scholarly journals β-Galactosidase-Producing Isolates in Mucoromycota: Screening, Enzyme Production, and Applications for Functional Oligosaccharide Synthesis

2021 ◽  
Vol 7 (3) ◽  
pp. 229
Author(s):  
Bettina Volford ◽  
Mónika Varga ◽  
András Szekeres ◽  
Alexandra Kotogán ◽  
Gábor Nagy ◽  
...  
Keyword(s):  
Wheat Bran ◽  
Enzyme Production ◽  
Specific Activity ◽  
Prebiotic Synthesis ◽  
Crude Enzyme ◽  
Oligosaccharide Synthesis ◽  
Industrial Enzymes ◽  
Chromogenic Agar ◽  
Lichtheimia Ramosa ◽  
Excellent Source

β-Galactosidases of Mucoromycota are rarely studied, although this group of filamentous fungi is an excellent source of many industrial enzymes. In this study, 99 isolates from the genera Lichtheimia, Mortierella, Mucor, Rhizomucor, Rhizopus and Umbelopsis, were screened for their β-galactosidase activity using a chromogenic agar approach. Ten isolates from the best producers were selected, and the activity was further investigated in submerged (SmF) and solid-state (SSF) fermentation systems containing lactose and/or wheat bran substrates as enzyme production inducers. Wheat bran proved to be efficient for the enzyme production under both SmF and SSF conditions, giving maximum specific activity yields from 32 to 12,064 U/mg protein and from 783 to 22,720 U/mg protein, respectively. Oligosaccharide synthesis tests revealed the suitability of crude β-galactosidases from Lichtheimia ramosa Szeged Microbiological Collection (SZMC) 11360 and Rhizomucor pusillus SZMC 11025 to catalyze transgalactosylation reactions. In addition, the crude enzyme extracts had transfructosylation activity, resulting in the formation of fructo-oligosaccharide molecules in a sucrose-containing environment. The maximal oligosaccharide concentration varied between 0.0158 and 2.236 g/L depending on the crude enzyme and the initial material. Some oligosaccharide-enriched mixtures supported the growth of probiotics, indicating the potential of the studied enzyme extracts in future prebiotic synthesis processes.

scholarly journals Production of ethanol and clarification of apple juice by pectinase enzyme produced from Aspergillus terreus NCFT 4269.10

2016 ◽  
Vol 4 (1) ◽  
pp. 67 ◽  
Author(s):  
Bijay Sethi ◽  
Amrita Satpathy ◽  
Subodh Tripathy ◽  
Sidarth Parida ◽  
Sameer Kumar Singdevsachan ◽  
...  
Keyword(s):  
Solid State ◽  
Wheat Bran ◽  
Solid State Fermentation ◽  
Apple Juice ◽  
Aspergillus Terreus ◽  
Specific Activity ◽  
Sole Source ◽  
Crude Enzyme ◽  
Maximum Production ◽  
Pectinase Production

Aspergillus terreus NCFT 4269.10 was evaluated by liquid static surface fermentation (LSSF), shaking fermentation (ShF) and solid state fermentation (SSF) for the production of pectinase. Among various substrates tested, banana peels supported maximum production of pectinase i.e. 1000 ± 141.42 U/ml. The biomass of A. terreus was maximum with wheat bran (0.55±0.07g/50ml). Pectinase produced by A. terreus displayed higher specific activity when wheat bran was used as the sole source of carbon and energy. After successful fermentation, crude enzyme was purified to electrophoretic homogeneity with a specific activity of 1846.50 U/mg from an initial specific activity of 1282.05 U/mg. The cell free-dialyzed-enzyme containing 107100 U was purified to 1.44 fold with an overall enzyme yield of 35.70%.Immobilization study revealed that the production of pectinase was increased up to third cycle and decreased thereafter when further pectinase production was carried out by immobilized spores of A. terreus.

