Optimization for coproduction of protease and cellulase from Bacillus subtilis M-11 by the Box–Behnken design and their detergent compatibility

Yazici, Sercan Özbek; Özmen, İsmail

doi:10.1007/s43153-020-00025-x

Cited by 17 publications

(7 citation statements)

References 29 publications

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“…Furthermore, the enzyme's structure and activity remain intact, ensuring optimal performance [ 12 ]. In a similar study, the maximum cellulase production using B. subtilis strain M-11 was achieved at a temperature of 42°C [ 12 , 33 ]. In contrast, the maximum cellulase production was obtained using Bacillus sp.…”

Section: Resultsmentioning

confidence: 99%

Synthesis, Optimization, and Characterization of Cellulase Enzyme Obtained from Thermotolerant Bacillus subtilis F3: An Insight into Cotton Fabric Polishing Activity

Fouda,

Alshallash,

Atta

et al. 2023

J. Microbiol. Biotechnol.

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The efficacy of 40 bacterial isolates obtained from hot spring water samples to produce cellulase enzymes was investigated. As a result, the strain Bacillus subtilis F3, which was identified using traditional and molecular methods, was selected as the most potent for cellulase production. Optimization was carried out using one-factor-at-a-time (OFAT) and BOX-Behnken Design to detect the best conditions for the highest cellulase activity. This was accomplished after an incubation period of 24 h at 45°C and pH 8, with an inoculum size of 1% (v/v), 5 g/l of peptone as nitrogen source, and 7.5 g/l of CMC. Moreover, the best concentration of ammonium sulfate for cellulase enzyme precipitation was 60% followed by purification using a dialysis bag and Sephadex G-100 column chromatography to collect the purified enzyme. The purified cellulase enzyme was characterized by 5.39-fold enrichment, with a specific activity of 54.20 U/mg and a molecular weight of 439 kDa. There were 15 amino acids involved in the purified cellulase, with high concentrations of 160 and 100 mg/l for glycine and proline respectively. The highest stability and activity of the purified cellulase was attained at pH 7 and 50°C in the presence of 150 ppm of CaCl 2 , NaCl, and ZnO metal ions. Finally, the biopolishing activity of the cellulase enzyme, as indicated by weight loss percentages of the cotton fabric, was dependent on concentration and treatment time. Overall, the thermotolerant B. subtilis F3 strain has the potential to provide highly stable and highly active cellulase enzyme for use in biopolishing of cotton fabrics.

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Section: Resultsmentioning

confidence: 99%

Synthesis, Optimization, and Characterization of Cellulase Enzyme Obtained from Thermotolerant Bacillus subtilis F3: An Insight into Cotton Fabric Polishing Activity

Fouda,

Alshallash,

Atta

et al. 2023

J. Microbiol. Biotechnol.

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“…Bacterial CMCase with high stability in detergents are reported from Bacillus sp. SMIA‐2 [22], Bacillus subtilis M‐11 [23], and Streptomyces drozdowiczii [46]. The CELs activities of strain VP111 were retained in presence of denaturant urea, which possibly indicates lack of much weak interactions in the active sites.…”

Section: Discussionmentioning

confidence: 99%

“…Therefore, tolerance to product inhibition is another aspired character for CELs, particularly in plant biomass saccharification [20]. However, at present the CELs with halo‐tolerance, alkaline‐tolerance, thermo‐tolerance, organic solvent‐tolerance, and end product‐tolerance are prominently recognized from the species of Bacillus [21–25], rather than any Actinobacteria.…”

Section: Introductionmentioning

confidence: 99%

Multipurpose cellulases of Promicromonospora sp. VP111, with broad substrate specificity and tolerance properties

