Application of response surface methodology to evaluate the influence of temperature and initial pH on the production of β-1,3-glucanase and carboxymethylcellulase from Trichoderma harzianum

Théodore, K.; Panda, T.

doi:10.1016/0141-0229(94)00029-8

Cited by 33 publications

(18 citation statements)

References 16 publications

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“…Similar values have been reported, but the optimum temperature of M. perniciosa was lower when compared to most others (Nagata et al 1990, Fontaine et al 1997, Bara et al 2003, Marco and Felix 2007, and higher in relation to T. harzianum (Théodore and Panda 1995). Murray et al (2001) have also pointed out that the thermal stability of the T. emersonii enzyme is noteworthy because the estimated t 1/2 values at 70 • C and 80 • C were 136 min and 25 min, respectively, while 15% of the original activity remained after 15 min at 100 • C in the absence of substrate.…”

Section: Discussionsupporting

confidence: 73%

Production, purification and characterization of a thermostable β-1,3-glucanase (laminarinase) produced by Moniliophthora perniciosa

Sena

Valasques

Góes-Neto

et al. 2011

An. Acad. Bras. Ciênc.

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The enzyme glucanase from Moniliophthora perniciosa was produced in liquid medium and purified from the culture supernatant. A multivariate statistical approach (Response Surface Methodology -RSM) was employed to evaluate the effect of variables, including inducer (yeast extract) and fermentation time, on secreted glucanase activities M. perniciosa detected in the culture medium. The crude enzyme present in the supernatant was purified in two steps: precipitation with ammonium sulfate (70%) and gel filtration chromatography on Sephacryl S-200. The best inducer and fermentation time for glucanase activities were 5.9 g L −1 and 13 days, respectively. The results revealed three different isoforms (GLUI, GLUII and GLUIII) with purification factors of 4.33, 1.86 and 3.03, respectively. The partially purified enzymatic extract showed an optimum pH of 5.0 and an optimum temperature of 40 • C. The enzymatic activity increased in the presence of KCl at all concentrations studied. The glucanase activity was highest in the presence of 0.2 M NaCl. The enzyme showed high thermal stability, losing only 10.20% of its specific activity after 40 minutes of incubation at 90 • C. A purified enzyme with relatively good thermostability that is stable at low pH might be used in future industrial applications.

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Section: Discussionsupporting

confidence: 73%

Production, purification and characterization of a thermostable β-1,3-glucanase (laminarinase) produced by Moniliophthora perniciosa

Sena

Valasques

Góes-Neto

et al. 2011

An. Acad. Bras. Ciênc.

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“…For all procedures optimization the response surface methodology was used [16,18,19], which includes design of factorial experiments, development of models for the response surface estimation and model-based search of optimum point. Statistical models for approximation the desired response surfaces are developed using data of factorial experiments that were carried out according to close to D-optimal experimental designs n B [15; 20].…”

Section: Fig1 Complex Technological For Grease Wastes Utilization Dmentioning

confidence: 99%

Optimization of Complex Technology for Grease Wastes Utilization

Aikaitė-Stanaitienė

Matikevičienė

Levišauskas

et al. 2015

ETR

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IntroductionSustainable technologies promote the development of green techniques and products in order to live in clean and healthy environment. New effective waste recycling and recovery technologies are introduced. Our goal is to develop an effective and affordable complex-technology for recovery of fatty pollutants from meat, fish and oil processing enterprises. At the same time, it will reduce the quantity of biodegradable waste disposed in landfills. Lipids (characterized as oils, greases, fats and fatty acids) are one of the most important components of natural foods and many synthetic compounds and emulsions. Further, lipids constitute one of the major types of organic matter found in municipal wastewater [1]. The amount of lipid-rich wastewater increases every year due to urbanization and the development of factories. The incidence of grease in different businesses is quite considerable. These applies, for example, in slaughterhouses, sausage and meet product factories, restaurants, and fish processing plants, industrial undertakings in which oils and fats are processed and barrel-washing plants [2; 3]. Suspended lipids can be readily removed from wastewater by physical methods. Nevertheless, chemically and/or physically stabilized lipid/water emulsions should be managed in an appropriate manner. This is necessary because lipids that pass through physic-chemical treatment processes contribute to the levels of biological oxygen demand (BOD) and chemical oxygen demand (COD) in the effluents [4; 5; 6]. Many manufacturing, food processing and industrial facilities dispose of liquid waste into sewer lines. Liquid waste often contains grease and other organic contaminants which, over time, lead to clogs in pipes. The treatment of this problem is to clean pipes with caustic drain cleaners, mechanically rout the pipes or to replace the pipes completely. Even when grease-traps are included in a drainage system, the grease traps can form a permanent, solid grease layer over the top of the water which requires "pump-out" of the grease-trap [3; 7]. In other situations, liquid waste is disposed into septic tanks and drain-fields. High concentrations of FOG in the waste water can lead to grease build-up on rocks in the drain-field which eventually form a seal over the rocks 258

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“…Variables in coded levels β-(1→3)-Glucanase activity (U/ ml) influenced by the level of β-D-glucan present as inducer, and the types of glucosidic linkages present in the β-glucans used as carbon sources [21][22][23][24]. In a previous study, production of β-(1→3)-glucanases by T. harzianum Rifai grown on botryosphaeran (a (1→3)(1→6)-β-D-glucan from B. rhodina MAMB-05 [23] was optimized in shake-flasks.…”

Section: Experimental Runmentioning

confidence: 99%

Production of β-(1,3)-glucanases by Trichoderma harzianum Rifai: Optimization and Application to Produce Gluco-oligosaccharides from Paramylon and Pustulan

Giese¹,

Dekker

Barbosa-Dekker³

et al. 2012

Fermentat Technol

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Abstractβ-(1→3)-Glucanases were produced by Trichoderma harzianum Rifai PAMB-86 cultivated on botryosphaeran in a bench-fermenter and optimised by the response surface method. Maximal enzyme titres occurred at 5 days, initial pH 5.5 and aeration of 1.5vvm. β-(1→3)-The β-glucanolytic enzyme complex produced by T. harzianum Rifai PAMB-86 was fractionated by gel filtration into 2 fractions (F-I, F-II), and employed to produce gluco-oligosaccharides from algal paramylon ((1→3)-β-D-glucan) and lichen pustulan ((1→6)-β-D-glucan). Both enzymes attacked paramylon to the extent of ~15-20% in 30 min releasing glucose and laminaribiose as major end-products, and laminarioligosaccharides of degree of polymerization (DP) ≥3. Only F-I degraded pustulan resulting in ~2% degradation at 30 min, with glucose, gentiobiose and gentio-oligosaccharides of DP ≥4 as major products. The difference in the nature of the hydrolysis products can be explained by the substrate specificities of each enzyme fraction, and the structural differences of the β-D-glucans attacked.

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Application of response surface methodology to evaluate the influence of temperature and initial pH on the production of β-1,3-glucanase and carboxymethylcellulase from Trichoderma harzianum

Cited by 33 publications

References 16 publications

Production, purification and characterization of a thermostable β-1,3-glucanase (laminarinase) produced by Moniliophthora perniciosa

Production, purification and characterization of a thermostable β-1,3-glucanase (laminarinase) produced by Moniliophthora perniciosa

Optimization of Complex Technology for Grease Wastes Utilization

Production of β-(1,3)-glucanases by Trichoderma harzianum Rifai: Optimization and Application to Produce Gluco-oligosaccharides from Paramylon and Pustulan

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