Production and Properties of a Bacterial Thermostable Exo-inulinase

2001 ◽  
Vol 56 (11-12) ◽  
pp. 1022-1028 ◽  
Author(s):  
Kristina Uzunova ◽  
Anna Vassileva ◽  
Margarita Kambourova ◽  
Viara Ivanova ◽  
Dimitrina Spasova ◽  
...  
Keyword(s):  
Enzyme Production ◽  
Enzyme Preparation ◽  
Batch Cultivation ◽  
Crude Enzyme ◽  
Growth Time ◽  
Bacillus Sp ◽  
High Thermostability ◽  
Crude Enzyme Preparation ◽  
Ph Range

Abstract Enzyme production of newly isolated thermophilic inulin-degrading Bacillus sp. 11 strain was studied by batch cultivation in a fermentor. The achieved inulinase and invertase activi­ ties after a short growth time (4.25 h) were similar or higher compared to those reported for other mesophilic aerobic or anaerobic thermophilic bacterial producers and yeasts. The investigated enzyme belonged to the exo-type inulinases and splitted-off inulin, sucrose and raffinose. It could be used at temperatures above 65 °C and pH range 5.5-7.5. The obtained crude enzyme preparation possessed high thermostability. The residual inulinase and inver­ tase activities were 92-98% after pretreatment at 65 °C for 60 min in the presence of substrate inulin.

scholarly journals Comparative Evaluation of Agroindustrial Byproducts for the Production of Alkaline Protease by Wild and Mutant Strains ofBacillus subtilisin Submerged and Solid State Fermentation

2013 ◽  
Vol 2013 ◽  
pp. 1-6 ◽  
Author(s):  
Hamid Mukhtar ◽  
Ikramul Haq
Keyword(s):  
Bacillus Subtilis ◽  
Solid State ◽  
Wheat Bran ◽  
Solid State Fermentation ◽  
Soybean Meal ◽  
Alkaline Protease ◽  
Enzyme Production ◽  
Enhanced Production ◽  
Industrial Byproducts ◽  
Agroindustrial Byproducts

The present study describes the screening of different agroindustrial byproducts for enhanced production of alkaline protease by a wild and EMS induced mutant strain ofBacillus subtilisIH-72EMS8. During submerged fermentation, different agro-industrial byproducts were tested which include defatted seed meals of rape, guar, sunflower, gluten, cotton, soybean, and gram. In addition to these meals, rice bran, wheat bran, and wheat flour were also evaluated for protease production. Of all the byproducts tested, soybean meal at a concentration of 20 g/L gave maximum production of the enzyme, that is, 5.74  ±  0.26 U/mL from wild and 11.28  ±  0.45 U/mL from mutant strain, during submerged fermentation. Different mesh sizes (coarse, medium, and fine) of the soybean meal were also evaluated, and a finely ground soybean meal (fine mesh) was found to be the best. In addition to the defatted seed meals, their alkali extracts were also tested for the production of alkaline protease byBacillus subtilis, but these were proved nonsignificant for enhanced production of the enzyme. The production of the enzyme was also studied in solid state fermentation, and different agro-industrial byproducts were also evaluated for enzyme production. Wheat bran partially replaced with guar meal was found as the best substrate for maximum enzyme production under solid state fermentation conditions.

scholarly journals Extraction and purification of L-Asparaginase II from local isolate of Proteus vulgaris

2011 ◽  
Vol 8 (1) ◽  
pp. 509-518
Author(s):  
Baghdad Science Journal
Keyword(s):  
Enzyme Production ◽  
Quantitative Methods ◽  
Specific Activity ◽  
Deae Cellulose ◽  
Ion Exchanger ◽  
Optimum Conditions ◽  
Proteus Vulgaris ◽  
Clinical Specimens ◽  
Extraction And Purification ◽  
High Level

Forty one isolates of genus Proteus were collected from 140 clinical specimens such as urine, stool, wound, burn, and ear swabs from patients of both sex. These isolates were identified to three Proteus spp. P. mirabilis, P. vulgaris and P. penneri .The ability of these bacteria to produce L-asparaginase II by using semi quantitative and quantitative methods was determined. P. vulgaris Pv.U.92 was distinguished for high level of L-asparaginase II production with specific activity 1.97 U/mg. Optimum conditions for enzyme production were determined; D medium with 0.3% of L-asparagine at pH 7.5 with temperature degree 35°C for incubation. Ultrasonication was used to destroy the P. vulgaris Pv.U.92 cells then ASNase II was extracted and purified throughout several purification steps including precipitation with (NH4)2SO4(60-80%), DEAE-cellulose ion exchanger chromatography followed by Sephacryl S-300 filtration. The specific activity was 155.6 U/ mg and the purification fold was 27.3 with 10.4% yield.

scholarly journals Production and partial characterization of a crude cold-active cellulase (CMCase) from Bacillus mycoides AR20-61 isolated from an Alpine forest site