2023

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Cellulolytic actinobacterium, Promicromonospora sp. VP111 concomitantly produced cellulases (CELs), xylanase and pectinase when grown on commercial cellulose and untreated agricultural lignocellulosic residues (wheat straw and sugarcane bagasse). Secreted CELs hydrolyzed (enhanced with Co 2+ ion) multiple cellulosic substrates, including sodium carboxymethyl cellulose (Na-CMC), Whatman filter paper no. 1, microcrystalline cellulose (avicel), p-nitrophenyl-β-D-glucopyranoside (pNPG), laminarin, and cellulose powder. The CELs showed stabilities in the presence of various chemicals, including glucose (0.2 M), detergents (1%, w/v or v/v), denaturants (1%, w/v or v/v), and sodium chloride (NaCl, 30%, w/v). The CELs were fractionated using ammonium sulfate precipitation and dialysis. Activities (%) of fractionated CELs were retained at 60°C for endoglucanase/carboxymethyl cellulase (CMCase) (88.38), filter paper cellulase (FPase) (77.55), and β-glucosidase (90.52), which indicated of thermo-stability. Similarly, the activities (%) for CMCase (85.79), FPase (82.48), and β-glucosidase (85.92) at pH 8.5 indicated of alkaline-stability. Kinetic factors, K m and V max for endoglucanase component of fractionated CELs were 0.014 g/l and 158.23 µM glucose/min/mL, respectively. Fractionated CELs yielded activation energies (kJ/mol) of 17.933, 6.294, and 4.207 for CMCase, FPase, and β-glucosidase activities, respectively in linear thermostable Arrhenius plots. Thus, this study reports on the multipurpose CELs from an untreated agricultural residue utilizing Promicromonospora in relation to broad substrate specificity, halo-tolerance,

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“…As these enzymes are used together not only in detergent industries, these are used together in the food and pharmaceutical industries too. Coproduction of cocktail enzymes is one way to reduce the cost of production and these approaches were found to be practical by other researchers [ 4 , 7 , 43 ].…”

Section: Discussionmentioning

confidence: 99%

“…Enzymes with a variety of applications in the detergent industry, food industry, feed industry, pharmaceutical industry, leather industry, peptide synthesis, and recovery of silver from used X-ray films are developed [ 2 ]. Among these, detergent industries are the primary consumers of enzymes, in terms of both volume and value [ 3 ], consuming about 60% of all the enzymes produced [ 4 ]. Among hydrolytic enzymes, microbial alkaline protease dominates commercial applications with a significant share of the market captured by subtilisins and/or alkaline protease from Bacillus spp.…”

Section: Introductionmentioning

confidence: 99%

Screening and Identification of Thermotolerant and Osmotolerant Bacillus amyloliquefaciens BKHE Isolated from Kinema of Eastern Nepal for Alkaline Protease Production

Pandey¹,

Shrestha²,

Karki

et al. 2022

International Journal of Microbiology

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Alkaline protease is one of the most important industrial enzymes which are excessively used in the detergent industry, food industry, feed industry, pharmaceutical industry, leather industry, etc. 60% of the produced alkaline protease is consumed by the detergent industry alone. In the present study, bacterial isolates that can produce alkaline protease for purpose of bio-detergent were screened among the isolates isolated from kinema (an alkaline fermented food of eastern Nepal). Selected bacterial isolates were further screened for hemolysis activity and the production of other hydrolytic enzymes. Four bacterial isolates selected were tested for their capacity to produce alkaline protease in five different fermentation mediums. Isolate BKHE produces a high amount of alkaline protease (0.4705 ± 0.035 U/mL/min) in fermentation medium M2 (sucrose, 11 g/L; yeast extract, 5 g/L; and KNO3, 5.2 g/l, pH 9). The selected isolate was identified as Bacillus amyloliquefaciens BKHE based on 16S rRNA sequencing and phenotypic features. This bacterial strain was also found to be thermotolerant (confluent growth at 50°C) and salt tolerant up to 10% NaCl concentration. With its versatile ability, bacterial isolate or purified enzymes have potential applications in the food and detergent industry.

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Optimization for coproduction of protease and cellulase from Bacillus subtilis M-11 by the Box–Behnken design and their detergent compatibility

Cited by 17 publications

References 29 publications

Synthesis, Optimization, and Characterization of Cellulase Enzyme Obtained from Thermotolerant Bacillus subtilis F3: An Insight into Cotton Fabric Polishing Activity

Synthesis, Optimization, and Characterization of Cellulase Enzyme Obtained from Thermotolerant Bacillus subtilis F3: An Insight into Cotton Fabric Polishing Activity

Multipurpose cellulases of Promicromonospora sp. VP111, with broad substrate specificity and tolerance properties

Screening and Identification of Thermotolerant and Osmotolerant Bacillus amyloliquefaciens BKHE Isolated from Kinema of Eastern Nepal for Alkaline Protease Production

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