Comparative study for obtaining inulinase and invertase by yeasts (original) (raw)
Related papers
Inulinase Production from Plant Materials by some Local Yeast Strains
Journal of Agricultural Chemistry and Biotechnology, 2020
Four inulinolytic yeast isolates were isolated and identified by molecular methods. They were belonged to Candida catenulata, Sarocladium kiliense, Galactomyces candidum and Scopulariopsis brevicaulis. The production of inulinase by the previous isolates through, 72h was done on two media using jerusalem artichoke tubers, garlic bulbs, dahlia tubers and chicory roots as natural sources of inulin. The highest values of the produced inulinase were obtained on Bharathi et al. (2011) medium after 48h of incubation. Jerusalem artichoke proved to be the best inulin source for enzyme production by Scopulariopsis brevicaulis (38.22 µg/ml), followed by dahlia (32.45 µg/ml). The best substrate for inulinase production by Sarocladium kiliense was dahlia (29.21 µg/ml) followed by garlic (28.65 µg/ml). As for Galactomyces candidum the maximum enzyme production was obtained using jerusalem artichoke (34.96 µg/ml) followed by garlic (31.84 µg/ml). The best material for inulinase production by Candida catenulate (34.15 µg/ml) was dahlia, followed by garlic (31.40 µg/ml). It can be concluded that inulin containing plant materials could be employed as a carbon source for inulinase production, it offer advantage in comparison to purified substrate because it have low cost and high productivity.
Parameters Optimization for Increased Intracellular Inulinase Activity of a Yeast Strain
Ecological Engineering and Environment Protection
This study reveals the selection of a yeast strain, possessing inulinase activity and finding the optimal conditions of cultivation. Intra- and extracellular activity assay was performed after cultivation on media, containing inulin as a sole source of carbon. Optimization of the cultivation conditions was carried out for establishing the favorable conditions for biosynthesis of inulinase. Modifying the physicochemical and nutritional parameters of a cultivation process lead to major improvement of the enzyme activity. Highest intra- and extracellular inulinase activity was registered when 1.5% inulin was used, 5 % inoculum, temperature 28°C, pH=6.5 and agitation of 200rpm. The selected strain Kluyveromyces sp. C showed higher values for the intracellular inulinase activity, making it suitable for immobilization and further use. Key words: Kluyveromyces sp., inulinase activity, parameters optimization
Use ofK L a as a criterion for scaling up the inulinase fermentation process
Applied Biochemistry and Biotechnology, 1996
The scale-up of inulinase production in aerated cultures of Candida kefyr DSM 70106 was studied, taking into account the criterion of maintaining Kaa constant. The culture was carried out batchwise, in a 15-L fermentor, with Kaa varying from 25 to 199 h -1. The highest inulinase production was attained with an initial Kaa value of 46 h -1. A large scale fermentation (300-L fermentor) was performed using identical culture medium conditions. The responses obtained for the bench and scaled-up experiments showed similar behaviors, and the results were, respectively, 0.60 and 0.58 U-mL -1.h -~ for productivity and 43.0 and 41.5 U.mL -~ for activities.
International Journal of Biochemistry and Biophysics, 2013
A Saccharomyces cerevisiae MK was isolated from toddy sample. The effect of different production parameters such as pH, temperature, incubation time, carbon source, nitrogen source (organic and inorganic), inoculum concentrations, sucrose concentrations, metal ions, surfactants, amino acids, buffers, agricultural residues and agricultural residue concentration on invertase production by the isolated Saccharomyces cerevisiae MK strain were studied. The enzyme production was assayed in submerged fermentation (SmF). Maximum invertase activity was found at pH 6, 30°C, 48 hours, sucrose, yeast extract (organic nitrogen), ammonium chloride (inorganic nitrogen), 2% inoculum concentration, 2% sucrose concentration, calcium chloride, poly ethylene glycol, methionine, citrate buffer, orange peel-4%. A higher titre of invertase enzyme activity (0.48 ± 0.011 IU/ml) was obtained in the optimized production medium.
World Journal of Microbiology & Biotechnology, 2005
Invertase (β-D-fructofuranoside fructohydrolase, EC 3.2.1.26) finds major uses in confectionery and in the production of invert syrup. In the present study, we report on invertase production by wild cultures of Saccharomyces cerevisiae. The yeast strains were isolated from dates available in a local market. Five hyperproducing yeast strains (>100- fold higher invertase activity) were kinetically analysed for invertase production. Saccharomyces cerevisiae strain GCA-II was found to be a better invertase-yielding strain than all the other isolates. The values of Q p and Y p/s for GCA-II were economical as compared to other Saccharomyces cultures. The effect of sucrose concentration, rate of invertase synthesis, initial pH of fermentation medium and different organic nitrogen sources on the production of invertase under submerged culture conditions was investigated. Optimum concentrations of sucrose, urea and pH were 3, 0.2 (w/v), and 6 respectively. The increase in the enzyme yield obtained after optimization of the cultural conditions was 47.7%.
