Optimization of protease production by Bacillus cereus HMRSC30 for simultaneous extraction of chitin from shrimp shell with value-added recovered products

2021 ◽  
Author(s):  
Hilmi Amanah Aditya Cahyaningtyas ◽  
Wasana Suyotha ◽  
Benjamas Cheirsilp ◽  
Asep Awaludin Prihanto ◽  
Shigekazu Yano ◽  
...  
Keyword(s):  
Bacillus Cereus ◽  
Value Added ◽  
Protease Production ◽  
Simultaneous Extraction ◽  
Shrimp Shell

scholarly journals Upcycling chitin-containing waste into organonitrogen chemicals via an integrated process

2020 ◽  
Vol 117 (14) ◽  
pp. 7719-7728 ◽  
Author(s):  
Xiaoqiang Ma ◽  
Gökalp Gözaydın ◽  
Huiying Yang ◽  
Wenbo Ning ◽  
Xi Han ◽  
...  
Keyword(s):  
Wide Spectrum ◽  
Value Added ◽  
Direct Conversion ◽  
Water Soluble ◽  
Integrated Biorefinery ◽  
E Coli ◽  
Shrimp Shell ◽  
Shell Waste ◽  
Shrimp Shell Waste ◽  
Value Added Products

Chitin is the most abundant renewable nitrogenous material on earth and is accessible to humans in the form of crustacean shell waste. Such waste has been severely underutilized, resulting in both resource wastage and disposal issues. Upcycling chitin-containing waste into value-added products is an attractive solution. However, the direct conversion of crustacean shell waste-derived chitin into a wide spectrum of nitrogen-containing chemicals (NCCs) is challenging via conventional catalytic processes. To address this challenge, in this study, we developed an integrated biorefinery process to upgrade shell waste-derived chitin into two aromatic NCCs that currently cannot be synthesized from chitin via any chemical process (tyrosine andl-DOPA). The process involves a pretreatment of chitin-containing shell waste and an enzymatic/fermentative bioprocess using metabolically engineeredEscherichia coli. The pretreatment step achieved an almost 100% recovery and partial depolymerization of chitin from shrimp shell waste (SSW), thereby offering water-soluble chitin hydrolysates for the downstream microbial process under mild conditions. The engineeredE. colistrains produced 0.91 g/L tyrosine or 0.41 g/Ll-DOPA from 22.5 g/L unpurified SSW-derived chitin hydrolysates, demonstrating the feasibility of upcycling renewable chitin-containing waste into value-added NCCs via this integrated biorefinery, which bypassed the Haber–Bosch process in providing a nitrogen source.

scholarly journals A cell-cell communication system regulates protease production during sporulation in bacteria of the Bacillus cereus group

2011 ◽  
Vol 82 (3) ◽  
pp. 619-633 ◽  
Author(s):  
Stéphane Perchat ◽  
Thomas Dubois ◽  
Samira Zouhir ◽  
Myriam Gominet ◽  
Sandrine Poncet ◽  
...  
Keyword(s):  
Bacillus Cereus ◽  
Communication System ◽  
Cell Communication ◽  
Protease Production ◽  
Bacillus Cereus Group ◽  
A Cell ◽  
Cell Cell

scholarly journals Thrombolytic Potential of Novel Thiol-Dependent Fibrinolytic Protease from Bacillus cereus RSA1

Biomolecules ◽  
2019 ◽  
Vol 10 (1) ◽  
pp. 3 ◽  
Author(s):  
Chhavi Sharma ◽  
Gad Elsayed Mohamed Salem ◽  
Neha Sharma ◽  
Prerna Gautam ◽  
Rajni Singh
Keyword(s):  
Bacillus Cereus ◽  
Fibrinolytic Activity ◽  
Thrombolytic Agent ◽  
Divalent Cations ◽  
Blood Clot ◽  
Fold Increase ◽  
Protease Production ◽  
Stability Range ◽  
Stain Removal

