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Journal articles on the topic 'Proteolytic enzymes'

Author: Grafiati

Published: 4 June 2021

Last updated: 1 August 2024

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1

Chirkin, A. A., O. M. Balaeva-Tikhomirova, V. V. Dolmatova, and I. O. Semenov. "Molecular-structural homology of proteolytic enzymеs in the studying of proteolysis mechanism and its regulation." Proceedings of the National Academy of Sciences of Belarus, Chemical Series 57, no. 2 (June 3, 2021): 206–17. http://dx.doi.org/10.29235/1561-8331-2021-57-2-206-217.

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The actual problem of experimental medicine is the substantiation of new model organisms that meet modern requirements of bioethics, cost and conditions of detention. The aim of this work was a comparative analysis of the homology degree of proteolytic enzymes in humans and pulmonary freshwater mollusks. The homology of enzymes in nucleotide sequences in humans and pulmonary freshwater mollusks in the analysis of unregulated proteolysis is 66–68 %; regulated proteolysis – 69–76 %; ubiquitin-like modifiers – 78–83 %; extracellular enzymes – 67–76 %; and intracellular enzymes – 65–72 %. The evolutionary conservatism of proteolytic enzymes and the presence of an open blood circulation, which allows the substances under study to be delivered from the hemolymph directly to target cells, make it possible to use these animals as cheap and convenient test organisms. The practical importance of a sufficiently high homology degree of proteolytic enzymes in humans and pulmonary freshwater mollusks justifies the expediency of forming mollusk aquaculture to obtain proteolytic enzyme protein preparations from their tissues within the framework of the tasks of biopharmaceuticals, cosmetics and the food industry.

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2

de Barros Soares, L. H., D. Ney Marques, P. Melchionna Albuquerque, and M. A. Záchia Ayub. "Influence of some commercial proteases and enzymatic associations on the hydrolytic solubilization of deboned poultry meat proteins Influencia de algunas proteasas comerciales y preparados enzimáticos en la solubilización hidrolitica de las proteínas de la carne de pollo separada mecánicamente." Food Science and Technology International 6, no. 4 (August 2000): 301–6. http://dx.doi.org/10.1177/108201320000600404.

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Mechanically deboned poultry meat (MDPM) was used as a basic source of protein to assess the efficiency of seven proteolytic enzymes and some enzymatic associations over the hydrolysis of that protein. As a main parameter, the evolution of protein solubilization during 4 h of proteolysis was evaluated. The enzymes alcalase, esperase, flavourzyme, fungal protease, HT-proteolytic, papain, proteopex, and combinations of alcalase + flavourzyme, esperase + flavourzyme, HT-proteolytic + flavourzyme, and proteopex + flavourzyme were applied at concentrations of 0.60% and 1.20% of commercial product as a function of total protein. The initial pH was adjusted to 7.0 or 8.0 and the temperature was maintained at 50 °C or 60 °C according to optimal conditions for each enzyme. The proteolytic activities of the enzymes were also compared with azocasein. The hydrolysis index (HI), i.e., the rate between the maximum value and the initial amount of soluble protein was formulated to allow the comparison among treatments. Results showed that the temperature did not influence the proteolysis in the tested model. The association of alcalase + flavourzyme was shown to be more efficient than all other treatments, obtaining more than 70% of soluble protein. Fungal protease pre sented the lowest results.

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3

Babinets, L. S., K. Y. Kytsai, and V. R. Mykuliak. "The influence of obesity on the parameters of the kallikrein-kinin system and proteolysis in chronic biliary pancreatitis." GASTROENTEROLOGY 58, no. 1 (April 7, 2024): 13–17. http://dx.doi.org/10.22141/2308-2097.58.1.2024.581.