2020 ◽  
Vol 70 (1) ◽  
Author(s):  
Elisa Steiner ◽  
Rosa Margesin
Keyword(s):  
Enzyme Activity ◽  
Bacterial Growth ◽  
Enzyme Production ◽  
Crude Enzyme ◽  
Cultivation Temperature ◽  
Bacillus Mycoides ◽  
Temperature Range ◽  
Alpine Forest ◽  
Cold Active ◽  
Ph Range

Abstract Purpose To evaluate the production of a cold-active CMCase (endoglucanase) by Bacillus mycoides AR20-61 isolated from Alpine forest soil and to characterize the crude enzyme. Methods After studying the effect of cultivation parameters (medium composition, temperature, NaCl concentration, pH) on bacterial growth and enzyme production, the crude enzyme was characterized with regard to the effect of pH, temperature, and inhibitors on enzyme activity and stability. Result Optimum growth and enzyme production occurred at 20–25 °C, pH 7, and 1–1.5% (w/v) CMC. Despite high biomass production over the whole growth temperature range (10–35 °C), enzyme production was low at 10 and 35 °C. CMC concentration had a minor effect on growth, independent of the growth temperature, but a significant effect on CMCase production at temperatures ≥ 20 °C. The crude enzyme was active over a broad temperature range (0–60 °C); the apparent optimum temperature for activity was at 40–50 °C. The cultivation temperature influenced the effect of temperature on enzyme activity and stability. A significantly higher thermosensitivity of the enzyme produced at a cultivation temperature of 10 °C compared to that produced at 25 °C was noted at 50 and 65 °C. The enzyme was highly active over a pH range of 4–6 and showed optimum activity at pH 5. No activity was lost after 60 min of incubation at 30 °C and pH 4–9. The CMCase was resistant against a number of monovalent and divalent metal ions, metal-chelating agents, and phenol. Conclusion The CMCase produced by the studied strain is characterized by high activities in the low temperature range (down to 0 °C) and acidic pH range, high stability over a broad pH range, and high resistance against a number of effectors. Our results also demonstrate the different, independent roles of temperature in bacterial growth, enzyme production, nutrient requirements during enzyme production, and enzyme characteristics regarding thermosensitivity, which has not yet been described for cellulases.

ENZYMIC DEGRADATION OF WHEAT BRAN TO IMPROVE ITS NUTRITIONAL VALUE FOR MONOGASTRICS

1969 ◽  
Vol 49 (2) ◽  
pp. 205-214 ◽  
Author(s):  
T. S. Neudoerffer ◽  
R. E. Smith
Keyword(s):  
Wheat Bran ◽  
Nutritional Value ◽  
Enzyme Preparation ◽  
Proteolytic Enzymes ◽  
Protein Digestibility ◽  
Reducing Sugar ◽  
Metabolizable Energy ◽  
Crude Enzyme ◽  
Sugar Accumulation ◽  
Crude Enzyme Preparation

The enzymic degradation of wheat bran using cellulolytic and proteolytic enzymes from a number of sources was investigated. Two enzyme combinations were found to be effective for the chemical alteration of wheat bran. Crude enzyme preparation from the fungus T. viride in combination with a commercial proteinase brought about a 32% reducing sugar accumulation, a 36% loss of holocellulose, a 40% loss of α-cellulose and a, 54% solubilization of protein. Crude enzyme preparation from the fungus M. verrucaria in combination with a commercial proteinase gave rise to a 27% reducing sugar accumulation, a 39% loss of holocellulose, a 22% loss of α-cellulose and 50% solubilization of protein. The nutritional value for the rat of wheat bran modified by either enzyme combination was significantly improved. Apparent protein digestibility was improved significantly. Preliminary experiments indicate that the modification of wheat bran increases the metabolizable energy.

scholarly journals Esterase Active in Polar Organic Solvents from the Yeast Pseudozyma sp. NII 08165

2014 ◽  
Vol 2014 ◽  
pp. 1-10 ◽  
Author(s):  
Deepthy Alex ◽  
Anju Shainu ◽  
Ashok Pandey ◽  
Rajeev K. Sukumaran
Keyword(s):  
Organic Solvents ◽  
Enzyme Production ◽  
Fold Increase ◽  
Methanol Concentration ◽  
Crude Enzyme ◽  
Biodiesel Production ◽  
Original Activity ◽  
Acyl Acceptor ◽  
Polar Organic Solvents

