Thermostable marine microbial proteases for industrial applications: scopes and risks

Barzkar, Noora; Homaei, Ahmad; Hemmati, Roohullah; Patel, Seema

doi:10.1007/s00792-018-1009-8

Cited by 60 publications

(31 citation statements)

References 132 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Proteases are enzymes with many uses in biotechnology, from hydrolysis of proteins to reduction of allergenicity or production of bioactive peptides, to fine chemistry (production of dipeptides, resolution of racemic mixtures, etc.) being the detergent industry the main consumer of proteases [1,2,3,4,5,6,7,8]. Alcalase, a protease solution supplied by Novozyme, has subtilisin Carlsberg as main component and it is produced by a strain of Bacillus licheniformis .…”

Section: Introductionmentioning

confidence: 99%

Further Stabilization of Alcalase Immobilized on Glyoxyl Supports: Amination Plus Modification with Glutaraldehyde

et al. 2018

View full text Add to dashboard Cite

Alcalase was immobilized on glyoxyl 4% CL agarose beads. This permitted to have Alcalase preparations with 50% activity retention versus Boc-l-alanine 4-nitrophenyl ester. However, the recovered activity versus casein was under 20% at 50 °C, as it may be expected from the most likely area of the protein involved in the immobilization. The situation was different at 60 °C, where the activities of immobilized and free enzyme became similar. The chemical amination of the immobilized enzyme or the treatment of the enzyme with glutaraldehyde did not produce any significant stabilization (a factor of 2) with high costs in terms of activity. However, the modification with glutaraldehyde of the previously aminated enzyme permitted to give a jump in Alcalase stability (e.g., with most than 80% of enzyme activity retention for the modified enzyme and less than 30% for the just immobilized enzyme in stress inactivation at pH 7 or 9). This preparation could be used in the hydrolysis of casein at pH 9 even at 67 °C, retaining around 50% of the activity after 5 hydrolytic cycles when the just immobilized preparation was almost inactive after 3 cycles. The modified enzyme can be reused in hydrolysis of casein at 45 °C and pH 9 for 6 cycles (6 h) without any decrease in enzyme activity.

show abstract

Section: Introductionmentioning

confidence: 99%

Further Stabilization of Alcalase Immobilized on Glyoxyl Supports: Amination Plus Modification with Glutaraldehyde

et al. 2018

View full text Add to dashboard Cite

show abstract

“…The optimum temperature for the maximum enzyme activity was found to be 45 °C, which implies that the enzyme is also thermostable (Briki et al 2016). Such thermostable proteases are important in biotechnological, and industrial applications due to their stability against denaturing agents, and other chemicals (Barzkar et al 2018). The enzyme shows maximum activity at pH 9, and hence can be classi ed as an alkaline protease.…”

Section: Application Of Protease In Contact Lens Cleansingmentioning

confidence: 98%

Isolation and Bioprocess Optimization of Halophilic and Alkaline Protease From Marine Streptomyces and Its Use As Contact Lens Cleaner

Sarkar

Suthindhiran

2020

Preprint

View full text Add to dashboard Cite

Abstract In the present study, an alkaline protease was isolated from marine Streptomyces sp. GS – 3. The strain was isolated from the backwaters of Puthuvypeen, Kerala, and identified as Streptomyces sp. by polyphasic taxonomy. The media for protease production was optimized by response surface methodology (RSM) using the Box-Behnken model. The maximum yield (357 U/ml) was observed using wheat bran as substrate (5.5%), pH 5.5, and the incubation period of 9 days at 28 ᴼC. The optimum temperature and pH conditions for the maximum enzyme activity were 45 °C, and 9 respectively. The Km and Vmax values of the enzyme were determined as 5.88%, and 38.46 µmol l− 1 min− 1 mg− 1, respectively, using 1% casein as substrate. The enzyme was isolated by solvent extraction with acetone, and the crude enzyme was characterized by Sodium Dodecyl Sulphate Poly-Acrylamide Gel Electrophoresis (SDS-PAGE) and Circular Dichroism (CD) studies. The enzyme sustained at high temperature (50 °C for 6 h), and alkaline pH (10) conditions, and was active in the presence of metal ions, and organic solvents. The purified enzyme was inhibited by phenylmethylsulphonyl fluoride (PMSF) suggesting it belong to serine protease. Further to exploit its application, contact lenses were incubated with the enzyme solution, and the protein debris on it was found to be scrubbed at an optimum time of 60 minutes. Therefore, it increases the transmittance of the contact lens indicating its use as a potential contact lens cleansing agent.