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Background. Clinical practice and science have accumulated data that obese patients suffer from severe forms of acute and chronic pancreatitis, which is explained by the accumulation of fat around the pancreas, a decreased activity of pancreatic enzymes. The purpose of the study is to describe the features of the kallikrein-kinin system and proteolysis in chronic biliary pancreatitis (CBP), depending on the presence of comorbid obesity. Materials and methods. One hundred and thirty-seven patients with chronic biliary pancreatitis were examined and divided into two groups depending on the presence of comorbid obesity: group I consisted of 22 patients with CBP and group II — of 115 patients with CBP and obesity. Results. The obtained results proved that an increase in body weight of patients with CBP lead to a more severe kallikrein-kinin system imbalance, with enhanced activation of inflammation and a decrease in the protective effect of the proteolysis. An increase in the degree of obesity in patients with CBP was accompanied by a more severe kallikrein-kinin system and proteolytic imbalance with an increase in the proteolytic enzymes level that have a damaging effect on the hepatic and pancreatic tissues and have a pro-inflammatory activity, as well as by a decrease in the content of the proteolytic enzyme inhibitors, which reliably weakened the protective effect of kallikrein-kinin system and proteolysis. Conclusions. 1) It was proved that there is a higher activity of the kallikrein-kinin system (according to proteolytic activation and kallikrein levels) and a decrease in the activity of proteolytic enzyme inhibitors (α2-macroglobulin and kininase II) in patients with chronic biliary pancreatitis and comorbid obesity compared to those without obesity (p < 0.05). 2) An increase in the degree of obesity lead to an increase of proteolytic activity and a decrease in the content of the proteolytic enzyme inhibitors in patients with chronic biliary pancreatitis. It was proved the aggravating effect of obesity on the kallikrein-kinin system and proteolytic imbalance, which must be taken into account while forming a comprehensive treatment of such patients.

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4

Choi, Jin-Ha. "Proteolytic Biosensors with Functional Nanomaterials: Current Approaches and Future Challenges." Biosensors 13, no. 2 (January 21, 2023): 171. http://dx.doi.org/10.3390/bios13020171.

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Proteolytic enzymes are one of the important biomarkers that enable the early diagnosis of several diseases, such as cancers. A specific proteolytic enzyme selectively degrades a certain sequence of a polypeptide. Therefore, a particular proteolytic enzyme can be selectively quantified by changing detectable signals causing degradation of the peptide chain. In addition, by combining polypeptides with various functional nanomaterials, proteolytic enzymes can be measured more sensitively and rapidly. In this paper, proteolytic enzymes that can be measured using a polypeptide degradation method are reviewed and recently studied functional nanomaterials-based proteolytic biosensors are discussed. We anticipate that the proteolytic nanobiosensors addressed in this review will provide valuable information on physiological changes from a cellular level for individual and early diagnosis.

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5

Salahuddin, Parveen, and Asad U. Khan. "Proteolytic Enzymes Database." Journal of Proteomics & Bioinformatics 01, no. 02 (May 24, 2008): 109–11. http://dx.doi.org/10.4172/jpb.1000017.

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6

Murphy, G. "PL2.2. Proteolytic enzymes." Cancer Treatment Reviews 34 (2008): 2. http://dx.doi.org/10.1016/j.ctrv.2008.03.016.

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7

Tikhonov, Sergey L., Natalya V. Tikhonova, Leonid S. Kudryashov, Olga A. Kudryashova, Nadezhda V. Moskovenko, and Irina N. Tretyakova. "Efficiency of Microencapsulation of Proteolytic Enzymes." Catalysts 11, no. 11 (October 21, 2021): 1270. http://dx.doi.org/10.3390/catal11111270.

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Currently, special attention is paid to the study of the effectiveness of the immobilization method—microencapsulation. The aim of the research is to obtain a complex enzyme preparation from pepsin and papain by sequential microencapsulation of enzymes in a pseudo-boiling layer and to evaluate its tenderizing effect on pork. The objects of research were enzymes: pepsin and papain, which were microencapsulated in a protective coating of maltodextrin. It was found that the biocatalytic activity of the complex enzyme preparation is higher than that of pure enzymes. Microencapsulation allows maintaining the high proteolytic activity of enzymes for a long storage period. It has been shown that the thickness of the protective layer during microencapsulation of pepsin and papain in the pseudo-boiling layer of maltodextrin should be in the range of 4–6 microns. During the research, the physicochemical properties of pork were studied depending on the duration of fermentation. It was found that the maximum activity of immobilized enzymes is shifted to the alkaline side. Pork salting with the use of a microencapsulated enzyme preparation in the brine increases the water-binding capacity of proteins to a greater extent in comparison with brine with pure enzymes. The presented data show the high efficiency of sequential microencapsulation of the enzyme pepsin and then papain into a protective layer of maltodextrin in order to preserve their activity during storage.

