#proteases

Fragmented Healing

An infection settling into a wound is like being kicked when you’re down. Infections make a bad situation worse, with microorganisms capitalising on a rare opportunity to slip past our protective skin, delaying healing and potentially leading to more serious problems. A new study aiming to characterise infected wounds in order to better predict and prevent them analysed the proteins found at healing and infected wound sites. During infection, bacteria provide their own protein-degrading enzymes which act alongside the body’s, so the resulting mix of protein fragments (peptides) is different. Analysing this mass of protein rubble revealed 150 peptides unique to infected wounds (pictured, with Staphylococcus aureus bacteria coloured yellow) and 90 found only in healing wounds, including some with antimicrobial properties. The researchers suggest that checking the protein fragments in wounds might help monitor healing, spot infection before symptoms show, and prevent bacteria rubbing salt in the wound.

Written by Anthony Lewis

Image by Mariena van der Plas and Matthias Mörgelin

Division of Dermatology and Venereology, Department of Clinical Sciences, Lund University, Lund, Sweden

Image originally published with a Creative Commons Attribution 4.0 International (CC BY 4.0)

Research published in eLife, July 2021

Host cell proteases can process viral capsid proteins — ScienceDaily

It has long been suggested that a cell protease could take part in enterovirus infection. However, the identity of such proteases have remained unknown. The work performed in the University of Jyväskylä shows, for the first time, that host cell calpain proteases can process enterovirus polyprotein in vitro. The research was published in Viruses scientific journal in November 2019.

Enteroviruses…

Proteases are the foremost important hydrolytic enzyme that plays a vital role in the metabolism and physiological activities of every organism. There is an increasing demand for protease enzyme worldwide. An extracellular protease producing strain was isolated from the gut of Portunus pelagicus and was identified as Bacillus subtilis. The stability of crude protease in various solid laundry detergents was investigated. The enzyme had an optimum activity at pH 9.0-10.0 and temperature 55-60°C. The protease was found to be stable towards non-ionic (Triton X-100, Tween 20, Tween 80, Brij 35) and ionic detergents (0.1% SDS) and were relatively stable in bleaching agents such as 1% H2O2 and 1% sodium perborate which retained 74% and 63% of their initial activity respectively. Except for acetone, all other organic solvents showed more than 70% of total activity in 10% of solvents (methanol, 2-propanol, xylene, toluene, and benzene). Moreover, the alkaline crude enzyme extract showed its stability and compatibility with commercial solid detergents. Wash performance analysis, stability in pH, temperature, thermal stability and the stability in the presence of surfactants, bleaching agents and organic solvents, suggest its application as a laundry additive.

Proteases are the foremost important hydrolytic enzyme that plays a vital role in the metabolism and physiological activities of every organism. There is an increasing demand for protease enzyme worldwide. An extracellular protease producing strain was isolated from the gut of Portunus pelagicus and was identified as Bacillus subtilis. The stability of crude protease in various solid laundry detergents was investigated. The enzyme had an optimum activity at pH 9.0-10.0 and temperature 55-60°C. The protease was found to be stable towards non-ionic (Triton X-100, Tween 20, Tween 80, Brij 35) and ionic detergents (0.1% SDS) and were relatively stable in bleaching agents such as 1% H2O2 and 1% sodium perborate which retained 74% and 63% of their initial activity respectively. Except for acetone, all other organic solvents showed more than 70% of total activity in 10% of solvents (methanol, 2-propanol, xylene, toluene, and benzene). Moreover, the alkaline crude enzyme extract showed its stability and compatibility with commercial solid detergents. Wash performance analysis, stability in pH, temperature, thermal stability and the stability in the presence of surfactants, bleaching agents and organic solvents, suggest its application as a laundry additive.

Proteases are the foremost important hydrolytic enzyme that plays a vital role in the metabolism and physiological activities of every organism. There is an increasing demand for protease enzyme worldwide. An extracellular protease producing strain was isolated from the gut of Portunus pelagicus and was identified as Bacillus subtilis. The stability of crude protease in various solid laundry detergents was investigated. The enzyme had an optimum activity at pH 9.0-10.0 and temperature 55-60°C. The protease was found to be stable towards non-ionic (Triton X-100, Tween 20, Tween 80, Brij 35) and ionic detergents (0.1% SDS) and were relatively stable in bleaching agents such as 1% H2O2 and 1% sodium perborate which retained 74% and 63% of their initial activity respectively. Except for acetone, all other organic solvents showed more than 70% of total activity in 10% of solvents (methanol, 2-propanol, xylene, toluene, and benzene). Moreover, the alkaline crude enzyme extract showed its stability and compatibility with commercial solid detergents. Wash performance analysis, stability in pH, temperature, thermal stability and the stability in the presence of surfactants, bleaching agents and organic solvents, suggest its application as a laundry additive.

The Global Proteases Market Study that gives a meticulous investigation of the current scenario of the market size, share, demand, growth, trends, and forecast in the coming years. The report firstly introduced the Proteases Market basics: definitions, classifications, applications and market overview; product specifications; manufacturing processes; cost structures, raw materials and so on. Then it analyzed the world main region market conditions, including the product price, profit, capacity, production, supply, demand and market growth rate and forecast etc. GET THE INSIDE SCOOP OF THE SAMPLE REPORT @[click here] The research study gives a complete list of all the leading players working in the Global Proteases Market. Moreover, the financial status, company profiles, business strategies and policies, along with the latest expansions in the worldwide market have been mentioned in the research study. Research objectives: • To study and analyze the Global Proteases market size by key regions/countries, product type and application, history data from 2012 to 2019, and forecast to 2024. • To understand the structure of Proteases Market by identifying its various sub-segments. • Focuses on the key Global Proteases Market players, to define, describe and analyze the value, market share, market competition landscape, SWOT analysis and development plans in next few years. • To analyze the Proteases Market with respect to individual growth trends, future prospects, and their contribution to the total market. • To share detailed information about the key factors influencing the growth of the market (growth potential, opportunities, drivers, industry-specific challenges and risks). • To project the size of Proteases Market, with respect to key regions, type 

Market Players: Novozymes A/S, Chr. Hansen Holdings A/S, E. I. Du Pont De Nemours and Company, Associated British Foods PLC, Koninklijke DSM N.V., Advanced Enzyme Technologies Ltd., Dyadic International Incorporated, Amano Enzyme Inc., Biocatalysts Limited, Specialty Enzymes & Biotechnologies By Source Animal Sources, Plant Sources, Microbial Sources By Product: Animal Product, Plant, Microbial By Method of Production Fermentation, Extraction, By Formulation Liquid Formulations, Lyophilized Powder, Others, Application, Food & Beverages, Feed, Soap & Detergent Industry By Pharmaceuticals Others • To analyze competitive developments such as expansions, agreements, new product launches and acquisitions in the market. READ DETAILED INDEX OF FULL RESEARCH STUDY AT @ [click here]