Fungal Proteases: Current and Potential Industrial Applications

Patyshakuliyeva, Aleksandrina

doi:10.1016/b978-0-12-819990-9.00025-1

Cited by 2 publications

(8 citation statements)

References 161 publications

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“…Most reported serine S8 family proteases from fungi, such as Trametes cingulate (pH 9.0) and Aspergillus clavatus ES1 (pH 8.5), have a similar optimal pH. Th APT3 has a wide range of pH stability from pH 4.0–11.0 (Figure S3c), which is superior to that of numerous proteases from fungal sources . The T opt of purified Th APT3 was 60 °C (Figure S3b), but the T opt of several other fungal proteases has been reported to be <50 °C …”

Section: Resultsmentioning

confidence: 95%

“…To comprehensively consider the commercial value of the triple-superposition mutant Th APT3-M9, the commercial protease ProK was measured simultaneously. ProK is currently the most widely used fungus-derived serine protease. , Recombinant Th APT3-M9 was more thermostable than the commercial ProK. The t 1/2 of commercial Prok at 55 °C was 34.7 min, whereas Th APT3-M9 extended to 178.4 min (approximately 5-fold) (Figure c and Table ).…”

Section: Resultsmentioning

confidence: 95%

“…The complete amino acid sequence of the protease Th APT3 consisted of 387 amino acids (Figure S2). The pre- Th APT3 shares a high identity (65.27%) with proteinase K (ProK) from Parengyodontium album (P06873.2), which is the most commercially successful protease derived from fungi among the S8 family proteases . As predicted by the SignalP 4.1 server, the first 15 amino acids (M-106–A-92) at the N-terminus constitute the signal peptide for Th APT3.…”

Section: Resultsmentioning

confidence: 99%

“…ThAPT3 has a wide range of pH stability from pH 4.0−11.0 (Figure S3c), which is superior to that of numerous proteases from fungal sources. 22 The T opt of purified ThAPT3 was 60 °C (Figure S3b), but the T opt of several other fungal proteases has been reported to be <50 °C. 22 ThAPT3 was stable at 50 °C; when incubated at 50 °C for 1 h, it retained >65% activity (Figure S3d).…”

Section: Preparation Of Recombinantmentioning

confidence: 98%

“…The pre-ThAPT3 shares a high identity (65.27%) with proteinase K (ProK) from Parengyodontium album (P06873.2), which is the most commercially successful protease derived from fungi among the S8 family proteases. 22 As predicted by the SignalP 4.1 server, the first 15 amino acids (M-106−A-92) at the N-terminus constitute the signal peptide for ThAPT3. The subsequent 91 amino acids (A-91−N-1) formed a propeptide, which was predicted by multiple sequence alignments and identified by N-terminal sequencing.…”

Section: Preparation Of Recombinantmentioning

confidence: 99%

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Improving the Activity and Stability of Serine Protease ThAPT3 by Alleviating Self-Cleavage and Its Application in Deproteinization of Shrimp Shells

Wang

Dong

Zhou

et al. 2023

J. Agric. Food Chem.

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The self-cleavage properties of proteases result in low activity and instability, which limit their industrial application. In this study, the serine protease ThAPT3 from Torrubiella hemipterigena was successfully expressed in Komagataella phaffii. We investigated the self-degradation mechanism of ThAPT3 and presented a rational strategy to alleviate self-cleavage. A major selfdegradation site (Leu 238 -Met 239 ) and a primary autolysis region were identified. The autolysis regions (loop 18 , α 8 -helix, and loop 19 ) were redesigned and optimized using loop transplantation, energy calculations, surface cavity optimization, and loop anchoring. A triple-superposition mutant, ThAPT3-M9 (M 239 GKDGAVAAGLC 250 → M 239 TLNRTTAANAC 250 /A251E/A254Q/R259L/ A267E/S280N), was obtained. Compared to the wild type, the autolysis of M9 was significantly alleviated, and its half-life at 60 °C was increased approximately 39-fold (from 1.6 to 62.4 min). The optimal temperature and specific activity of M9 increased by 5 °C (from 60 to 65 °C) and 62% (4985 vs 3078 U/mg), respectively. M9 showed significant advantages in shrimp shell deproteinization.

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Section: Resultsmentioning

confidence: 95%

Section: Resultsmentioning

confidence: 95%

Section: Resultsmentioning

confidence: 99%

Section: Preparation Of Recombinantmentioning

confidence: 98%

Section: Preparation Of Recombinantmentioning

confidence: 99%

See 3 more Smart Citations

Improving the Activity and Stability of Serine Protease ThAPT3 by Alleviating Self-Cleavage and Its Application in Deproteinization of Shrimp Shells

Wang

Dong

Zhou

et al. 2023

J. Agric. Food Chem.

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Microbial proteases and their applications

Song,

Zhang,

Wang

et al. 2023

Front. Microbiol.

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Proteases (proteinases or peptidases) are a class of hydrolases that cleave peptide chains in proteins. Endopeptidases are a type of protease that hydrolyze the internal peptide bonds of proteins, forming shorter peptides; exopeptidases hydrolyze the terminal peptide bonds from the C-terminal or N-terminal, forming free amino acids. Microbial proteases are a popular instrument in many industrial applications. In this review, the classification, detection, identification, and sources of microbial proteases are systematically introduced, as well as their applications in food, detergents, waste treatment, and biotechnology processes in the industry fields. In addition, recent studies on techniques used to express heterologous microbial proteases are summarized to describe the process of studying proteases. Finally, future developmental trends for microbial proteases are discussed.

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Fungal Proteases: Current and Potential Industrial Applications

Cited by 2 publications

References 161 publications

Improving the Activity and Stability of Serine Protease ThAPT3 by Alleviating Self-Cleavage and Its Application in Deproteinization of Shrimp Shells

Improving the Activity and Stability of Serine Protease ThAPT3 by Alleviating Self-Cleavage and Its Application in Deproteinization of Shrimp Shells

Microbial proteases and their applications

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