

et al. 2019

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“… Removal of starch coating (desizing) Aggarwal et al 2019 Pectinases A. tamarii Bioscouring and phytopigments processing Shanmugavel et al 2018 Laccases Phomopsis sp. Bleaching and deinking and biotransformation of aniline blue Navada and Kulal, 2020 Cold-active Lipases Penicillium canesense BPF4 and Pseudogymnoascus roseus BPF6 Lipid stain removal and facilitating cold washing as a step towards mitigation of climate change Sahay and Chouhan 2018 Serine alkaline Proteases Penicillium chrysogenium X5 Protein stain removal Omrane Benmrad et al 2018 Biodiesel and bioethanol Lipases Beauveria bassiana expressed in Aspergillus nidulans A773 Transesterification of triglycerides (biodiesel) Spiropulos Gonçalves et al 2020 Cellulases A. oryzae MDU-4 Cellulose hydrolysis in lignocellulosic ethanol production Saini et al 2020 Xylanases Thermomyces lanuginosus and Trichoderma reesei Degradation of hemicellulose Juodeikiene et al 2011 Laccases Ganoderma lucidum MDU-7 Digestion of lignin waste Saini et al 2020 Leather Lignolytic enzymes Trametes villosa SCS-10 Removal of unwanted fats and dyes during soaking and liming process and treatment of wastewater Ortiz-Monsalve et al 2017 …”

Section: Regulatory Aspects Of Mycozyme Secretionmentioning

confidence: 99%

Recent Developments in Industrial Mycozymes: A Current Appraisal

Nath

Kango

2021

Mycology

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Fungi, being natural decomposers, are the most potent, ubiquitous and versatile sources of industrial enzymes. About 60% of market share of industrial enzymes is sourced from filamentous fungi and yeasts. Mycozymes (myco-fungus; zymes-enzymes) are playing a pivotal role in several industrial applications and a number of potential applications are in the offing. The field of mycozyme production, while maintaining the old traditional methods, has also witnessed a sea change due to advents in recombinant DNA technology, optimisation protocols, fermentation technology and systems biology. Consolidated bioprocessing of abundant lignocellulosic biomass and complex polysaccharides is being explored at an unprecedented pace and a number of mycozymes of diverse fungal origins are being explored using suitable platforms. The present review attempts to revisit the current status of various mycozymes, screening and production strategies and applications thereof.

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“…The escalating demand of alkaline proteases in various industries entails the need of definite properties of enzyme like thermal stability profile, catalytic efficiency at higher pH, substrate specificity, kinetic studies, activity and stability in presence of organic solvents, surfactants etc. [19, 20, 21]. Bacillus derived alkaline proteases are stable at elevated temperatures and pH, but a majority are incompatible with detergent matrices [22, 23].…”

Section: Introductionmentioning

confidence: 99%

A novel thiol-dependent serine protease from Neocosmospora sp. N1

Matkawala

Nighojkar²,

Kumar

et al. 2019

Heliyon

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Alkaline proteases have several industrial applications. In the present study, newly isolated Neocosmospora sp. N1 was screened as hyper producer of serine protease. A multimeric protease of the fungus was purified to homogeneity till 96.78 fold purification with 22.51% recovery. The homogeneity of purified enzyme was checked by native PAGE and its molecular weight was found to be 198.03 kDa by MALDI-TOF. On SDS-PAGE analysis, enzyme was found to be a hetero oligomer of 17.66 kDa and 20.89 kDa subunits. The purified enzyme showed maximum activity with casein as substrate at 60 C and pH 8.5. The K m and V max values were found to be 0.015 mg/ml and 454.45 U/ml, respectively. The enzyme was completely inhibited by PMSF, while the activity was 40% enhanced using β-mercaptoethanol, suggesting that it is a thiol-dependent serine protease. The purified protease was active over an alkaline pH range from 7 to 12 and temperatures from 20 C to 60 C. The enzyme exhibited excellent stability, almost 100% towards organic solvents such as toluene, benzene and hexane, surfactants such as Triton X-100, Tween-20, Tween-80 and SDS, as well as commercial detergents. The significant properties of purified enzyme assure that it could be a potential candidate for commercial purposes.

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Production, purification, and biochemical characterization of serine alkaline protease from Penicillium chrysogenium strain X5 used as excellent bio-additive for textile processing

Cited by 40 publications

References 44 publications

Purification and biochemical characterization of a novel thermostable protease from the oyster mushroom Pleurotus sajor-caju strain CTM10057 with industrial interest

Purification and biochemical characterization of a novel thermostable protease from the oyster mushroom Pleurotus sajor-caju strain CTM10057 with industrial interest

Recent Developments in Industrial Mycozymes: A Current Appraisal

A novel thiol-dependent serine protease from Neocosmospora sp. N1

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