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8

Somers, Joanne M., Bernadette O'Brien, William J. Meaney, and Alan L. Kelly. "Heterogeneity of proteolytic enzyme activities in milk samples of different somatic cell count." Journal of Dairy Research 70, no. 1 (February 2003): 45–50. http://dx.doi.org/10.1017/s0022029902005988.

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Milk contains the alkaline proteinase plasmin and lysosomal proteinases; the significance of the latter is ill-defined. The objective of this study was to investigate composition and activities of several different proteolytic enzymes in milk samples of varying somatic cell count (SCC). Increasing milk SCC was correlated with increased plasmin, cathepsin D and cysteine protease activities, with concomitant increases in proteolysis in milk. Addition of plasmin inhibitors confirmed the heterogeneity of proteinase activities in milk, as urea-PAGE analysis of milk samples showed casein hydrolysis in milk after 7 d storage even in samples with inhibitors added; extent and heterogeneity of proteolysis was correlated with milk SCC. Rennet coagulation properties were not significantly correlated with SCC, or activities of measured enzymes. Milk of increasing SCC also exhibited decreased physical stability during incubation of milk at 37 °C. Pasteurized milk was more stable than raw milk, suggesting that the enzyme(s) or mechanisms leading to such instability are impaired by pasteurization. Overall, milk has a very heterogeneous proteolytic enzyme population, with a higher significance of non-plasmin enzymes, such as cathepsin D and cysteine proteinases, than perhaps previously recognised.

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9

Bergeron, F., R. Leduc, and R. Day. "Subtilase-like pro-protein convertases: from molecular specificity to therapeutic applications." Journal of Molecular Endocrinology 24, no. 1 (February 1, 2000): 1–22. http://dx.doi.org/10.1677/jme.0.0240001.

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Limited proteolysis of most large protein precursors is carried out in vivo by the subtilisin-like pro-protein convertases. Many important biological processes such as peptide hormone synthesis, viral protein processing and receptor maturation involve proteolytic processing by these enzymes, making them potential targets for the development of novel therapeutic agents. However, the efficient development of such molecules requires a better understanding of the molecular mechanisms of proteolytic protein processing. Herein, we review the most recent findings on the molecular aspects of subtilisin-like convertase activity, such as the structural analysis of the proteases, the mechanisms of enzyme/substrate specificity, their interaction with other proteins such as 7B2, and the comparative tissue and cellular distribution of the enzymes and their substrates. These data are then used as a background for the review of the known biological functions of subtilisin-like pro-protein convertases, the reported clinical cases involving proteolytic processing defects and, finally, the ongoing development of new therapeutic inhibitor molecules based on this knowledge.

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10

ÅGREN, GUNNAR. "Proteins and proteolytic enzymes." Acta Medica Scandinavica 105, no. 1-2 (April 24, 2009): 73–83. http://dx.doi.org/10.1111/j.0954-6820.1940.tb16083.x.

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11

Lehmann, P. V. "Immunomodulation by proteolytic enzymes." Nephrology Dialysis Transplantation 11, no. 6 (June 1, 1996): 953–55. http://dx.doi.org/10.1093/oxfordjournals.ndt.a027510.

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12

Tjwan Tan, P. S., Bert Poolman, and Wil N. Konings. "Proteolytic enzymes ofLactococcus lactis." Journal of Dairy Research 60, no. 2 (May 1993): 269–86. http://dx.doi.org/10.1017/s0022029900027606.

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13

Lehmann, P. V. "Immunomodulation by proteolytic enzymes." Nephrology Dialysis Transplantation 11, no. 6 (June 1996): 953–55. http://dx.doi.org/10.1093/ndt/11.6.953.

