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Industrial Chemicals: Enzymatic Transformation by Recombinant Microbes
Published in Yoshikatsu Murooka, Tadayuki Imanaka, Recombinant Microbes for Industrial and Agricultural Applications, 2020
Nitrile hydratase (Nilase; EC 4.2.1.84), which is composed of two subunits, a and β, catalyzes the conversion of nitrile compounds to the corresponding amides. The NHases have been discovered in several bacteria, such as Rhodococcus sp. N-774, P. chlororaphis B23, and R. rhodochrous Jl, and some of them are successfully used for industrial production of acrylamide. These NHases show interesting enzymatic characteristics; for example, enzymes from Rhodococcus sp. N-774 and P. chlororaphis B23 contain a nonheme iron and pyrroloquinoline quinone (PQQ) as prosthetic groups, whereas that from R. rhodochrous Jl requires only a cobalt ion for activity. In addition, NHase from strain N-774 requires photoactivation by UV irradiation for its activity [23].
RNA-Seq analysis of Phanerochaete sordida YK-624 degrades neonicotinoid pesticide acetamiprid
Published in Environmental Technology, 2023
Jianqiao Wang, Yilin Liu, Ru Yin, Nana Wang, Tangfu Xiao, Hirofumi Hirai
According to the relevant literature, in the microbial degradation of ACE, only a small number of ACE-degrading enzymes have been identified. Pure nitrile hydratase (NHase) obtained from E. meliloti CGMCC 7333 could degrade 93.9% of ACE in the reaction, and ACE was transformed to IM 1–2 [15]. In addition, a novel amidase, AceAB, was purified from Pigmentiphaga sp. strain D-2; this enzyme played a major role in the hydrolysis of ACE to IM 1–4 [36]. In this study, we did not detect NHase and amidase among the upregulated DEGs. Some genes in the upregulated DEGs were determined to encode oxidoreductases and dehydrogenases based on the Swiss-Prot database. The genes that we obtained under ACE-degrading conditions should be further heterologously expressed to confirm their functions.
A review on bio-functional models of catechol oxidase probed by less explored first row transition metals
Published in Journal of Coordination Chemistry, 2022
Rashmi Rekha Tripathy, Shuvendu Singha, Sohini Sarkar
Before the nineteenth-century cobalt was used as pigment and coloring agent. Cobalt blue, cobalt green and cobalt violet, made with some common inorganic salts of cobalt or mixture of cobalt and other metals, have been used as the artist’s pigments since the middle ages. In modern age, cobalt-based super alloys have found applications in prosthetics and electrochemistry [93,94]. Being a part of vitamin B12 cobalt takes an essential part in metabolism of animals. Nitrile hydratase, prolidase, glucose isomerase, methylmalonyl-CoA carboxytransferase, aldehyde decarbonylase, lysine-2,3-aminomutase, bromoperoxidase and methionine aminopeptidase are examples of cobalt-containing enzymes that are present in various living systems. Recently, some of the cobalt(III) complexes have been found capable of antiviral and antimicrobial activities [95]. Apart from all biological and electrochemical applications, cobalt compounds are quite popular as oxidation catalysts. It can mimic catechol oxidase and act as effective bio-catalysts in catechol oxidation. Just like iron and manganese, varying oxidation states of cobalt (+2 and +3) can catalyze the oxidation with varying mechanisms. Metal centric path [7] and/or ligand centric radical path [41, 54, 68] may be followed during the catalytic cycle.
Streptomyces genus as biotechnological tool for pesticide degradation in polluted systems
Published in Critical Reviews in Environmental Science and Technology, 2018
Gabriela Briceño, María Soledad Fuentes, Juliana María Saez, María Cristina Diez, Claudia Susana Benimeli
Enzyme-based pesticide degradation is an innovative treatment method for the removal of pesticides from polluted environments (Verma et al., 2014). The advantage of enzymatic remediation over microbial treatment include high reaction activity towards recalcitrant pesticides, lower sensitivity to the pesticide concentration, coverage of a wide range of physicochemical gradients in the environment and easy control of field application (Gupta et al., 2015). Microorganisms belonging to Streptomyces genus represent an efficient source of oxidoreductases and hydrolytic enzymes. Amylase, protease, cellulase, xylanase, esterase, nitrile hydratase, laccase, dehydrogenase, and dehalogenase are some of the enzymes that could be involved in pesticides degradation (Karigar & Rao, 2011; Shivlata & Satyanarayana, 2015).