scholarly journals Protease Produced by Endophytic Fungi: A Systematic Review

Molecules ◽  
2021 ◽  
Vol 26 (22) ◽  
pp. 7062
Author(s):  
Victor Hugo Souto Bezerra ◽  
Samuel Leite Cardoso ◽  
Yris Fonseca-Bazzo ◽  
Dâmaris Silveira ◽  
Pérola Oliveira Magalhães ◽  
...  

The purpose of this systematic review was to identify the available literature of production, purification, and characterization of proteases by endophytic fungi. There are few complete studies that entirely exhibit the production, characterization, and purification of proteases from endophytic fungi. This study followed the PRISMA, and the search was conducted on five databases: PubMed, PMC, Science Direct, Scopus Articles, and Web of Science up until 18 May 2021, with no time or language restrictions. The methodology of the selected studies was evaluated using GRADE. Protease production, optimization, purification, and characterization were the main evaluated outcomes. Of the 5540 initially gathered studies, 15 met the inclusion criteria after a two-step selection process. Only two studies optimized the protease production using statistical design and two reported enzyme purification and characterization. The genus Penicillium and Aspergillus were the most cited among the eleven different genera of endophytic fungi evaluated in the selected articles. Six studies proved the ability of some endophytic fungi to produce fibrinolytic proteases, demonstrating that endophytic fungi can be exploited for the further production of agents used in thrombolytic therapy. However, further characterization and physicochemical studies are required to evaluate the real potential of endophytic fungi as sources of industrial enzymes.

Author(s):  
Swapnali S Gujarathi ◽  
Sandip B. Bankar ◽  
Laxmi A. Ananthanarayan

Bacteriocins are bactericidal or bacteriostatic in action and active against closely related species. Nisin is the bacteriocin produced by the lactic acid bacteria (LAB). Nisin is a small (3353 Da), cationic, hydrophobic, and 34-amino acid peptide. It is used in products such as pasteurized processed cheese, salad dressing, and liquid whole eggs to inhibit the growth of Gram-positive microorganisms including Listeria monocytogenes. The objective of the present work was to study production, purification and characterization of nisin. The production of nisin was carried out using Lactococcus lactis subsp lactis MTCC 440 by one-factor-at-a-time method and statistical design (Orthogonal array). Purification was carried out using ammonium sulphate precipitation followed by hydrophobic interaction and gel chromatography. Characterization was done for pH and temperature stability. The activity of nisin after one factor at a time optimization was found to be 5120 AU/ml. The activity of the nisin increased to 6800 AU/ml after optimization by Orthogonal Array design. Ammonium sulphate precipitation gives good yield of nisin with 60 to 80% saturation with 2.52 fold purity. The overall purification by hydrophobic interaction and gel filtration chromatography was 10.87 fold with 50.84% yield and 8.8 fold with 49.65% yield as compared to crude broth respectively.


2021 ◽  
Vol 93 (suppl 3) ◽  
Author(s):  
FELYPE T.B. ROCHA ◽  
ROMERO M.P. BRANDÃO-COSTA ◽  
ANNA GABRIELLY D. NEVES ◽  
KETHYLEN B.B. CARDOSO ◽  
THIAGO P. NASCIMENTO ◽  
...  

Author(s):  
Adebayo-Tayo Bukola Christianah ◽  
Onifade Deborah Ajoke

Endo-β-1,4-D-mannanase (β-mannanase; EC 3.2.1.78) catalyses the random hydrolysis of mannoglycosidic bonds in mannan-based polysaccharides. These enyzmes are commonly found in nature and are located within the structure of mannans and heteromannans (galactomannan, glucomannan and galactoglucomannan) in the hemicellulose fraction of trees with soft tissues and hard tissues, locust bean seed.  Most β-mannanases degrade mannooligosaccharides down to a degree of polymerization of four. In this study mannanase was produced using a submerged fermentation method from Bacillus subtilis. The effect of growth of the organism and processing parameters on the production of mannanase were determined after which optimization studies were carried out. The enzyme was partially purified using ammonium sulphate, dialysis and gel filtration. The partially purified enzyme was characterized. The result of the study showed that mannanase enzyme from Bacillus subtilis was optimally produced in a medium comprising of galactose, peptone, sugarcane bagasse at a pH of 6.0 and a temperature of 45 oC. The enzyme was most stable and active at pH 10.0 and at a temperature of 40 oC.  and 60 respectively.


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