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14

Brannon-Peppas, Lisa. "Handbook of Proteolytic Enzymes." Journal of Controlled Release 68, no. 1 (July 2000): 136–37. http://dx.doi.org/10.1016/s0168-3659(00)00257-1.

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15

HARHEN, BRENDAN, and FRANK BARRY. "Immobilization of proteolytic enzymes." Biochemical Society Transactions 18, no. 2 (April 1, 1990): 314–15. http://dx.doi.org/10.1042/bst0180314.

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16

Ribári, Ottó, István Sziklai, and Géza J. Kiss. "Proteolytic Enzymes in Otosclerosis." ORL 49, no. 6 (1987): 282–86. http://dx.doi.org/10.1159/000275953.

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17

Baeza, Gustavo, Duberlis Correa, and Carlos Salas. "Proteolytic enzymes inCarica candamarcensis." Journal of the Science of Food and Agriculture 51, no. 1 (1990): 1–9. http://dx.doi.org/10.1002/jsfa.2740510102.

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18

Scolari, G., M. Vescovo, P. G. Sarra, and V. Bottazzi. "Proteolysis in cheese made with liposome-entrapped proteolytic enzymes." Le Lait 73, no. 3 (1993): 281–92. http://dx.doi.org/10.1051/lait:1993326.

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19

Kudryashova, I. V. "Proteolysis and proteolytic enzymes in structural plasticity of synapses." Neurochemical Journal 3, no. 3 (September 2009): 164–72. http://dx.doi.org/10.1134/s1819712409030027.

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20

Panicke, L., M. Schmidt, T. Król, and R. Staufenbiel. "Proteolytische Aktivitäten der lysosomalen Enzyme bei Milchrindern* – 2. Mitteilung: Lysosomale Enzymaktivitäten und die Milchleistung bei Kühen." Archives Animal Breeding 42, no. 5 (October 10, 1999): 443–50. http://dx.doi.org/10.5194/aab-42-443-1999.

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Abstract. Title of the paper: Proteolytic activities of lysosomal enzymes in dairy cattle, II. Lysosomal enzyme activities and milk performance Lysosomal enzymes were gained from plasma and leucocytes using 1011 blood samples of 786 dairy cows. There is a correlation between enzyme activities and milk produetion traits with significant correlation coefficients rp = 0,4–0,5 for the daily milk yield at control as well as for the lactation Performance in 305 days during the second third of the first lactation. The level of enzyme activities shows a higher effect on the Performance than the proteolysis. No additional gain of information is to be expected from the leucocytes what limits the pallet to the plasma enzymes.

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21

Sun, Z., W. Carpiaux, D. Fan, Y. Fan, R. Lakshminarayanan, and J. Moradian-Oldak. "Apatite Reduces Amelogenin Proteolysis by MMP-20 and KLK4 in vitro." Journal of Dental Research 89, no. 4 (February 16, 2010): 344–48. http://dx.doi.org/10.1177/0022034509360660.

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Two enamel proteases, matrix metalloproteinase-20 (MMP-20) and kallikrein 4 (KLK4), are known to cleave amelogenin and are necessary for proper enamel formation. However, the effect of hydroxyapatite (HAP) on the proteolytic activity of these enzymes remains unclear. To investigate whether apatite affects normal amelogenin proteolysis, we used 2 different isoforms of amelogenin combined with the appropriate enzymes to analyze proteolytic processing rates in the presence or absence of synthetic hydroxyapatite (HAP) crystals (N = 3). We found a distinct dose-dependent relationship between the amount of HAP present in the proteolysis mixture and the rate of rP172 degradation by rpMMP-20, whereas the effect of HAP on proteolysis of either rP172 or rP148 by rhKLK4 was less prominent.

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22

Nikolaieva, I. "AMPHIBIAN SKIN SECRETIONS: A POTENTIAL SOURCE OF PROTEOLYTIC ENZYMES." Biotechnologia Acta 11, no. 5 (October 2018): 42–48. http://dx.doi.org/10.15407/biotech11.05.042.

