A novel thermostable xylanase from Geobacillus vulcani GS90: Production, biochemical characterization, and its comparative application in fruit juice enrichment

Production of microbial enzymes at the industrial scale and their commercialization has gained a lot of focus and importance. Some of the industrially important enzymes from microbial origin include lipases, amylases, proteases, xylynases, pectinases etc. The objective of the study was production and application of bacterial pectinase for industrial use (clarification of fruit juices). Here the isolation of microorganism and characterization was done, then pectinase assay was performed and finally fruit juice was clarified using this enzyme. Here decayed orange peel was used as the sample and it was collected from a local market, South Kalamsseri- Cochin. The collected decayed orange part was subjected to serial dilution in order to isolate the organism. The dilutions were then plated on appropriate media (pecin agar media) and spread plate was performed. After the incubation time, colonies with zone were obtained which showed the production of pectinase enzyme. These isolated colonies were then inoculated to the petri plate containing pectin agar media and streak plate was performed. After 24 h incubation, the isolated colonies were subjected to Gram’s staining. It was Gram negative bacilli. The biochemical characterization (IMViC test) was done and VP Citrate tests were positive. Then the colonies were inoculated in Pectinase Production Broth. After 24 h incubation, the media was centrifuged for the isolation of enzymes. The enzyme assay was done by titration technique and the enzyme activity was found to be 0.78 U. This isolated enzyme was used for the clarification of apple juice and lime juice. According to the findings obtained from the study, the clarification of fruit juice by the use of bacterial pectinase is most cost effective and yield good results for industrial use.

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Purification and Biochemical Characterization of a Highly Thermostable Xylanase from Actinomadura sp. Strain Cpt20 Isolated from Poultry Compost

Applied Biochemistry and Biotechnology ◽

10.1007/s12010-011-9457-y ◽

2011 ◽

Vol 166 (3) ◽

pp. 663-679 ◽

Cited By ~ 39

Author(s):

Zina Taibi ◽

Boudjemaa Saoudi ◽

Mokhtar Boudelaa ◽

Héla Trigui ◽

Hafedh Belghith ◽

...

Keyword(s):

Biochemical Characterization ◽

Thermostable Xylanase

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Use Of Baceriocin Producing Lactobacilli Strains From Fruits And Vegetables In Food Preservation

THE JOURNAL OF MICROBIOLOGY AND MOLECULAR GENETICS ◽

10.52700/jmmg.v1i1.4 ◽

2020 ◽

Vol 1 (1) ◽

Author(s):

Syeda Fatima Zehra ◽

Umaima Rubbani ◽

Atia Iqbal

Keyword(s):

Fruits And Vegetables ◽

Fruit Juice ◽

Biochemical Characterization ◽

Bacteriocin Production ◽

Antibiotic Activity ◽

Food Preservation ◽

Zone Of Inhibition ◽

Biochemical Activity ◽

Selective Media

Bacteriocin producing bacteria plays an important role in food preservation. The bacteriocin producing Lactobacilli strains were isolated from different fruits and vegetables from the local markets of Punjab, Pakistan. The bacterial were grown on MRS selective media and their biochemical activity was checked further for the confirmation of Lactobacilli. Antimicrobial activity of these selected strains was checked against different pathogens. For further characterization of bacteriocin production by Lactobacilli, the activity of bacteriocin at different parameters such as at different temperature and pH and the proteolytic activity were checked. Antibiotic activity of bacteriocin producing Lactobacilli was also checked against ampicillin, ciprofloxacin, streptomycin and tetracycline. Out of total strains isolated, 10 strains were selected as Lactobacilli on the basis of their morphology and biochemical characterization. 80% of strains showed zone of inhibition with the best zone being shown by Ct2 (14 mm) against E.coli (ETCC) and A3 (14 mm) against Enterobacteria. Bacteriocin ability of these selected strains was found maximum at 7 pH and 35ºC. The strain T1 was sensitive to ampicillin, ciprofloxacin and streptomycin and strain T2 was resistant to ciprofloxacin, streptomycin and tetracycline. The best characterized strains were selected for fruit juice preservation where lactobacilli producing bacteriocin prevent the growth of other food spoiling bacteria.

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A thermophilic α-l-Arabinofuranosidase from Geobacillus vulcani GS90: heterologous expression, biochemical characterization, and its synergistic action in fruit juice enrichment

European Food Research and Technology ◽

10.1007/s00217-018-3075-7 ◽

2018 ◽

Vol 244 (9) ◽

pp. 1627-1636 ◽

Cited By ~ 6

Author(s):

Hüseyin İlgü ◽

Yusuf Sürmeli ◽

Gülşah Şanlı-Mohamed

Keyword(s):

Heterologous Expression ◽

Fruit Juice ◽

Biochemical Characterization ◽

Synergistic Action

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Purification and Biochemical Characterization of Cysteine Protease from Baby Kiwi (Actinidia arguta)

The Open Biochemistry Journal ◽

10.2174/1874091x01913010054 ◽

2019 ◽

Vol 13 (1) ◽

pp. 54-63

Author(s):

Sayaka Miyazaki-Katamura ◽

Mio Yoneta-Wada ◽

Miyuki Kozuka ◽

Tomohisa Sakaue ◽

Takuya Yamane ◽

...

