Enzyme Production by Induratia spp. Isolated from Coffee Plants in Brazil

Monteiro, Mônica Cristina Pereira; Tavares, Dérica Gonçalves; Nery, Eduardo Mateus; Queiroz, Marisa Vieira de; Pereira, Olinto Liparini; Cardoso, Patrícia Gomes

doi:10.1590/1678-4324-2020180673

Cited by 18 publications

(13 citation statements)

References 56 publications

(59 reference statements)

Supporting

Mentioning

Contrasting

Order By: Relevance

“… Plant Endophytic fungi Enzyme References 1 Allium cepa Beauveria bassiana MN544934 Xylanase, endoglucanase Amobonye et al ( 2021 ) 2 Coffee plants Induratia sp. CML4013 Lipase, amylase, protease, phytase, pectinase, cellulase Monteiro et al ( 2020 ) 3 Vitis labrusca L. Diaporthe sp. KM362392 Endoglucanase Felber et al ( 2019 ) 4 Fusarium culmorum KM362384 Endoglucanase 5 Andropogon gayanus Fusarium verticillioides Endoglucanase, cellobiase, cellulase de Almeida et al ( 2019 ) 6 Phoenix dactylifera L. Penicillium bilaiae TDPEF30 Protease (especially acidic protease) Ben et al ( 2019 ) 7 Simarouba glauca Phomopsis sp.…”

Section: Research Progress On the Biodegradation Activity Of Endophytic Fungimentioning

confidence: 99%

Biotransformation ability of endophytic fungi: from species evolution to industrial applications

Liu

Zhou

Cui

et al. 2021

Appl Microbiol Biotechnol

View full text Add to dashboard Cite

Increased understanding of the interactions between endophytic fungi and plants has led to the discovery of a new generation of chemical compounds and processes between endophytic fungi and plants. Due to the long-term co-evolution between fungal endophytes and host plants, endophytes have evolved special biotransformation abilities, which can have critical consequences on plant metabolic processes and their composition. Biotransformation or bioconversion can impact the synthesis and decomposition of hormones, sugars, amino acids, vitamins, lipids, proteins, and various secondary metabolites, including flavonoids, polysaccharides, and terpenes. Endophytic fungi produce enzymes and various bioactive secondary metabolites with industrial value and can degrade or sequester inorganic and organic small molecules and macromolecules (e.g., toxins, pollutants, heavy metals). These fungi also have the ability to cause highly selective catalytic conversion of high-value compounds in an environmentally friendly manner, which can be important for the production/innovation of bioactive molecules, food and nutrition, agriculture, and environment. This work mainly summarized recent research progress in this field, providing a reference for further research and application of fungal endophytes. Key points •The industrial value of degradation of endophytes was summarized. • The commercial value for the pharmaceutical industry is reviewed. Graphical abstract

show abstract

Section: Research Progress On the Biodegradation Activity Of Endophytic Fungimentioning

confidence: 99%

Biotransformation ability of endophytic fungi: from species evolution to industrial applications

Liu

Zhou

Cui

et al. 2021

Appl Microbiol Biotechnol

View full text Add to dashboard Cite

show abstract

“…Fouda et al [38] George et al [65] Gupta et al [36] Hassan [66] Indarmawan et al [67] Jagannath et al [68] Jalili et al [69] Kapoor et al [70] Katoch et al [71] Katoch et al [72] Kudryavtseva et al [73] Kumar et al [74] Kuzhalvaymani et al [75] Leake and Read [76] Lindstrom et al [77] Liu et al [78] Lopez-Llorca et al [79] Lumyong et al [80] Maccheroni et al [81] Martins et al [82] Meshram et al [39] Mishra et al [83] Monteiro et al [84] Orlandelli et al [85] Prathyusha et al [86] Rajagopal et al [87] Rajesh and Ravishankar Rai [88] Reddy et al [89] Santos et al [90] Seshagiri and Tallapragada [91] Sharma et al [92] Silva et al [93] Sopalun and Iamtham [94] Sopalun et al [95] Swetha et al [96] Wu et al [97] Zaferanloo et al [98] Reasons for exclusion:…”

Section: Referencesmentioning

confidence: 99%

Protease Produced by Endophytic Fungi: A Systematic Review

et al. 2021

View full text Add to dashboard Cite

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.

show abstract

“…Amylase activity and protein production was measured using Di nitrosalysilic acid and folin reagent (Jain et al 2020 and Lowry et al 1951). The speci c activity of amylase was calculated by dividing the activity into protein (Monteiro 2020).…”

Section: Enzyme Assaymentioning

confidence: 99%

Production optimization using Plackett-Burman and Box-Behnken designs with partial characterization of amylase from marine actinomycetes

Bukhari

Al-Agamy

Kelany

et al. 2021

Preprint

View full text Add to dashboard Cite

Amylase is an industrial enzyme that is used in the food and biofuel industries. We screened four actinomycetes strains for amylase biosynthesis. The Streptomyces rochei strain had a larger hydrolytic zone (24 mm) on starch agar plates, than the other isolates. Plackett-Burman’s experimental design was implemented to optimize the conditions for amylase production by the selected strains. Growth under optimized culture conditions led to 1.7, 9.8, 7.7, and 3.12 -fold increases for the isolates S. griseorubens, S. rochei, S. parvus, and Streptomyces sp., respectively, in the specific activity measurement in comparison with growth under primary conditions. When applying the Box-Behnken design on S. rochei using the most significant parameters starch, K2HPO4, pH, and temperature, there was a 12.22-fold increase in the specific activity measurement: 7.37 U/mg. The optimal fermentation medium formula was kept at 30.6°C for seven days. The amylase from S. rochei was partially purified, and its molecular weight was determined using Sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The molecular weight was found to be 45, 43, and 53 kDa. Amylase was particularly active at pH 6 and 65°C. The purified enzyme was most active at 65°C and a pH of 6, thermal stability of 70°C for 40 min and salt concentration of 1 M with a Km and Vmax of 6.58 mg/ml and 21.93 mg/ml/min, respectively. The amylase improved by adding Cu + 2, Zn + 2, and Fe + 2 (152.21%, 207.24%, and 111.89%). Increased production of amylase enzyme by Streptomyces rochei KR108310 attracts the production of industrially significant products.

show abstract

Enzyme Production by Induratia spp. Isolated from Coffee Plants in Brazil

Cited by 18 publications

References 56 publications

Biotransformation ability of endophytic fungi: from species evolution to industrial applications

Biotransformation ability of endophytic fungi: from species evolution to industrial applications

Protease Produced by Endophytic Fungi: A Systematic Review

Production optimization using Plackett-Burman and Box-Behnken designs with partial characterization of amylase from marine actinomycetes

Contact Info

Product

Resources

About