Microbial Inulinases: Fermentation Process, Properties, and Applications
Advances in Applied Microbiology, 1983
which can be used to synthesize useful compounds; others which can stereospecifically carry out important bioconversion reactions; and some which are able to hydrolyze polymers into interesting monomers. All these reactions can be performed under mild operating conditions with renewable resources as substrates (Rose, 1980). The microbial enzyme, inulinase, hydrolyzes the plant polymer inulin into practically pure fructose. Inulin accumulates as a reserve polymer in several interesting agricultural crops such as Jerusalem artichoke, chicory, scorzonera, dahlia, and several others. As such, inulinase offers interesting perspectives in view of the growing need for production of pure fructose syrups or may present an alternative way to produce the so-called "Ultra High Fructose Glucose Syrups" (UHFGS)not from starch, but from inulin. Conventional fructose production from starch needs at least three enzymatic steps, including a-amylase, amyloglucosidase, and glucose isomerase action, yielding only ? 45% fructose solutions at the best. Fructose formation from inulin is a single enzymatic step reaction and yields are up to 95% fructose. Indeed, fructose emerges more and more as a safe and alternative sweetener to sucrose, which causes problems related to corpulence, cariogenicity, atherosclerosis, and diabetes. Furthermore, fructose is more soluble than sucrose, displays a greater sweetening power, and can mask the bitter aftertaste of saccharin. Chemical acid hydrolysis of inulin to fructose displays several drawbacks; this has also forced interest toward the microbial inulinase enzyme and its applications. Another timely application of inulinase consists of the direct fermentation of inulin into ethanol with inulinase-producing yeasts. 11. History Lindner had already observed by 1900 that the yeast Saccharomyces mumianus, as well as a few unidentified yeast strains, were able to utilize inulin. Elaborations on these observations were reported by Grafe and Vouk (1913) and by Kluyver (1914), and Sacchetti (1933) unequivocally proved that Kluyveromyces fragilis grows at the expense of inulin. As for the molds, Aspergillus niger inulinase was first described in 1924 by Pringsheim and Kohn. Weidenhagen (1932) defended the opinion that a single enzyme-a pfructofuranosidase from yeast-hydrolyzed sucrose, inulin, rainose, irisine, gentianose, and stachyose. It was further claimed that only autolyzed yeast cells displayed inulinase activity. Until then, the existence of a true inulinase enzyme was strongly in doubt. Some years later, Adams et al. (1943) showed that even purified invertases from different yeast strains displayed varying inulinase activity depending upon the strain involved; it also became apparent that inulinase activity displayed a pH and temperature optimum quite
Inulinase production by Saccharomyces sp. in solid state fermentation using wheat bran as substrate
Annals of Microbiology
A newly isolated inulinase-producing Saccharomyces sp. from spontaneously fermented sugar cane was employed for inulinase production in solid state fermentation. All the substrates used—wheat bran, rice bran, banana peel, orange peel and bagasse—supported inulinase production. However, the highest inulinase production (78.29 ± 0.13 U/g ds, units per gram of dry substrate) was recorded with wheat bran, while orange bagasse gave the lowest inulinase production (22.47 ± 0.01 U/g ds). A time course of inulinase production revealed that maximum inulinase production of 90.15 U/g ds was reached at 72 h of fermentation. A 24-h-old inoculum and an inoculum density of 4% was also found to be optimal, yielding inulinase production of 88.5 ± 0.02 U/g ds and 80.9 ± 0.25 U/g ds, respectively, by the Saccharomyces sp. Furthermore, a moisture content of 65% was found to support maximum inulinase production of 81.5 ± 0.02 U/g ds. pH and temperature studies showed pH 5.5 and 35°C to be optimum for inulinase production of 91.0 ± 0.60 U/g ds and 89.5 ± 0.06 U/g ds, respectively, by this Saccharomyces sp.
The ability of yeast to secrete intracellular and extracellular forms of invertase has been demonstrated by studies, however not much research has focused on intracellular invertase. Here we report the biochemical and chromatographic properties of intracellular invertase from invertase hyperproducer obtained from Abagboro village, Ile-Ife, Nigeria and compared it with that from a brewery which had been commercially selected. Saccharomyces cerevisiae and Saccharomyces carlsbergensis were isolated from fresh palm wine obtained from Abagboro village, Ile-Ife and from green beer obtained from a local brewery, respectively. Isolates were grown on liquefied cassava-soy bean mash for 72 hours. Yeast biomass harvested was homogenized to obtain crude intracellular invertase and purified by chromatographic techniques. Physicochemical properties and kinetic parameters (Km and Vmax) of the enzymes was studied. Native and subunit molecular weights of purified invertase from an hyperproducer (Sac...
Isolation Screening and Optimization of Invertase Production under Submerged Fermentation
Invertase producing 17 isolates of yeast were isolated and characterized from different sample of fruits in which isolate R5 give maximum invertase production. The enzyme activity reached to maximum when incubation time was 48 hrs, and pH 5. Different Carbon and Nitrogen source were investigated for the enzyme production and sucrose and yeast extract was found to be best Carbon and Nitrogen source for invertase production. Incubation temperature 30ºC, inoculum size 5%, were found to be optimum temperature and inoculam size for invertase production.
Food and Bioprocess …, 2009
In this work, production of inulinase was studied. Media formulation was optimized by experimental design and response surface techniques, as well as the pretreatment of the agro-industry residues used in the formulation of fermentation medium. Two agro-industry residues were investigated: sugarcane molasses (SCM) and corn steep liquor (CSL). Pretreatment with sulfuric acid was the most effective for clarification of SCM (pH 5.0, 24 h of resting time and final pH 4.0). Clarification of CSL was accomplished with phosphoric acid (pH 3.0, 24 h of resting time and final pH 5.5). A color reduction of approximately 70% was achieved for both substrates. The highest production of inulinase was obtained in a medium containing 100 g l −1 of pretreated SCM, 100 g l −1 of pretreated CSL and 6 g l −1 of Prodex Lac (yeast hydrolysate), yielding 1,139 U ml −1 .