Keyword(s):

Ion Exchange ◽

Cysteine Protease ◽

Fruit Juice ◽

Biochemical Characterization ◽

Cysteine Proteases ◽

Biochemical Properties ◽

Ion Exchange Chromatography ◽

Exchange Chromatography ◽

Potential Health ◽

Actinidia Arguta

Background: It has recently been reported that the fruit, stems and leaves of Actinidia arguta have various potential health effects including an antioxidant effect, anticancer effect, anti-allergic effect and α-glucosidase inhibitory effect. However, little is known about the biochemical properties of cysteine protease in the fruit juice of A. arguta. Methods: Ion exchange chromatography to purify the cysteine protease from the fruit juice of A. arguta, and some synthetic substrates to determinate the enzyme activity were used. Results: Cysteine protease was purified to homogeneity from A. arguta fruit juice by ion exchange chromatography. The molecular weight of the purified enzyme was calculated to be approximately 25,500 by SDS-PAGE in the presence of β-ME. The enzyme rapidly hydrolyzed the substrate Z-Leu-Arg-MCA and moderately hydrolyzed other substrates including Boc-Val-Leu-Lys-MCA, Z-Val-Val-Arg-MCA and Z-Phe-Arg-MCA. Kinetic parameters for these four substrates were determined. The Km, Vmax, Kcat and Kcat/Km values for Z-Leu-Arg-MCA, the most preferentially cleaved by the enzyme, were 100 μM, 63.8 μmoles/mg/min, 27.26 sec-1 and 0.2726 sec-1μM-1, respectively. Furthermore, the activity of the enzyme was strongly inhibited by inhibitors including antipain, leupeptin, E-64, E-64c, kinin-free-LMW kininogen and cystatin C. Those biochemical data indicated that the enzyme was a cysteine protease. The amino acid sequence of the first 21 residues of cysteine protease purified from Actinidia arguta was Val1-Leu-Pro-Asp-Tyr5-Val-Asp-Trp-Arg-Ser10-Ala-Gly-Ala-Val-Val15-Asp-Ile-Lys-Ser-Qln20-Gly. This sequence showed high homology to the sequences of actinidin from Acinidia deliciosa (95.0%) and actinidin from Actinidia eriantha (90%). These three cysteine proteases were thought to be common allied species. Conclusion: The biochemical properties of the enzyme purified from A. arguta fruit juice were determined. These basic data are expected to contribute to the maintenance and improvement of human health as well as to the promotion of protein digestion and absorption through its proteolytic functions.

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Plant Pathology Diagnosed by X-Ray Microanalysis

Proceedings, annual meeting, Electron Microscopy Society of America ◽

10.1017/s0424820100129152 ◽

1987 ◽

Vol 45 ◽

pp. 974-975

Author(s):

J. H. Resau ◽

N. Howell ◽

S. H. Chang

Keyword(s):

Electron Microscopy ◽

Plant Pathology ◽

Biochemical Characterization ◽

Nutrient Deficiency ◽

Green Leaf ◽

Parasitic Infestation ◽

X Ray

Spinach grown in Texas developed “yellow spotting” on the peripheral portions of the leaves. The exact cause of the discoloration could not be determined as there was no evidence of viral or parasitic infestation of the plants and biochemical characterization of the plants did not indicate any significant differences between the yellow and green leaf portions of the spinach. The present study was undertaken using electron microscopy (EM) to determine if a micro-nutrient deficiency was the cause for the discoloration.Green leaf spinach was collected from the field and sent by express mail to the EM laboratory. The yellow and equivalent green portions of the leaves were isolated and dried in a Denton evaporator at 10-5 Torr for 24 hrs. The leaf specimens were then examined using a JEOL 100 CX analytical microscope. TEM specimens were prepared according to the methods of Trump et al.

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The in vivo distribution and dynamics of DNA topoisomerase II in Drosophila embryonic nuclei and chromosomes

Proceedings, annual meeting, Electron Microscopy Society of America ◽

10.1017/s0424820100146217 ◽

1993 ◽

Vol 51 ◽

pp. 74-75

Author(s):

Jason R. Swedlow ◽

Neil Osheroff ◽

Tim Karr ◽

John W. Sedat ◽

David A. Agard

Keyword(s):

Topoisomerase Ii ◽

Biochemical Characterization ◽

Developmental Cycle ◽

Dna Topoisomerase Ii ◽

Chromosomal Distribution ◽

Dna Topoisomerase ◽

Ideal System ◽

Dnase Treatment

DNA topoisomerase II is an ATP-dependent double-stranded DNA strand-passing enzyme that is necessary for full condensation of chromosomes and for complete segregation of sister chromatids at mitosis in vivo and in vitro. Biochemical characterization of chromosomes or nuclei after extraction with high-salt or detergents and DNAse treatment showed that topoisomerase II was a major component of this remnant, termed the chromosome scaffold. The scaffold has been hypothesized to be the structural backbone of the chromosome, so the localization of topoisomerase II to die scaffold suggested that the enzyme might play a structural role in the chromosome. However, topoisomerase II has not been studied in nuclei or chromosomes in vivo. We have monitored the chromosomal distribution of topoisomerase II in vivo during mitosis in the Drosophila embryo. This embryo forms a multi-nucleated syncytial blastoderm early in its developmental cycle. During this time, the embryonic nuclei synchronously progress through 13 mitotic cycles, so this is an ideal system to follow nuclear and chromosomal dynamics.

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