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23

Petushkova, Anastasiia I., and Andrey A. Zamyatnin. "Redox-Mediated Post-Translational Modifications of Proteolytic Enzymes and Their Role in Protease Functioning." Biomolecules 10, no. 4 (April 23, 2020): 650. http://dx.doi.org/10.3390/biom10040650.

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Proteolytic enzymes play a crucial role in metabolic processes, providing the cell with amino acids through the hydrolysis of multiple endogenous and exogenous proteins. In addition to this function, proteases are involved in numerous protein cascades to maintain cellular and extracellular homeostasis. The redox regulation of proteolysis provides a flexible dose-dependent mechanism for proteolytic activity control. The excessive reactive oxygen species (ROS) and reactive nitrogen species (RNS) in living organisms indicate pathological conditions, so redox-sensitive proteases can swiftly induce pro-survival responses or regulated cell death (RCD). At the same time, severe protein oxidation can lead to the dysregulation of proteolysis, which induces either protein aggregation or superfluous protein hydrolysis. Therefore, oxidative stress contributes to the onset of age-related dysfunction. In the present review, we consider the post-translational modifications (PTMs) of proteolytic enzymes and their impact on homeostasis.

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24

Nafia, Siti Zidna Ilma, Sri Pujiyanto, and Anto Budiharjo. "Isolasi, Skrining, dan Identifikasi Molekuler Bakteri Termotoleran Proteolitik dari Sumber Air Panas Nglimut Gonoharjo Kendal." Bioma : Berkala Ilmiah Biologi 24, no. 1 (June 13, 2022): 30–35. http://dx.doi.org/10.14710/bioma.24.1.30-35.

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The potential for the use of enzymes in industry is starting to be widely used. Protease is one of the most widely used enzymes in industry. Protease is an enzyme capable of hydrolyzing peptide bonds in proteins. Proteolytic thermotolerant bacteria are one of the important sources of thermostable enzymes that can be isolated from hot springs. The purpose of this study was to isolate and screen proteolytic thermotolerant bacteria and to identify molecularly the best isolates of proteolytic thermotolerant bacteria from the hot springs of Nglimut Gonoharjo. Isolation was carried out by graded dilution on Sodium Agar (NA) and Thermus Agar (TA) media using the spread plate method, and the proteolytic activity test using the paper disc method. Characterization of proteolytic bacterial isolates was carried out by macroscopic and microscopic morphology with gram staining. Molecular identification with 16S rRNA gene through amplification, electrophoresis, sequencing, BLAST analysis and phylogenetic reconstruction. The isolation results obtained 32 proteolytic thermotolerant isolates with irregular and round colony shape characteristics, Gram positive and Gram negative, and stem cells. The results of the enzyme test showed that isolate T5 was the best isolate with a proteolytic index value of 1.90 and was identified as Bacillus subtilis. Gram Positive and Gram Negative, and have stem cells. The results of the enzyme test showed that isolate T5 was the best isolate with a proteolytic index value of 1.90 and was identified as Bacillus subtilis.

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25

Barthomeuf, Chantal. "Application of enzyme purification processes to proteolytic enzymes." Journal of Chromatography A 473 (January 1989): 1–26. http://dx.doi.org/10.1016/s0021-9673(00)91286-x.

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26

Kopitz, J., G. O. Kisen, P. B. Gordon, P. Bohley, and P. O. Seglen. "Nonselective autophagy of cytosolic enzymes by isolated rat hepatocytes." Journal of Cell Biology 111, no. 3 (September 1, 1990): 941–53. http://dx.doi.org/10.1083/jcb.111.3.941.

