Study on Decolorization Effect of Three Dyes by Fermentation Crude Enzyme Solution of Marasmius tricolor 310b

2021 ◽  
Vol 10 (01) ◽  
pp. 81-89
Author(s):  
志慧 王
Keyword(s):  
Crude Enzyme ◽  
Enzyme Solution ◽  
Crude Enzyme Solution

scholarly journals Preparation and immobilization Glucoamylase and Pectinase by CLEA method

2014 ◽  
Vol 17 (2) ◽  
pp. 45-51
Author(s):  
Giang Thi Linh Tran ◽  
Oanh Ngoc Huynh
Keyword(s):  
Aspergillus Niger ◽  
Enzyme Preparation ◽  
Immobilized Enzyme ◽  
Solution Culture ◽  
Crude Enzyme ◽  
Cross Linking ◽  
Solid Culture ◽  
Enzyme Solution ◽  
Crude Enzyme Solution ◽  
Semi Solid

CLEA method (cross-linking enzyme aggregates) combines enzyme preparation and immobilization from solution culture into the same step. In this study, we applied CLEA method to immobilize two enzymes, glucoamylase and pectinase, from crude enzyme solution obtained from semi-solid culture of Aspergillus niger. The results showed that: In the same immobilized conditions (glucoamylase: 7% glutaraldehyde, 5°C, 2 hours; pectinase: 10% glutaraldehyde, 5°C, 2 hours), the immobilized enzyme from crude enzyme solution, has the abilities to be reused and activation stability under the influences of pH and temperature higher than immobilized commercial enzyme respectively.

scholarly journals Safety Evaluation and Whole Genome Sequencing of Aspergillus japonicas PJ01 Reveal Its Potential to Degrade Citrus Segments in Juice Processing

Foods ◽  
2021 ◽  
Vol 10 (8) ◽  
pp. 1736
Author(s):  
Yujiao Qian ◽  
Zhipeng Gao ◽  
Jieyi Wang ◽  
Chen Wang ◽  
Gaoyang Li ◽  
...  
Keyword(s):  
Whole Genome Sequencing ◽  
Genome Sequencing ◽  
Gene Annotation ◽  
Gc Content ◽  
Crude Enzyme ◽  
Control Group ◽  
Whole Genome ◽  
Enzyme Solution ◽  
Juice Processing ◽  
Crude Enzyme Solution

Aspergillus japonicas PJ01 (A. japonicas PJ01) is a strain isolated from the rotten branches. In previ-ous studies, it was shown that it can produce complex enzymes to degrade polysaccharide com-ponents. In this study, we evaluated the safety of its crude enzyme solution. Acute oral toxicity, subchronic toxicity, micronucleus and sperm malformation tests all validated the high biologi-cal safety for the crude enzymes. Secondly, we carried out the citrus segment degradation ex-periment of crude enzyme solution. Compared with the control group, the crude enzyme solu-tion of A. japonicas PJ01 can completely degrade the segments in 50 min, which provides the basis for enzymatic peeling during juice processing. The whole genome sequencing showed that the genome of A. japonicus PJ01 has a GC content of 51.37% with a size of 36204647 bp, and encoded 10070 genes. GO, COG, KEGG and CAZy databases were used in gene annotation analyses. Pathway enrichment showed many genes related to carbohydrate metabolism, rich in genes re-lated to pectinase, xylanase and carboxylcellulase. Therefore, the complex enzyme produced by A. japonicus PJ01 can be used in gizzard juice processing to achieve efficient enzymatic decapsu-lation.

scholarly journals Enzyme-Assisted Method for Phycobiliproteins Extraction from Porphyra and Evaluation of Their Bioactivity

Processes ◽  
2021 ◽  
Vol 9 (3) ◽  
pp. 560
Author(s):  
Chung-Hsiung Huang ◽  
Wei-Chen Chen ◽  
Yu-Huei Gao ◽  
Guan-Wen Chen ◽  
Hong-Ting Victor Lin ◽  
...  
Keyword(s):  
Liquid Chromatography ◽  
Enzymatic Hydrolysis ◽  
Antioxidant Activities ◽  
Polyacrylamide Gel Electrophoresis ◽  
Radical Scavenging ◽  
Crude Enzyme ◽  
Dependent Manner ◽  
Concentration Dependent Manner ◽  
Enzyme Solution ◽  
Crude Enzyme Solution