The present study demonstrates the production and thrombolytic potential of a novel thermostable thiol-dependent fibrinolytic protease by Bacillus cereus RSA1. Statistical optimization of different parameters was accomplished with Plackett–Burman design and validated further by central composite design with 30.75 U/mL protease production. Precipitation and chromatographic approaches resulted in 33.11% recovery with 2.32-fold purification. The molecular weight of fibrinolytic protease was 40 KDa and it exhibited a broad temperature and pH stability range of 20–80 °C and pH 5–10 with utmost activity at 50 °C and pH 8, respectively. The protease retained its fibrinolytic activity in organic solvents and enhanced the activity in solutions with divalent cations (Mn2+, Zn2+, and Cu2+). The enzyme kinetics revealed Km and Vmax values of 1.093 mg/mL and 52.39 µg/mL/min, respectively, indicating higher affinity of fibrinolytic activity towards fibrin. Also, complete inhibition of fibrinolytic activity with DFP and a 2-fold increase with DTT and β-mercaptoethanol indicates its thiol-dependent serine protease nature. MALDI–TOF analysis showed 56% amino acid sequence homology with Subtilisin NAT OS = Bacillus subtilis subsp. natto. The fibrinolysis activity was compared with a commercial thrombolytic agent for its therapeutic applicability, and fibrinolytic protease was found highly significant with absolute blood clot dissolution within 4 h in in vitro conditions. The isolated fibrinolytic protease of Bacillus cereus RSA1 is novel and different from other known fibrinolytic proteases with high stability and efficacy, which might have wide medicinal and industrial application as a thrombolytic agent and in blood stain removal, respectively.

scholarly journals Regulation of Extracellular Protease Production in Bacillus cereus

1967 ◽  
Vol 93 (3) ◽  
pp. 1023-1030 ◽  
Author(s):  
Sharon Levisohn ◽  
Arthur I. Aronson
Keyword(s):  
Bacillus Cereus ◽  
Extracellular Protease ◽  
Protease Production

scholarly journals Fish Waste-Potential Low Cost Substrate for Bacterial Protease Production: A Brief Review

2016 ◽  
Vol 10 (1) ◽  
pp. 335-341 ◽  
Author(s):  
Aishwarya Ramkumar ◽  
Nallusamy Sivakumar ◽  
Reginald Victor
Keyword(s):  
Low Cost ◽  
Value Added ◽  
Protease Production ◽  
Industrial Biotechnology ◽  
Fish Waste ◽  
Environment And Health ◽  
Protease Enzyme ◽  
The Rich ◽  
The Cost ◽  
Value Added Products

Industrial biotechnology processes have recently been exploited for an economic utilization of wastes to produce value added products. Of which, fish waste is one of the rich sources of proteins that can be utilized as low cost substrates for microbial enzyme production. Fish heads, tails, fins, viscera and the chitinous materials make up the wastes from fish industries. Processing these wastes for the production of commercial value added products could result in a decrease in the cost of production. In addition, we can eliminate the pollution of the environment and health issues due to the improper disposal of these fish wastes. This review highlights the potential use of fish waste as a cheaper substrate for the production of economically important protease enzyme.

scholarly journals Novel recombinant keratin degrading subtilisin like serine alkaline protease from Bacillus cereus isolated from marine hydrothermal vent crabs

2021 ◽  
Vol 11 (1) ◽  
Author(s):  
Revathi Gurunathan ◽  
Bin Huang ◽  
Vinoth Kumar Ponnusamy ◽  
Jiang-Shiou Hwang ◽  
Hans-Uwe Dahms
Keyword(s):  
Bacillus Cereus ◽  
Hydrothermal Vents ◽  
Extreme Environments ◽  
Serine Proteinase ◽  
Value Added ◽  
Hydrolytic Activity ◽  
Industrial Applications ◽  
Protease Gene ◽  
Hydrolytic Activities ◽  
Promising Source

AbstractMicrobial secondary metabolites from extreme environments like hydrothermal vents are a promising source for industrial applications. In our study the protease gene from Bacillus cereus obtained from shallow marine hydrothermal vents in the East China Sea was cloned, expressed and purified. The protein sequence of 38 kDa protease SLSP-k was retrieved from mass spectrometry and identified as a subtilisin serine proteinase. The novel SLSP-k is a monomeric protein with 38 amino acid signal peptides being active over wide pH (7–11) and temperature (40–80 °C) ranges, with maximal hydrolytic activities at pH 10 and at 50 °C temperature. The hydrolytic activity is stimulated by Ca2+, Co2+, Mn2+, and DTT. It is inhibited by Fe2+, Cd2+, Cu2+, EDTA, and PMSF. The SLSP-k is stable in anionic, non-anionic detergents, and solvents. The ability to degrade keratin in chicken feather and hair indicates that this enzyme is suitable for the degradation of poultry waste without the loss of nutritionally essential amino acids which otherwise are lost in hydrothermal processing. Therefore, the proteinase is efficient in environmental friendly bioconversion of animal waste into fertilizers or value added products such as secondary animal feedstuffs.

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