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Seven cytosolic enzymes with varying half-lives (ornithine decarboxylase, 0.9 h; tyrosine aminotransferase, 3.1 h; tryptophan oxygenase, 3.3 h; serine dehydratase, 10.3 h; glucokinase, 12.7 h; lactate dehydrogenase, 17.0 h; aldolase, 17.4 h) were found to be autophagically sequestered at the same rate (3.5%/h) in isolated rat hepatocytes. Autophagy was measured as the accumulation of enzyme activity in the sedimentable organelles (mostly lysosomes) of electrodisrupted cells in the presence of the proteinase inhibitor leupeptin. Inhibitors of lysosomal fusion processes (vinblastine and asparagine) allowed accumulation of catalytically active enzyme (in prelysosomal vacuoles) even in the absence of proteolytic inhibition, showing that no inactivation step took place before lysosomal proteolysis. The completeness of protection by leupeptin indicates, furthermore, that a lysosomal cysteine proteinase is obligatorily required for the initial proteolytic attack upon autophagocytosed proteins. The experiments suggest that sequestration and degradation of normal cytosolic proteins by the autophagic-lysosomal pathway is a nonselective bulk process, and that nonautophagic mechanisms must be invoked to account for differential enzyme turnover.

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TAILLANDIER, Daniel, Eveline AUROUSSEAU, Dominique MEYNIAL-DENIS, Daniel BECHET, Marc FERRARA, Patrick COTTIN, André DUCASTAING, et al. "Coordinate activation of lysosomal, Ca2+-activated and ATP-ubiquitin-dependent proteinases in the unweighted rat soleus muscle." Biochemical Journal 316, no. 1 (May 15, 1996): 65–72. http://dx.doi.org/10.1042/bj3160065.

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Nine days of hindlimb suspension resulted in atrophy (55%) and loss of protein (53%) in rat soleus muscle due to a marked elevation in protein breakdown (66%, P < 0.005). To define which proteolytic system(s) contributed to this increase, soleus muscles from unweighted rats were incubated in the presence of proteolytic inhibitors. An increase in lysosomal and Ca2+-activated proteolysis (254%, P < 0.05) occurred in the atrophying incubated muscles. In agreement with the measurements in vitro, cathepsin B, cathepsins B+L and m-calpain enzyme activities increased by 111%, 92% and 180% (P < 0.005) respectively in the atrophying muscles. Enhanced mRNA levels for these proteinases (P < 0.05 to P < 0.001) paralleled the increased enzyme activities, suggesting a transcriptional regulation of these enzymes. However, the lysosomal and Ca2+-dependent proteolytic pathways accounted for a minor part of total proteolysis in both control (9%) and unweighted rats (18%). Furthermore the inhibition of these pathways failed to suppress increased protein breakdown in unweighted muscle. Thus a non-lysosomal Ca2+-independent proteolytic process essentially accounted for the increased proteolysis and subsequent muscle wasting. Increased mRNA levels for ubiquitin, the 14 kDa ubiquitin-conjugating enzyme E2 (involved in the ubiquitylation of protein substrates) and the C2 and C9 subunits of the 20 S proteasome (i.e. the proteolytic core of the 26 S proteasome that degrades ubiquitin conjugates) were observed in the atrophying muscles (P < 0.02 to P < 0.001). Analysis of C9 mRNA in polyribosomes showed equal distribution into both translationally active and inactive mRNA pools, in either unweighted or control rats. These results suggest that increased ATP-ubiquitin-dependent proteolysis is most probably responsible for muscle wasting in the unweighted soleus muscle.

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Ayuningrum, Diah, Aninditia Sabdaningsih, and Oktavianto Eko Jati. "The Potential of Phylogenetically Diverse Culturable Actinobacteria from Litopenaeus vannamei Pond Sediment as Extracellular Proteolytic and Lipolytic Enzyme Producers." Tropical Life Sciences Research 33, no. 3 (September 30, 2022): 165–92. http://dx.doi.org/10.21315/tlsr2022.33.3.10.

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Enzymes are catalysts that can increase the reaction time of a biochemical process. Hydrolytic enzymes have a pivotal role in degrading organic waste in both terrestrial and aquatic environments. The aims of this study were (1) to investigate the ability of actinobacteria isolated from Litopenaeus vannamei pond sediment to produce proteolytic and lipolytic enzymes, (2) to identify promising candidates using 16S rRNA gene amplification, and (3) to construct a phylogenetic tree based on the 16S rRNA genes. A skim milk agar medium was used in the preliminary experiment of the proteolytic assay, and a Tween 20/80 medium was used in the lipolytic assay. Fifteen and 20 (out of 40) actinobacterial isolates showed great potential for proteolytic and lipolytic activities, respectively. Furthermore, four actinobacteria isolates produced both enzyme types with proteolytic and lipolytic index scores of 1–6.5. The most promising candidates were SA 2.2 (IM8), SC 2.1 (IM6), SD 1.5 (IM6) and SE 1.1 (IM8). BLAST homology results showed a high similarity between the actinobacteria isolates and Streptomyces verucosisporus, S. mangrovicola, S. barkulensis and Nocardiopsis lucentensis, respectively. Therefore, actinobacteria from Litopenaeus vannamei pond sediment are high-potential proteolytic and lipolytic enzyme producers.

