Technical viability of the production, partial purification and characterisation of inulinase using pretreated agroindustrial residues

Treichel, Helen; Mazutti, Márcio A.; Filho, Francisco Maugeri; Rodrigues, Maria Isabel

doi:10.1007/s00449-008-0262-0

Cited by 37 publications

(26 citation statements)

References 25 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Deactivation energy E a(d) for glucoamylase calculated using an Arrhenius plot (Fig. 7) was found to be 74.85 kJ mol -1 , which was considerably lower than other reported enzymes [13]. The glucoamylase presented z value of 6.19, which indicates that to reduce 90 % of decimal reduction time, it is necessary to increase temperature by 6.19°C [26].…”

Section: Thermostability and Thermodynamics Of The Glucoamylasementioning

confidence: 75%

See 1 more Smart Citation

Kinetic and Thermodynamic Characterization of Glucoamylase from Colletotrichum sp. KCP1

2013

View full text Add to dashboard Cite

Extracellular glucoamylase of Colletotrichum sp. KCP1 produced through solid state fermentation was purified by two steps purification process comprising ammonium sulphate precipitation followed by gel permeation chromatography (GPC). The Recovery of glucoamylase after GPC was 50.40 % with 19.3-fold increase in specific activity. The molecular weight of enzyme was found to be 162.18 kDa by native-PAGE and was dimeric protein of two sub-units with molecular weight of 94.62 and 67.60 kDa as determined by SDS-PAGE. Activation energy for starch hydrolysis was 26.45 kJ mol -1 while temperature quotient (Q 10 ) was found to be 1.9. The enzyme was found to be stable over wide pH range and thermally stable at 40-50°C up to 120 min while exhibited maximum activity at 50°C with pH 5.0. The pKa 1 and pKa 2 of ionisable groups of active site controlling V max were 3.5 and 6.8, respectively. V max , K m and K cat for starch hydrolysis were found to be 58.82 U ml -1 , 1.17 mg (starch) ml -1 and 449 s -1 , respectively. Activation energy for irreversible inactivation (E a(d) ) of glucoamylase was 74.85 kJ mol -1 . Thermodynamic parameters of irreversible inactivation of glucoamylase and starch hydrolysis were also determined.

show abstract

Section: Thermostability and Thermodynamics Of The Glucoamylasementioning

confidence: 75%

“…Decimal reduction time, is defined as the time needed for reduction of 90 % of initial activity while z value represents the increase of temperature required to reduce 90 % of decimal reduction time [12,13].…”

Section: Thermal Inactivation and Thermodynamics Of Enzyme Activitymentioning

confidence: 99%

Kinetic and Thermodynamic Characterization of Glucoamylase from Colletotrichum sp. KCP1

2013

View full text Add to dashboard Cite

show abstract

“…Corn steep liquor and molasses had been pretreated using active carbon separately. The fermentations were started with 10% (V/V) inoculum at initial pH 5.0 (no pH control) and 36°C for 72 h according to a previous work by our research group [15]. A pitchedup blade impeller was used for agitation.…”

Section: Bioreactormentioning

confidence: 99%

Use of a sequential strategy of experimental design to optimize the inulinase production in a batch bioreactor

Treichel

Mazutti

Maugeri

et al. 2009

J Ind Microbiol Biotechnol

Self Cite

View full text Add to dashboard Cite

A potential application of inulinase in the food industry is the production of fructoligosaccharides (FOS) by the transfructosilation of sucrose. The FOSs present many interesting functional properties besides their ability to increase the shelf-life and flavor of many products. The use of an industrial medium represents a good alternative to producing inulinase at low cost, since the activity may improve, or at least remain the same, as that obtained using a synthetic medium. This work was an optimization study of the inulinase production by Kluyveromyces marxianus NRRL Y-7571 using industrial pre-treated culture medium in a bioreactor employing a sequential strategy of experimental design. Initially, a Plackett-Burman (Screening Design) design was used, where the studied variables were molasses, corn steep liquor, yeast extract concentration, and agitation and aeration rates. After the analysis of the effects, a central composite rotational design (CCRD) was carried out. The optimized condition for the inulinase production was: 250 g/l of molasses, 80 g/l of corn steep liquor, 6 g/l of yeast extract, 300 rpm of agitation and 1.5 vvm aeration rate, which resulted in an enzymatic activity of 1,317 +/- 65 U/ml.

show abstract

“…So far, many moulds and yeasts were tested for inulinases production and some of them could produce high inulinase activity. Among them, Kluyveromyces marxianus Kalil et al, 2001;Kushi et al, 2000;Mazutti et al, 2007;Singh et al, 2006;Treichel et al, 2009), Pichia guilliermondii Yu et al, 2009), Cryptococcus aureus (Sheng et al, 2008), Candida kefyr (Pessoa et al, 1998), some yeast strains isolated from marine microbiota (Gao et al, 2007), Aspergillus ficuum (Chen et al, 2011), Aspergillus niger (Kango, 2008;Kumar et al, 2005), Pseudomonas spp. (Kim et al, 1997), Arthrobacter spp.…”

Section: Introductionmentioning

confidence: 99%

Screening of Biotechnological Parameters for Fructofuranosidases Production by a Newly Isolated Fungal Strain Using Plackett-Burman Design

Bonciu

Constantin

Bahrim³

2011

Not Bot Hort Agrobot Cluj

View full text Add to dashboard Cite

Previously some fungal strains with good inulinase potential biosynthesis were screening and the most performing strain is the newly fungal strain, Rhizoctonia spp. coded I-PN4. In this study, the Plackett Burman design was used to identify the effect of process parameters upon fructofuranosidases (inulinase and invertase) production with new selected fungal strain. The agitation rate, yeast extract, buckwheat flour and K 2 HPO 4 concentration from fermentative medium composition, were determined as the most influential variables that have positive effects on fructofuranosidases biosynthesis. Temperature has a negative effect on both invertase and inulinase biosynthesis yield. In optimal established fermentative conditions, the maximum yields for extracellular inulinase was 6.2198 UI and 4.7664 UI for invertase respectively. The linear model fits well for variable screening and is globally significant, as R 2 is 88.36% for inulinase production and 84.24% for invertase production respectively.

show abstract

Technical viability of the production, partial purification and characterisation of inulinase using pretreated agroindustrial residues

Cited by 37 publications

References 25 publications

Kinetic and Thermodynamic Characterization of Glucoamylase from Colletotrichum sp. KCP1

Kinetic and Thermodynamic Characterization of Glucoamylase from Colletotrichum sp. KCP1

Use of a sequential strategy of experimental design to optimize the inulinase production in a batch bioreactor

Screening of Biotechnological Parameters for Fructofuranosidases Production by a Newly Isolated Fungal Strain Using Plackett-Burman Design

Contact Info

Product

Resources

About