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Diversity and Utilization of Marine Cyanobacteria
Published in Gokare A. Ravishankar, Ranga Rao Ambati, Handbook of Algal Technologies and Phytochemicals, 2019
Several important enzymes are known to be produced in high enough amounts by cyanobacteria to be useful for commercial ventures. The fact that several marine cyanobacteria could be useful for large-scale production of enzymes such as beta lactamase, protease and lipase has been identified and characterized (Prabakaran et al., 1994). Several common as well as unique sequence-specific endonucleases are known from cyanobacteria such as Anabaena cylindrica (Acy I), Anabaena flos-aquae (Afl I and Afl III), Anabaena variabilis (AvaI and Ava II), Anabaena variabilis UW (Avr II), Nostoc sp. PCC 7524 (Nsp C I) and Microcoleus sp. UFEX 2220 (Mst II), which can be made available in the market at lesser cost since cyanobacterial biomass production is much less expensive than bacteria (Elhai and Wolk, 1988; Patterson, 1996). Extra cellular phosphatases from cyanobacterial isolates have also been reported. They have the capacity to mineralize organic phosphorous by alkaline phosphotase activity (Giraudet et al., 1997). Several studies have reported the possibility of producing enzymes such as chitinase, L-asparaginase, L-glutaminase, amylase, protease, lipase, cellulase, urease and superoxide dismutase (Burja et al., 2001; Tan, 2007; Abed et al., 2009). Photoproduction of ammonia and amino acids in large amounts by cyanobacteria, which can be harvested continuously over longer periods, has been investigated (Musgrave et al., 1982; Mitsui et al., 1983; Subramanian and Shanmugasundaram, 1986b; Kerby et al., 1989).
Bioprocess Parameters of Production of Cyanobacterial Exopolysaccharide
Published in Gokare A. Ravishankar, Ranga Rao Ambati, Handbook of Algal Technologies and Phytochemicals, 2019
Onkar Nath Tiwari, Sagnik Chakraborty, Indrama Devi, Abhijit Mondal, Biswanath Bhunia, Shen Boxiong
Several genera of cyanobacteria can produce EPSs. They include Anabaena variabilis (Bhatnagar et al. 2012), Nostoc calcicola (Singh & Das 2011), Limnothrix redekei PUPCCC116 (Khattar et al. 2010) and many more.
Physiology of Moss-Bacterial Associations
Published in R. N. Chopra, Satish C. Bhatla, Bryophyte Development: Physiology and Biochemistry, 2019
Luretta D. Spiess, Barbara B. Lippincott, James A. Lippincott
Blue-green algae epiphytic on the leaves of mosses are of importance in nitrogen fixation in the Arctic.62-64 The algae Anabaena variabilis and Nostoc muscorum, growing in association with the moss Funaria hygrometrica, cause rapid growth of the moss and an increase in the number of gametophores, while Funaria in turn has a growth-promoting effect on the cyanobacter. A survey 6 years after the volcanic island Surtsey formed off the coast of Iceland showed that wherever Funaria was found Anabaena colonies were also growing, suggesting some positive interaction between the two plants which could be important to their colonization of the island.65
Preclinical and clinical developments in enzyme-loaded red blood cells: an update
Published in Expert Opinion on Drug Delivery, 2023
Marzia Bianchi, Luigia Rossi, Francesca Pierigè, Sara Biagiotti, Alessandro Bregalda, Filippo Tasini, Mauro Magnani
Phenylketonuria (PKU) is an inborn metabolic disease caused by pathogenic variants in the phenylalanine hydroxylase (PAH) gene resulting in increased blood phenylalanine (Phe) concentrations which are neurotoxic and lead to severe intellectual disability, autistic behavior, seizures, and epilepsy [57]. The management of PKU has been extensively covered in the literature and recent reviews highlight emerging therapies, which could improve patient health, compliance, and quality of life [58,59]. Among these, the enzyme replacement therapy based on recombinant phenylalanine ammonia lyase (rAvPAL) from Anabaena variabilis, catalyzing the deamination of Phe to the nontoxic product trans-cinnamate, plays a leading role. Indeed, pegvaliase (Palynziq®, BioMarin Pharmaceutical Inc., USAA), a PEGylated recombinant PAL, has been approved by FDA (2018) and EMA (2019) for treatment of adult patients.
Phenylketonuria in the adult patient
Published in Expert Opinion on Orphan Drugs, 2019
Leticia Ceberio, Álvaro Hermida, Eva Venegas, Francisco Arrieta, Montserrat Morales, Maria Forga, Montserrat Gonzalo
A promising alternative is based on the enzyme replacement therapy. The enzyme phenylalanine ammonia lyase (PAL), obtained from a recombinant mutant of Anabaena variabilis, converts Phe to ammonia and trans-cinnamic acid, sub-products that are metabolized by the liver and excreted in the urine (Figure 2). Pegvaliase is a pegylated PAL that can be provided daily by subcutaneous self-administration. The formulation with polyethylene glycol (PGE) reduces the immune response against the exogenous enzyme and the associated adverse events. PGE also improves the pharmacodynamic stability of PAL, increasing the enzymatic activity. Pegvaliase has been recently approved by FDA for the treatment of adult patients with PKU who have blood Phe concentrations > 600 µmol/L [54]. To date, results from 7 clinical trials and >350 patients have proved the efficacy and safety of this novel therapy in reducing the plasma Phe levels in adults with PKU. A relatively high risk of anaphylaxis was detected during clinical trials. The reported AEs were mild or moderate and the most common AEs were arthralgia, injection-site reaction and erythema and headache [55]. Long-term clinical trials as well as a phase III trial in Europe are currently ongoing.
Treatment options and dietary supplements for patients with phenylketonuria
Published in Expert Opinion on Orphan Drugs, 2018
Júlio César Rocha, Anita MacDonald
Phenylalanine-ammonia lyase is an enzyme responsible for converting Phe to ammonia and trans-cinnamic acid [122]. The first attempt to use this enzyme in PKU patients was in the late 1980s, when the enzyme was given orally, three times per day, after meals, to an untreated PKU patient for 12 consecutive days. Although only 25% blood Phe decrease was achieved, it was an important observation [123]. In order to improve protease resistance, a recombinant Anabaena variabilis Phenylalanine-Ammonia Lyase was developed from Escherichia coli and PEGylated to reduce immunogenicity (rAvPAL-PEG) [124,125]. Pegvaliase, the PEGylated PAL, is developed as an enzyme substitution therapy to reduce blood Phe concentration in adults with PKU [126].