Esterases/lipases active in water miscible solvents are highly desired in biocatalysis where substrate solubility is limited and also when the solvent is desired as an acyl acceptor in transesterification reactions, as with the case of biodiesel production. We have isolated an esterase from the glycolipid producing yeast-Pseudozyma sp. NII 08165 which in its crude form was alkali active, thermo stable, halo tolerant and also capable of acting in presence of high methanol concentration. The crude enzyme which maintained 90% of its original activity after being treated at 70°C was purified and the properties were characterized. The partially purified esterase preparation had temperature and pH optima of 60°C and 8.0 respectively. The enzyme retained almost complete activity in presence of 25% methanol and 80% activity in the same strength of ethanol. Conditions of enzyme production were optimized, which lead to 9 fold increase in the esterase yield. One of the isoforms of the enzyme LIP1 was purified to homogeneity and characterized. Purified LIP1 had a Km and Vmax of 0.01 and 1.12, respectively. The purified esterase lost its thermo and halo tolerance but interestingly, retained 97% activity in methanol.

scholarly journals Chitosanase production by Paenibacillus ehimensis and its application for chitosan hydrolysis

2010 ◽  
Vol 53 (6) ◽  
pp. 1461-1468 ◽  
Author(s):  
Maria Giovana Binder Pagnoncelli ◽  
Nathália Kelly de Araújo ◽  
Nayane Macêdo Portela da Silva ◽  
Cristiane Fernandes de Assis ◽  
Sueli Rodrigues ◽  
...  
Keyword(s):  
Carbon Source ◽  
Enzyme Production ◽  
Culture Medium ◽  
Maximum Level ◽  
Crude Enzyme ◽  
Good Stability ◽  
Submerged Cultures ◽  
Paenibacillus Ehimensis ◽  
Chitosan Hydrolysis ◽  
Chitosanase Activity

The chitosanase production by Paenibacillus ehimensis was studied in submerged cultures and the chitosan hydrolysis was evaluated by using these enzymes without purification. The bacterium produced inducibles enzymes after 12 h of growth in a culture medium containing 0.2% (w/v) of soluble chitosan as carbon source. The enzyme production was strongly repressed by the presence of glucose. The production started as soon as the available sugars finished in the culture medium. The maximum level of chitosanase activity was 500 U.L-1 at 36°C after 36 h incubation. The crude enzyme was optimally active at pH 6.0 and 55°C and in these conditions, the enzyme presented good stability (6 days). The enzyme without purification was used to hydrolyze the chitosan which resulted chitooligosaccharides between 20 and 30 min of reaction.

scholarly journals Rabbit reticulocyte coated vesicles carrying the transferrin- transferrin receptor complex: I. Purification and partial characterization

Blood ◽  
1987 ◽  
Vol 70 (4) ◽  
pp. 1035-1039
Author(s):  
HR Choe ◽  
ST Moseley ◽  
J Glass ◽  
MT Nunez
Keyword(s):  
Transferrin Receptor ◽  
Specific Activity ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Protein Composition ◽  
Coated Vesicles ◽  
Coated Vesicle ◽  
Receptor Complex ◽  
Assembly Factor ◽  
Excellent Source

Coated vesicles bearing the transferrin-transferrin receptor complex were isolated from rabbit reticulocytes by freeze-thaw cell lysis, followed by differential centrifugation with pelleting of vesicles at 100,000 g. Electronmicroscopy demonstrated the vesicles to have the characteristic morphology of coated vesicles, including the appearance of triskelions. The protein composition of the vesicles as determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis included transferrin, transferrin receptor, and proteins of apparent mol wt of approximately 180,000, 140,000, 100,000, and 47,000 daltons. The 180,000 and 100,000 mol wt proteins were identified as clathrin and coated vesicle assembly factor proteins, respectively, by Western blot analyses. The vesicles had a Mg2+-dependent ATPase with a specific activity of approximately 8.5 nmoles ATP converted/min/mg vesicle protein. The vesicles could acidify the intravesicular space, as evidenced by the stimulation of the Mg2+-ATPase by the protonophore FCCP. Reticulocytes appear to be an excellent source of coated vesicles and as such should provide a model for studying the endocytosis of transferrin and the steps of iron uptake that proceed in these vesicles.

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