Due to the poor protein availability of algae in their unprocessed form, development of extraction methods for phycobiliproteins is of great significance. This study aimed to extract phycoerythrin (PE) and phycocyanin (PC) from Porphyra via bacterial enzymatic hydrolysis and to evaluate their bioactivity. To induce enzyme production, Porphyra powder was added into the culture medium of two marine bacterial strains. The pH and enzyme activity of the cultured supernatant, namely crude enzyme solution, were significantly raised. For PE and PC extraction, Porphyra were incubated within crude enzyme solution with homogenization and ultrasonication followed by ultrafiltration process. After distinguishing by fast performance liquid chromatography (FPLC), three major fractions were observed and identified as R-PE, R-PC and small molecular PE by high-performance liquid chromatography (HPLC) and polyacrylamide gel electrophoresis (PAGE) analysis. With respect to bioactivity, these three fractions exhibited free radical scavenging and antioxidant activities in a various degree. In addition, the angiotensin-converting-enzyme (ACE) inhibitory activity of both R-PE and R-PC fractions was observed in a concentration-dependent manner. Taken together, the employed process of bacterial enzymatic hydrolysis is suggested to be a feasible method to obtain PE and PC from Porphyra without limiting their bioactivity.

Purification and Characterization of Ginsenoside-Hydrolyzing β-Glucosidase from Wheat Bran

2013 ◽  
Vol 641-642 ◽  
pp. 906-909
Author(s):  
Chun Zhi Zhang ◽  
Ming Chen ◽  
Hai Chen Guo ◽  
Guo Ren Zu ◽  
Li Chen
Keyword(s):  
Molecular Weight ◽  
Wheat Bran ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Deae Cellulose ◽  
Polyacrylamide Gel ◽  
Purification And Characterization ◽  
Enzyme Solution ◽  
Crude Enzyme Solution

The ginsenoside-hydrolyzing β-glucosidase that can converse the major ginsenosides into the minor ginsenosides was isolated from wheat bran, and the enzyme was purified and characterized. The crude enzyme solution extracted from wheat bran could hydrolyse the protopanaxadiol-type ginsenosides such as Rb1, Rc, Rd and Rg3, but could not hydrolyse the protopanaxatriol-type ginsenosides such as Re and Rg2. The enzyme fractionated on the DEAE-Cellulose DE-52 column was purified to one spot in SDS polyacrylamide gel electrophoresis, and the molecular weight of enzyme in the fraction 34, 47, and 61 was approximately 62 kDa, 62 kDa, and 68 kDa, respectively.

XYLANASE, AN ENVIRONMENTALLY FRIENDLY BLEACHING AGENT FOR PULP AND PAPER: Characterization And Stabilization Study Of Bacillus licheniformis I-5 CRUDE Xylanase

2018 ◽  
Vol 7 (3) ◽  
Author(s):  
Budiasih Wahyuntari., dkk
Keyword(s):  
Thermal Stability ◽  
Bacillus Licheniformis ◽  
Hot Spring ◽  
Sodium Dodecyl ◽  
Luria Broth ◽  
Crude Enzyme ◽  
Half Time ◽  
Triton X100 ◽  
Sds Page ◽  
Xylanolytic Enzymes

Isolate I-5 was isolated from Ciseeng hot spring, West Java and was identified as Bacillus licheniformis I-5. The isolate produces extracellular xylanolytic enzymes on Oatspelt containing Luria broth agar medium. Optimal activity of the crude enzyme was  observed at 50ºC and pH 7. The effect of sodium dodecyl sulphate, b-mercaptoethanol and Triton-X100 were observed. Incubating the crude enzyme in 1.5% SDS and 1.5% b-mercaptoethanol at 50oC for 90 minutes then adding Triton-X100 at final concentration of 3.5% for 45 minutes only reduced 5.75% of the initial enzyme activity. SDS/PAGE and zymogram analysis showed that at least two xylanolytic enzymes presence in the crude enzyme. The molecular weight of the enzyme was estimated about 127 and 20kD. The enzyme hydrolysed xylan into xylobiose, xylotriose and other longer xylooligosaccharides. Thermal stability of the crude enzyme was observed at 50, 60, and 70oC and pH 7 and 8. The results showed that the half time of the crude enzyme incubated at 50, 60, and 70oC pH 7 was 2 hours 55 minutes; 2 hours 33 minutes and 1 hour 15 minutes respectively. The half time at 50, 60 and 70oC, pH 8 was 2 hours 48 minutes; 1 hour 22 minutes and 1 hour 9 minutes respectively.keywords: Xilanase, Bacillus licheniformis I-5, thermal stability

In-Vitro Effects of Ricinus Communis Seed Kernel Extract On Some Antioxidant And Hydrolytic Enzymes In Nymph And Adult Zonocerus Variegatus (Grasshopper)

