The production of extracellular inhibitors of papain and trypsin by Streptomyces sp. 22 was studied under different cultural conditions including complex and defined media, temperatures ranging from 18 degrees C to 37 degrees C and a variety of sole carbon and nitrogen sources. In complex nutritionally rich medium, maximal specific growth rates were obtained at 37 degrees C, whereas the highest specific production rates for both papain and trypsin inhibitors were registered at 18 degrees C. Studies on the effect of different carbon and nitrogen sources in defined media underline the importance of the nitrogen source as a strong regulator of the biosynthesis of both inhibitors. Enhanced formation of the inhibitory compounds occurred in the presence of casein. The dynamics of the formation of both inhibitors in defined media showed close association with growth. However, a partial separation of production phases for papain and trypsin inhibitors was observed in complex medium. The results imply differences in the regulation of biosynthesis of the two inhibitors.
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http://dx.doi.org/10.1007/BF00170634 | DOI Listing |
Food Res Int
February 2025
College of Food Science and Engineering, Yangzhou University, Yangzhou, Jiangsu 225127, China. Electronic address:
Effects of enzymolysis by seven proteases (Alcalase, Bromelain, Flavourzyme, Papain, Pepsin, Protamex, and Trypsin) with distinct cleavage specificities on the emulsification performance of hempseed protein (HPI) and its correlation with the structural and interfacial characteristics were explored in this study. Upon enzymolysis, a remarkable decrease in α-helix and β-turn was observed in resultant hydrolysates (HPH), accompanied by a rise in β-sheet and random coil, notably by Alcalase, Bromelain, Papain, and Trypsin. Overall, proteolysis led to noticeable reductions in surface hydrophobicity and total sulfhydryls as well as a redshift in intrinsic fluorescence, with Papain showing the most pronounced effects, possibly due to its higher hydrolysis degree (4.
View Article and Find Full Text PDFAAPS J
January 2025
Shanghai Institute of Materia Medica, Chinese Academy of Sciences, Shanghai, 201210, China.
Antibody-drug conjugates (ADCs) are intricate compounds that pose significant challenges in bioanalytical characterization. Therefore, multiple bioanalytical methods are required to comprehensively elucidate their pharmacokinetic (PK) profiles. In this study, we investigated DS001, an ADC consisting of a humanized monoclonal antibody (hRS7), a cleavable chemical linker, and the microtubule inhibitor monomethyl auristatin E (MMAE), with a drug-to-antibody ratio (DAR) of 8.
View Article and Find Full Text PDFFoods
December 2024
Lab of Biorefinery, Shanghai Advanced Research Institute, Chinese Academy of Sciences, Shanghai 201210, China.
Antioxidants play an important role in maintaining health and enhancing food stability by neutralizing free radicals. This study aimed to extract antioxidant peptides from white-feathered chicken bones through enzymatic hydrolysis, optimize the enzymatic hydrolysis conditions, and further investigate the relevance between the amino acid composition, molecular weight, and antioxidant activity of the resulting chicken bone hydrolysate. Alcalase was the most effective enzyme for hydrolyzing cooked chicken bones compared with papain, pepsin, and trypsin, yielding hydrolysates with the highest DH and ABTS radical scavenging activity.
View Article and Find Full Text PDFJ Sci Food Agric
December 2024
Microbiology Department, The Institute of Science, Dr. Homi Bhabha State University, Mumbai, India.
Background: Bacillus subtilis AU-2, isolated from the gut of Tribolium castaneum, was used for protease production. The purified protease was evaluated for its potential in food-related applications including meat tenderization, milk coagulation, and the preparation of enzymatic soybean hydrolysates. Enzymatic hydrolysis of soy protein is an effective method for producing protein hydrolysates with optimal techno-functional properties.
View Article and Find Full Text PDFFood Res Int
January 2025
Dpto. Tecnología de Alimentos, Instituto Universitario de Ingeniería de Alimentos - FoodUPV, Universitat Politècnica de València, Camino de Vera s/n, 46022 Valencia, Spain. Electronic address:
The hydrolysis of legume proteins improves their nutritional and functional properties. Usually done by mixing flour with an enzyme solution, the process can be simplified using vacuum enzyme impregnation during soaking. This study used vacuum impregnation with papain or bromelain to obtain hydrolysed broad bean flours.
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