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Anuarbekova, S. S. "Enzymes of microorganisms. Proteases of lactic acid bacterias." Bulletin of Shakarim University. Technical Sciences, no. 3(11) (September 28, 2023): 5–19. http://dx.doi.org/10.53360/2788-7995-2023-3(11)-1.

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The work is devoted to the enzymes of microorganisms. This review article presents the characteristics of microbial enzymes, their classifications according to various parameters. The study examines the role of microbial enzymes in various areas of human life. Enzymes are involved in the biochemical processes of microorganisms for their protection, reproduction, and growth. Enzyme producers are various taxonomic groups of bacteria, filamentous fungi, actinomycetes and yeasts. The article describes hydrolytic enzymes, reveals the importance of the protease enzyme involved in various processes with microorganisms. The main producers of proteolytic enzymes are bacteria of the genus Bacillus, Lactobacillus, Streptococcus, Micrococcus, Pseudomonas, fungi of the genus Aspergillus, Penicillium, Blakeslea, actynomicetes of the genus Streptomyces, Actinomyces. Particular attention is paid to lactic acid bacteria. The significance of the use of protease in the biotechnological industry, in particular, for the development of preparations, starter cultures, bioadditives, and functional food products with desired properties, is shown. The article mentions the results of a study of the proteolytic activity of cultures of microorganisms, obtained by me and my colleagues. The objects of study were bacilli, yeast, fungi and lactic acid bacteria.To assess proteolytic activity, in vitro methods, chromatographic and other methods are used.

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Gudzenko, O. V., V. О. Ivanytsia, and L. D. Varbanets. "Bacteria of the Black Sea Are Producers of Proteolytic Enzymes." Mikrobiolohichnyi Zhurnal 84, no. 3 (December 17, 2022): 3–8. http://dx.doi.org/10.15407/microbiolj84.03.003.

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Despite the fact that in recent years there has been a certain enhancing interest in the study of marine microorganisms, nevertheless, marine bacteria as producers of biologically active substances, in particular enzymes, are still poorly studied. The marine biota is significantly different from the terrestrial one; therefore, there is a high probability of detecting in the marine environment different from terrestrial bacteria producers of enzymes with unique specificity and activity, for the needs of modern biotechnology. Proteolytic enzymes play an important role in these studies. Since the majority of microbial producers are characterized by a number of serious deficiencies, in particular, most of the elastase producers described in the literature are pathogenic for humans, the search for new, effective producers continues to be an urgent problem, given that highly active producers of proteolytic enzymes, in particular elastase, are generally absent in Ukraine. In this regard, the purpose of this work was to screen microorganisms isolated from the Black Sea for the presence of effective producers of proteolytic enzymes. Methods. We used methods of determining proteolytic (caseinilytic, elastolytic, fibrinolytic, fibrinogenolytic) activity. Results. The study of the enzymatic activity of the isolates showed that on the 10th day of cultivation in the supernatant of the culture liquid, caseinolytic activity was not detected only in one isolate 56, whereas very insignificant activity was observed in isolates 7, 20, and 50. The maximum activity was detected in isolate 247 (0.2 units/mL), and lower one - in isolates 46 (0.16 U/mL), 52 (0.15 U/mL), 51 (0.135 U/mL), 54 (0.08 U/mL), and 44 (0.05 U/mL). Of the 10 studied isolates, elastase activity was found only in four of them. The highest activity was found in isolates 51 and 54 (20.83 and 19.96 U/mL, respectively). Lower levels of activity (15.62 U/mL and 12.15 U/mL, respectively) were shown by isolates 52 and 247. The studied isolates also differed in their ability to hydrolyze fibrin and fibrinogen. T e highest fi brinolytic activity (2.33 U/mL) was found in isolates 46 and 54, significantly lower in isolate 20 (0.5 U/mL) and isolate 44 (0.33 U/mL). The rest isolates did not show fibrinolytic activity. As for fibrinogenolytic activity, it was noted in 6 studied cultures. The highest levels of activity were observed in isolate 51 (1.16 U/mL). Lower activity was found in isolates 54 (0.66 U/mL), 7 (0.5 U/mL), and 247 (0.33 U/mL). In isolate 50, it was minimal (0.083 U/mL). Conclusions. No correlation was found between elastase, fibrinolytic and fibrinogenic activity in the studied isolates. Thus, isolates 51, 54 and, to a lesser extent, 52 and 247 synthesize elastase activity. The highest fibrinolytic activity was in isolates 46 and 54, and fibrinogenolytic activity was in isolate 51. It was shown that the Black Sea is rich in marine bacterial species, which can be effective producers of a number of practically important enzymes, in particular, proteolytic ones with specificity to elastin, fibrin, and fibrinogen, which can be promising for implementation in biotechnological processes.