2019 ◽  
Vol 3 (1) ◽  
pp. 129-137
Author(s):  
Gbadebo E . Adeleke ◽  
Olaniyi T. Adedosu ◽  
Rachael O. Adeyi ◽  
John O. Fatoki
Keyword(s):  
Ricinus Communis ◽  
Hydrolytic Enzymes ◽  
Crude Enzyme ◽  
Economic Losses ◽  
Seed Kernel ◽  
Zonocerus Variegatus ◽  
Sod Activity ◽  
Enzyme Preparations ◽  
In Vitro Effects

Background: Many plants have been identified for their insecticidal properties as alternatives to synthetic ones, which are toxic to untargeted organisms and environment. Ricinus communis (Castor) has been re-ported to exhibit insecticidal properties against insect pests. Zonocerus variegatus (Grasshopper) is a notable pest of several crops, and has been linked with great economic losses to farmers. The present study investigates the in-vitro toxicity of R. communis seed kernel extract (RCSKE) on the activities of selected antioxidant and hydrolytic enzymes in nymph and adult Zonocerus variegatus (Grasshopper), using cypermethrin (CYPER-M) and chlorpyrifos (CPF) as standard conventional pesticides. Methods: Seed kernel of Ricinus communis (Castor) was subjected to acidified aqueous extraction to obtain the extract (RCSKE). Crude enzyme preparations were obtained from nymph and adult Z. variegatus grass-hoppers. The in-vitro effects of different concentrations (15, 30, 45, 60, 75, 90 and 105μg/ml) each of RCSKE, CYPER-M and CPF on the activities of superoxide dismutase (SOD), catalase (CAT), acetylcholinesterase (AChE) and carboxylesterase (CES) in crude enzyme preparations were estimated spectrophotometrically. The level of statistical significance was 0.05. Results: The RCSKE significantly reduced the in-vitro SOD activity (p < 0.05) in nymph Z. variegatus at all the concentrations, whereas both CYPER-M and CPF significantly reduced the activity only at certain concentrations. The CAT activity in the nymph was significantly decreased by RCSKE and CPF at all the concentrations, but CYPER-M decreased it only at certain concentrations. In adult Z. variegatus, SOD activity was not significantly affected (p > 0.05), while CAT activity was significantly increased (p < 0.05) by the three agents at all the concentrations. The AChE and CES activities in the nymph were significantly reduced by RCSKE, CYPER-M and CPF at all the concentrations. The RCSKE and CPF significantly increased the CES activity, while CYPER-M caused a significant decrease in the activity in adult Z. variegatus. Conclusion: The seed kernel extract of Ricinus communis is an effective pesticidal agent and hence, it could be a source of biopesticide alternative with greater potential than cypermethrin and chlorpyrifos. In addition, the antioxidant, acetylcholinesterase and carboxylesterase enzymes in the nymphs of Z. variegatus grasshoppers are more susceptible to the effect of the extract than in the adult grasshoppers.

Enzymatic Textile Dyes Decolorization by In vitro and In silico Studies

2019 ◽  
Vol 13 (4) ◽  
pp. 268-276
Author(s):  
Sridevi Ayla ◽  
Monika Kallubai ◽  
Suvarnalatha Devi Pallipati ◽  
Golla Narasimha
Keyword(s):  
Molecular Docking ◽  
In Silico ◽  
Docking Studies ◽  
Textile Dyes ◽  
Crude Enzyme ◽  
Eastern Ghats ◽  
Textile Dye ◽  
Phanerochaete Sordida ◽  
Molecular Docking Studies ◽  
In Silico Studies

Background:Laccase, a multicopper oxidoreductase (EC: 1.10.3.2), is a widely used enzyme in bioremediation of textile dye effluents. Fungal Laccase is preferably used as a remediating agent in the treatment and transformation of toxic organic pollutants. In this study, crude laccase from a basidiomycetes fungus, Phanerochaete sordida, was able to decolorize azo, antroquinone and indigoid dyes. In addition, interactions between dyes and enzyme were analysed using molecular docking studies.Methods:In this work, a white rot basidiomycete’s fungus, Phanerochaete sordida, was selected from forest soil isolates of Eastern Ghats, and Tirumala and lignolytic enzymes production was assayed after 7 days of incubation. The crude enzyme was checked for decolourisation of various synthetic textile dyes (Vat Brown, Acid Blue, Indigo, Reactive Blue and Reactive Black). Molecular docking studies were done using Autodock-4.2 to understand the interactions between dyes and enzymes.Results:Highest decolourisation efficiency was achieved with the crude enzyme in case of vat brown whereas the lowest decolourisation efficiency was achieved in Reactive blue decolourisation. Similar results were observed in their binding affinity with lignin peroxidase of Phanerochaete chrysosporium through molecular docking approach.Conclusion:Thus, experimental results and subsequent in silico validation involving an advanced remediation approach would be useful to reduce time and cost in other similar experiments.

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.

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