Efficient enzyme-catalyzed synthesis of peptide secondary amides for use as serine proteinase inhibitors

Sergeev, Maxim; Voyushina, Tatiana L.; Sergeeva, Olga A.; Belozerskaya, G.G.

doi:10.1016/j.molcatb.2012.04.019

Cited by 2 publications

(2 citation statements)

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“…Proteinase K from Parengyodontium album is also observed to facilitate feather degradation, a useful quality for waste management application. 70 Subtilisin can also be used to degrade proteinaceous recalcitrant solid fish biowastes, which are abundant in nature and largely generated by fisheries-processing industry, which is a known environmental concern, by converting them into products like protein hydrolysates and chitinous materials that could be used in other industries. This is proven with a study conducted by Mechri et al, 72 in which they used a recently discovered thermostable and halotolerant subtilisin SAPN isolated from Melghiribacillus thermohalophilus Nari2A T to extract chitin from crab and shrimp shell by-products.…”

Section: Waste Managementmentioning

confidence: 99%

“…in 2020, demonstrates efficient hydrolytic activity on soluble keratin released from chicken feathers and when the substrate‐binding site of protease Als is substituted with binding site of homologous protease C2 from the same strain, efficient hydrolytic activity on insoluble keratin substrates is observed. Proteinase K from Parengyodontium album is also observed to facilitate feather degradation, a useful quality for waste management application 70 …”

Section: Versatile Applications Of Subtilisinmentioning

confidence: 99%

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Versatility of subtilisin: A review on structure, characteristics, and applications

Azrin

Ali

Rahman

et al. 2022

Biotech and App Biochem

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Due to its thermostability and high pH compatibility, subtilisin is most known for its role as an additive for detergents in which it is categorized as a serine protease according to MEROPS database. Subtilisin is typically isolated from various bacterial species of the Bacillus genus such as Bacillus subtilis, B. amyloliquefaciens, B. licheniformis, and various other organisms. It is composed of 268-275 amino acid residues and is initially secreted in the precursor form, preprosubtilisin, which is composed of 29-residues signal peptide, 77-residues propeptide, and 275-residues active subtilisin. Subtilisin is known for the presence of high and low affinity calcium binding sites in its structure. Native subtilisin has general properties of thermostability, tolerance to neutral to high pH, broad specificity, and calcium-dependent stability, which contribute to the versatility of subtilisin applicability. Through protein engineering and immobilization technologies, many variants of subtilisin have been generated, which increase the applicability of subtilisin in various industries including detergent, food processing and packaging, synthesis of inhibitory peptides, therapeutic, and waste management applications.

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Section: Waste Managementmentioning

confidence: 99%

Section: Versatile Applications Of Subtilisinmentioning

confidence: 99%