Extraction and characterization of alkaline protease from Streptomyces sp. GS-1 and its application as dehairing agent

Sarkar, Gargi; Suthindhiran, K.

doi:10.1016/j.bcab.2020.101590

Cited by 28 publications

(10 citation statements)

References 44 publications

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“…RM4, 60 and Streptomyces sp. GS‐1 61 have been used as a dehairing agent. Hence, the use of immobilized protein potentially improved the gelatinase and dehairing activities of alkaline protease.…”

Section: Discussionmentioning

confidence: 99%

Expression and immobilization of trypsin‐like domain of serine protease from Pseudomonas aeruginosa for improved stability and catalytic activity

et al. 2022

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Protein engineering and enzyme immobilization strategies have produced numerous biocatalysts for modern industrial applications. In this study, we have also used these two strategies for improving the operational stability and catalytic efficiency of serine protease from Pseudomonas aeruginosa. The enzyme serine protease was truncated to separate its trypsin‐like domain from the PDZ1 and PDZ2 domains. The truncated trypsin‐like domain was expressed in Escherichia coli BL21, and its catalytic activity and thermostability were estimated. Later this trypsin‐like domain was immobilized with 2% Na‐alginate. The immobilized domain showed 10°C increase in optimum temperature compared to its free counterpart. Kinetic studies showed two‐folds increased Vmax of the immobilized domain. Likewise, the Km value of this domain was 11.5 folds lower compared to the free trypsin‐like domain. The catalytic efficiency (Kcat/Km) of the immobilized enzyme also elevated to 311 folds. Additionally, the immobilized trypsin‐like domain remained active in the presence of surfactants (Triton‐X 100, SDS, and Tween‐40) and metal ions (Mg2+, Ca2+, Na+, and Zn2+). It also efficiently removes gelatin layer from X‐ray film and hair from sheepskin. Thus, the immobilized trypsin‐like domain of serine protease, with increased thermostability and catalytic efficiency, is operationally more stable than the soluble truncated trypsin‐like domain.

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Section: Discussionmentioning

confidence: 99%

Expression and immobilization of trypsin‐like domain of serine protease from Pseudomonas aeruginosa for improved stability and catalytic activity

et al. 2022

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“…Distinct actinomycetes colonies were isolated and frequently subcultured till pure cultures were obtained. 16 The cultures were maintained on starch casein agar plates and incubated at 28-30 °C for 7-10 day.…”

Section: Isolation Of Streptomyces Sp Lcj1amentioning

confidence: 99%

Optimization of Protease Production by Streptomyces SP. LCJ1A Using Response Surface Methodology

Swarna¹,

Gnanadoss²

2022

Int J Life Sci Pharm Res

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Protease is an industrially important enzyme obtained from plants and animals. Production of high amounts of protease at low cost is necessary for its use in different commercial applications. The main objective of this work was to formulate a suitable medium and to optimize various parameters for protease production by Streptomyces sp. LCJ1A which was isolated from Pichavaram mangroves, Tamil Nadu, India. The organism was quantitatively and qualitatively screened for protease production. Sequencing of 16S rRNA was done and the sequence was deposited in NCBI and Accession no. KU 870428 was obtained. For optimization, the conventional one-time factor method followed by the Plackett-Burman design was used to optimize various media components. Variables with a significant influence on the production of protease have been identified. Variables such as maltose, peptone, pH and temperature have shown its strong impact on protease production and the ideal concentration of these factors was further investigated by Response Surface Methodology. The Optimum values of tested variables for favourable protease production were: Maltose, peptone, pH and temperature. Further, the interaction effects of maltose and peptone were found to be extremely important suggesting that both components were extremely crucial for protease production. 186.92 U/mL of protease enzyme was obtained in the experimental study which was close to the predicted value of 190.67 U/mL, which could validate the model. Using such optimized variables, the protease production was increased by 10 times when compared with the unoptimized medium. This is the first report on the conventional and statistical optimization of protease production from Streptomyces sp. LCJ1A. This study also showed that statistical methods are indeed a better approach for optimization of media, when compared with conventional one- factor-at-a-time method in terms of an enhanced protease yield in a short time

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“…Indeed, the addition of EDTA could inhibit all proteolytic bands of the crude-enzyme cocktail (Figure S3). Notably, most proteases from the Streptomyces genus generally belong to the serine protease group [11,31,33,38], and only a few enzymes are metalloproteases [38]. Finally, the addition of 2-ME (2-mercaptoethanol), a reducing agent, only caused partial inhibition of the activity of S. speibonae TKU048 s crude-enzyme cocktail (63.60% ± 3.60%).…”

Section: The Characterization Of Crude-enzyme Cocktailmentioning

confidence: 99%

Conversion of Fishery Waste to Proteases by Streptomyces speibonae and Their Application in Antioxidant Preparation

Tran

Doan

Nguyen

et al. 2022

Fishes

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Proteinaceous wastes from the fishery process are an abundant renewable resource for the recovery of a variety of high-value products. This work attempted to utilize several proteinaceous wastes to produce proteases using the Streptomyces speibonae TKU048 strain. Among different possible carbon and nitrogen sources, the protease productive activity of S. speibonae TKU048 was optimal on 1% tuna head powder. Further, the casein/gelatin/tuna head powder zymography of the crude enzyme revealed the presence of three/nine/six proteases, respectively. The crude-enzyme cocktail of S. speibonae TKU048 exhibited the best proteolytic activity at 70 °C and pH = 5.8. Sodium dodecyl sulfate strongly enhanced the proteolytic activity of the cocktail, whereas FeCl3, CuSO4, and ethylenediaminetetraacetic acid could completely inhibit the enzyme activity. Additionally, the crude-enzyme cocktail of S. speibonae TKU048 could efficiently enhance the 2,2-diphenyl-1-picrylhydrazyl and 2,2′-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) radical scavenging activities of all tested proteinaceous materials including the head, viscera, and meat of tuna fish; the head, viscera, and meat of tilapia fish; the head, meat, and shell of shrimp; squid pen; crab shell; and soybean. Taken together, S. speibonae TKU048 revealed potential in the reclamation of proteinaceous wastes for protease production and antioxidant preparation.

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Extraction and characterization of alkaline protease from Streptomyces sp. GS-1 and its application as dehairing agent

Cited by 28 publications

References 44 publications

Expression and immobilization of trypsin‐like domain of serine protease from Pseudomonas aeruginosa for improved stability and catalytic activity

Expression and immobilization of trypsin‐like domain of serine protease from Pseudomonas aeruginosa for improved stability and catalytic activity

Optimization of Protease Production by Streptomyces SP. LCJ1A Using Response Surface Methodology

Conversion of Fishery Waste to Proteases by Streptomyces speibonae and Their Application in Antioxidant Preparation

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