A serine protease from newly isolated Bacillus sp. for efficient silk degumming, sericin degrading and colour bleaching activities

Suwannaphan, Sunisa; Fufeungsombut, Ekkasit; Promboon, Amornrat; Chim-anage, Patoomporn

doi:10.1016/j.ibiod.2016.12.009

Cited by 40 publications

(26 citation statements)

References 40 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Slow-release dosage form preparation containing collagenases with alkaline proteases is extensively used in therapeutic applications. The hydrolysis of collagen by the enzyme liberates low-molecular-weight peptides without any amino acid release for therapeutic use (Romsomsa et al, 2010; Suwannaphan et al, 2017). For the treatment of various diseases, such as burns, carbuncles, furuncles, and wounds, a preparation of elastoterase immobilized on bandage is used (Davidenko, 1999; Palanivel et al, 2013).…”

Section: Medical Fieldmentioning

confidence: 99%

Microbial Proteases Applications

Razzaq

Shamsi

Ali³

et al. 2019

Front. Bioeng. Biotechnol.

423

195

View full text Add to dashboard Cite

The use of chemicals around the globe in different industries has increased tremendously, affecting the health of people. The modern world intends to replace these noxious chemicals with environmental friendly products for the betterment of life on the planet. Establishing enzymatic processes in spite of chemical processes has been a prime objective of scientists. Various enzymes, specifically microbial proteases, are the most essentially used in different corporate sectors, such as textile, detergent, leather, feed, waste, and others. Proteases with respect to physiological and commercial roles hold a pivotal position. As they are performing synthetic and degradative functions, proteases are found ubiquitously, such as in plants, animals, and microbes. Among different producers of proteases, Bacillus sp. are mostly commercially exploited microbes for proteases. Proteases are successfully considered as an alternative to chemicals and an eco-friendly indicator for nature or the surroundings. The evolutionary relationship among acidic, neutral, and alkaline proteases has been analyzed based on their protein sequences, but there remains a lack of information that regulates the diversity in their specificity. Researchers are looking for microbial proteases as they can tolerate harsh conditions, ways to prevent autoproteolytic activity, stability in optimum pH, and substrate specificity. The current review focuses on the comparison among different proteases and the current problems faced during production and application at the industrial level. Deciphering these issues would enable us to promote microbial proteases economically and commercially around the world.

show abstract

Section: Medical Fieldmentioning

confidence: 99%

Microbial Proteases Applications

Razzaq

Shamsi

Ali³

et al. 2019

Front. Bioeng. Biotechnol.

423

195

View full text Add to dashboard Cite

show abstract

“…The enzymatic treatment of silk has received remarkable attention as an alternative for degumming because it is performed by applying proteolytic enzymes that selectively react with only specific parts of the silk to destroy the unwanted sericin and causes little hydrolytic damage to fibroin [ 25 ]. Alkaline proteases are considerable degumming reagents owing to their activity and stability under alkaline conditions where they can readily break the sericin chains and produce a higher degumming efficiency for silk [ 26 ]. In a previous study, silk fabric was treated with alkaline proteases 3374-L and GC 897-H derived from genetically modified Bacillus subtilis at pH 10 for 30 min; the degumming ratio was approximately 25% and 22% for the two proteases, respectively, which is close to the results of soap-alkali degumming [ 27 , 28 ].…”

Section: Introductionmentioning

confidence: 99%

High Molecular Weight Silk Fibroin Prepared by Papain Degumming

et al. 2020

View full text Add to dashboard Cite

A major challenge for the silk textile industry and for the process of silk-based biomaterials is to find a degumming method that can completely remove sericin while avoiding obvious hydrolysis damage to the silk fibroin. In this study, papain was used to degum Bombyx mori silk fibers under nearly neutral conditions based on the specificity of papain to sericin. The degumming efficiency was investigated, as well as the mechanical properties and molecular weight of the sericin-free silk fibroin. The results indicated that increasing the papain concentration aided in sericin removal, as the concentration increased to 3.0 g/L, the degummed fibers showed a clean, smooth surface morphology and exhibited a yellow color when stained by picric acid and carmine, confirming the complete removal of sericin from silk fibroin. Furthermore, an analysis of the amino acid composition indicated that the silk fibroin suffered less damage because papain specifically cleaved the binding sites between L-arginine or L-lysine residue and another amino acid residue in sericin, leading to a significantly higher molecular weight and improved tensile strength compared to traditional sodium carbonate degumming. This study provides a novel degumming method which cannot only completely remove sericin, but also maintain the original strong mechanical properties and high molecular weight of silk fibroin.

show abstract

“…The activity of a serine protease isolated from Bacillus spp. was reported to be inhibited by both PMSF and EDTA . A serine metalloprotease purified from B. subtilis C142 was inhibited by multiple inhibitors including PMSF and EDTA …”

Section: Discussionmentioning

confidence: 99%

Purification and characterization of the thermostable protease produced by Serratia grimesii isolated from channel catfish

et al. 2018

View full text Add to dashboard Cite

BACKGROUND: Microbial spoilage of fishery products accounts for significant financial losses, yearly on a global scale. Psychrotrophic spoilage bacteria often secrete extracellular enzymes to break down surrounding fish tissue, rendering the product unsuitable for human consumption. For a better understanding of bacterial spoilage due to enzymatic digestion of fish products, proteases in Serratia grimesii isolated from North American catfish fillets (Ictalurus punctatus) were investigated. RESULTS: Mass spectrometric evidence demonstrated that S. grimesii secretes two distinct extracellular proteases and one lipase.Protease secretion displayed broad thermostability in the 30-90 ∘ C range. The major protease-secretion (O-1) was most active under alkaline conditions and utilized manganese as a co-factor. Organic solvents significantly disrupted the efficacy of S. grimesii extracellular enzymes and, in a series of bactericidal detergents, protease activity was highest when treated with Triton X-100. Ethylenediaminetetraacetic acid (EDTA) and phenylmethylsulfonyl fluoride (PMSF) significantly inhibited the enzyme activity, while protease was moderately stable under freeze-thaw and refrigerated storage. CONCLUSION: The influence of fish spoilage-related enzymes, depending on various factors, is discussed in this paper. This study will provide new insight into enzymatic spoilage and its control, which can be exploited to enhance food safety and the shelf-life of fishery products worldwide.

show abstract

A serine protease from newly isolated Bacillus sp. for efficient silk degumming, sericin degrading and colour bleaching activities

Cited by 40 publications

References 40 publications

Microbial Proteases Applications

Microbial Proteases Applications

High Molecular Weight Silk Fibroin Prepared by Papain Degumming

Purification and characterization of the thermostable protease produced by Serratia grimesii isolated from channel catfish

Contact Info

Product

Resources

About