show abstract

“…A large number of enzymes from deep-sea thermophilic microorganisms have been characterised to date (Table 1) [35], and thermophilic proteases, lipases and polymer-degrading enzymes, in particular, have found their way into industrial applications [11]. The diversity of deep-sea thermophiles makes them valuable in the search for novel thermostable proteolytic enzymes [56,57], which are attractive for use in the detergent, food and feed industries. Jin et al [44] reported the purification and characterisation of a thermostable and alkali-stable keratinase Ker02562 from Bacillus sp.…”

Section: Deep-sea Thermophilic Enzymesmentioning

confidence: 99%

Properties and Applications of Extremozymes from Deep-Sea Extremophilic Microorganisms: A Mini Review

et al. 2019

View full text Add to dashboard Cite

The deep sea, which is defined as sea water below a depth of 1000 m, is one of the largest biomes on the Earth, and is recognised as an extreme environment due to its range of challenging physical parameters, such as pressure, salinity, temperature, chemicals and metals (such as hydrogen sulphide, copper and arsenic). For surviving in such extreme conditions, deep-sea extremophilic microorganisms employ a variety of adaptive strategies, such as the production of extremozymes, which exhibit outstanding thermal or cold adaptability, salt tolerance and/or pressure tolerance. Owing to their great stability, deep-sea extremozymes have numerous potential applications in a wide range of industries, such as the agricultural, food, chemical, pharmaceutical and biotechnological sectors. This enormous economic potential combined with recent advances in sampling and molecular and omics technologies has led to the emergence of research regarding deep-sea extremozymes and their primary applications in recent decades. In the present review, we introduced recent advances in research regarding deep-sea extremophiles and the enzymes they produce and discussed their potential industrial applications, with special emphasis on thermophilic, psychrophilic, halophilic and piezophilic enzymes.Nearly three-quarters of the Earth's surface area is covered by ocean, the average depth of which is 3800 m, implying that the vast majority of our planet comprises deep-sea environments. The deep sea is one of the most mysterious and unexplored environments on the Earth, and it supports diverse microbial communities that play important roles in biogeochemical cycles [1]. The deep sea is also recognised as an extreme environment, as it is characterised by the absence of sunlight and the presence of predominantly low temperatures and high hydrostatic pressures, and these environmental conditions become even more challenging in particular habitats, such as deep-sea hydrothermal vents with their extremely high temperatures of >400 • C, deep hypersaline anoxic basins (DHABs) with their extremely high salinities and abysses of up to 11 km depth with their extremely high pressures.Deep-sea extremophiles are living organisms that can survive and proliferate in deep-sea environments that have extreme physical (pressure and temperature) and geochemical (pH, salinity and redox potential) conditions that are lethal to other organisms. The majority of deep-sea extremophiles belong to the prokaryotes, which are microorganisms in the domains of Archaea and Bacteria [2,3].These extremophilic microorganisms are functionally diverse and widely distributed in taxonomy [4], and they are classified into thermophiles (55 • C to 121 • C), psychrophiles (−2 • C to 20 • C), halophiles (2-5 M NaCl or KCl), piezophiles (>500 atmospheres), alkalophiles (pH > 8), acidophiles (pH < 4) and metalophiles (high concentrations of metals, e.g., copper, zinc, cadmium and arsenic) according to the extreme environments in which they grow and the extreme conditions they can tolerate. Ma...

show abstract

Thermostable marine microbial proteases for industrial applications: scopes and risks

Cited by 60 publications

References 132 publications

Further Stabilization of Alcalase Immobilized on Glyoxyl Supports: Amination Plus Modification with Glutaraldehyde

Further Stabilization of Alcalase Immobilized on Glyoxyl Supports: Amination Plus Modification with Glutaraldehyde

Isolation and Bioprocess Optimization of Halophilic and Alkaline Protease From Marine Streptomyces and Its Use As Contact Lens Cleaner

Properties and Applications of Extremozymes from Deep-Sea Extremophilic Microorganisms: A Mini Review

Contact Info

Product

Resources

About