Purification and Characterization of a New Endo-1,4-β-<scp>D</scp>-glucanase fromBeltraniella portoricensis

Baba, Yuko; Shimonaka, Atsushi; Koga, Jinichiro; Murashima, Koichiro; Kubota, Hitomi; Kono, Toshiaki

doi:10.1271/bbb.69.1198

Cited by 11 publications

(4 citation statements)

References 14 publications

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“…2A and B) and the optimal pH for BCE1, EGI, and EGII was acidic (3,32,37), these endoglucanases are not suitable for laundry use. Hence, we concluded that further characterization of BCE1, EGI, EGII, and EGVI for laundry use is not required.…”

Section: Resultsmentioning

confidence: 99%

Purification and Characterization of a New Family 45 Endoglucanase, STCE1, from Staphylotrichum coccosporum and Its Overproduction in Humicola insolens

Koga

Baba

Shimonaka

et al. 2008

Appl Environ Microbiol

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In the detergent industry, fungal endoglucanases have been used to release microfibrils (defibrillation) from the surface of dyed cellulosic fabrics to enhance color brightness. Although endoglucanases for laundry use must have various properties, such as a neutral or alkaline optimum pH, resistance to anionic surfactants and oxidizing agents (main components in detergents), and high defibrillation activity, all-purpose endoglucanases have not been obtained yet. As a result of screening of endoglucanases, a new family 45 endoglucanase (family 45 glycoside hydrolase), designated STCE1, was obtained and purified to apparent homogeneity from the culture supernatant of Staphylotrichum coccosporum NBRC 31817. The molecular mass of STCE1 was 49 kDa. The optimum pH for the carboxymethyl cellulase activity of STCE1 was 6.0, and the optimum temperature was 60°C. STCE1 was highly resistant to an anionic surfactant and an oxidizing agent. Furthermore, the defibrillation activities on dyed cotton and lyocell fabrics of STCE1 were higher than those of the other representative endoglucanases tested. These results indicate that STCE1 is an all-purpose enzyme for laundry use. A gene encoding STCE1, designated the stce1 gene, was cloned from S. coccosporum, and the complete sequence was determined. STCE1 consisted of three distinct domains: an N-terminal catalytic domain (family 45), a linker domain, and a C-terminal carbohydrate-binding module (family 1). The amino acid sequences of the catalytic domain of STCE1 were phylogenetically close to those of the family 45 endoglucanases EGL3, EGL4, and EGV from a Humicola sp. Hence, the stce1 gene was transferred into Humicola insolens and expressed. As a result, extremely high levels (0.90 mg protein per ml of culture supernatant, 27% of the total proteins) of the recombinant STCE1 were secreted as a mature form in the culture supernatant.

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Section: Resultsmentioning

confidence: 99%

Purification and Characterization of a New Family 45 Endoglucanase, STCE1, from Staphylotrichum coccosporum and Its Overproduction in Humicola insolens

Koga

Baba

Shimonaka

et al. 2008

Appl Environ Microbiol

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“…As pointed out by these authors, research on alkaline and neutral cellulases is particularly important for the textile industry, since acid enzymes tend to cause indigo backstaining in denim treatment and increased fabric weakening. Baba et al (2005) reported a considerable resistance of the native H. grisea endoglucanases EGL3 and EGL4 to the surfactant sodium dodecyl benzene sulfonate, thus opening the possibility of employing these enzymes in detergent formulations. An additional study on H. grisea rCBH1.2 compatibility with anionic surfactants and oxidizing agents, the main components of detergents, will be necessary to evaluate its potential for laundry usage.…”

Section: Discussionmentioning

confidence: 99%

An alkaline thermostable recombinant Humicola grisea var. thermoidea cellobiohydrolase presents bifunctional (endo/exoglucanase) activity on cellulosic substrates

Oliveira

Ulhôa

Silveira

et al. 2012

World J Microbiol Biotechnol

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Humicola grisea var. thermoidea is a deuteromycete which secretes a large spectrum of hydrolytic enzymes when grown on lignocellulosic residues. This study focused on the heterologous expression and recombinant enzyme analysis of the major secreted cellulase when the fungus is grown on sugarcane bagasse as the sole carbon source. Cellobiohydrolase 1.2 (CBH 1.2) cDNA was cloned in Pichia pastoris under control of the AOX1 promoter. Recombinant protein (rCBH1.2) was efficiently produced and secreted as a functional enzyme, presenting a molecular mass of 47 kDa. Maximum enzyme production was achieved at 96 h, in culture medium supplemented with 1.34 % urea and 1 % yeast extract and upon induction with 1 % methanol. Recombinant enzyme exhibited optimum activity at 60 °C and pH 8, and presented a remarkable thermostability, particularly at alkaline pH. Activity was evaluated on different cellulosic substrates (carboxymethyl cellulose, filter paper, microcrystalline cellulose and 4-para-nitrophenyl β-D-glucopyranoside). Interestingly, rCBH1.2 presented both exoglucanase and endoglucanase activities and mechanical agitation increased substrate hydrolysis. Results indicate that rCBH1.2 is a potential biocatalyst for applications in the textile industry or detergent formulation.

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“…Después de una búsqueda exhaustiva no se encontraron reportes de B. portoricensis en los que se evaluó su efecto contra estos patógenos y tampoco de interacciones o de compuestos, únicamente se encontró el efecto antimicrobiano contra B. subtillis de la cepa Beltraniella humicola (Gajbhiye et al, 2013). Por otra parte, también se ha reportado que B. portoricensis podría ser de mucha utilidad en la industria de los detergentes (Baba et al, 2005).…”

Section: Especie Fúngica Fracciónunclassified

Actividad Antimicrobiana De Extractos Obtenidos De La Interacción Dual Entre Micromicetos Saprobios

Medina-Baizabal

Abarca

Gamboa‐Angulo

2022

Trop Subtrop Agroecosyst

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Background: Saprophytic micromycetes are recognized for their extraordinary ability to biosynthesize various metabolites with biological properties that can be modified when interacting with other organisms. Objective: To evaluate the antibacerial and antifungal activity of extracts obtained from dual interactions of Acremonium masseei CICY029 (Am), Beltraniella portoricensis MR42 (Bp), Cylindrium elongatum MR45 (Ce) y Stachybotrys sp. MR33 (Ssp) and to obtain the chemical profile of the most active interaction. Methodology: The ethyl acetate extracts of the four strains and their six dual interactions were evaluated against ten pathogens by the microdilution method to determine their antifungal and antibacterial capacity. The most active extracts were partitioned, and the minimum inhibitory concentration (MIC) o their fractions were determined. The chemical profile of the most active interaction was analyzed by gas chromatography coupled to mass spectrometry. Results: The highest mycelial growth inhibitory activity (MCI = 100%) was obtained from the fungal extracts of the single culture of Stachybotrys sp., and the dual Ce-Ssp interaction against Colletotrichum gloeosporioides, Mycosphaerella fijiensis at the concentration of 2000 µg/mL, as well as against Candida albicans and Xanthomonas campestris at 400 µg/mL. The acetonitrile fraction of Stachybotrys sp. showed high effectiveness against Alternaria tagetica, C. gloeosporioides, M. fijiensis and X. campestris (MIC ≤ 250 -1000 µg/mL). A mixture of fatty acids and three unidentified components not observed in the single cultures were detected by GC-MS in the Ce-Ssp extract. Implications: Biological interactions between two saprophytic fungi are a viable alternative for inducing the production of new metabolites with the potential to control pathogenic bacteria and fungi. Conclusions: The antifungal and antibacterial potential of saprophytic micromycetes can be improved in their dual interaction, particularly between C. elongatum MR45 and Stachybotrys sp. MR33, is a promising option for further investigation as potential natural antimicrobials.

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Purification and Characterization of a New Endo-1,4-β-D-glucanase fromBeltraniella portoricensis

Cited by 11 publications

References 14 publications

Purification and Characterization of a New Family 45 Endoglucanase, STCE1, from Staphylotrichum coccosporum and Its Overproduction in Humicola insolens

Purification and Characterization of a New Family 45 Endoglucanase, STCE1, from Staphylotrichum coccosporum and Its Overproduction in Humicola insolens

An alkaline thermostable recombinant Humicola grisea var. thermoidea cellobiohydrolase presents bifunctional (endo/exoglucanase) activity on cellulosic substrates

Actividad Antimicrobiana De Extractos Obtenidos De La Interacción Dual Entre Micromicetos Saprobios

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