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31

Battifora, H., and M. Kopinski. "The influence of protease digestion and duration of fixation on the immunostaining of keratins. A comparison of formalin and ethanol fixation." Journal of Histochemistry & Cytochemistry 34, no. 8 (August 1986): 1095–100. http://dx.doi.org/10.1177/34.8.2426335.

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The effect of three proteases--trypsin, pepsin, and pronase--on the immunohistochemical staining of keratins with a broad-spectrum monoclonal antibody was investigated in paraffin sections of formalin and ethanol-fixed tissues by means of the peroxidase-antiperoxidase method. Both the length of exposure to the fixative and the duration of proteolysis were varied over a wide range. Ethanol-fixed tissues showed excellent preservation of the antigenicity of keratins, and no appreciable differences in immunostaining related to the length of fixation were found. The use of proteolytic enzymes did not improve these results; on the contrary, it caused rapid tissue disintegration. Formalin-fixed epithelial tissues stained weakly or failed to stain unless they were treated with a proteolytic enzyme. The optimal length of proteolysis varied with the degree of fixation; tissues that were fixed for long periods of time in formalin required longer exposure to a proteolytic enzyme and were more resistant to digestion than were tissues that were fixed briefly. No significant advantage of one protease over another was found in this study. We conclude that a proteolytic step must precede immunostaining for keratins if the tissue is fixed in formalin, but that the digestion period must be adjusted according to the length of exposure to the fixative. The superiority of alcohol over formalin fixation for the preservation of the antigenicity of keratins is confirmed by this study.

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32

Міхайлова, Р. В. "PROTEOLYTIC ENZYMES OF MYCELIAL FUNGI." Microbiology&Biotechnology, no. 3(15) (September 15, 2011): 47–62. http://dx.doi.org/10.18524/2307-4663.2011.3(15).92910.

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33

Fossum, Kåre. "PROTEOLYTIC ENZYMES AND BIOLOGICAL INHIBITORS." Acta Pathologica Microbiologica Scandinavica Section B Microbiology and Immunology 78B, no. 3 (August 15, 2009): 350–62. http://dx.doi.org/10.1111/j.1699-0463.1970.tb04314.x.

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34

Fossum, Kåre. "PROTEOLYTIC ENZYMES AND BIOLOGICAL INHIBITORS." Acta Pathologica Microbiologica Scandinavica Section B Microbiology and Immunology 78B, no. 5 (August 15, 2009): 605–18. http://dx.doi.org/10.1111/j.1699-0463.1970.tb04347.x.

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35

Fossum, Kåre. "PROTEOLYTIC ENZYMES AND BIOLOGICAL INHIBITORS." Acta Pathologica Microbiologica Scandinavica Section B Microbiology and Immunology 78B, no. 6 (August 15, 2009): 741–54. http://dx.doi.org/10.1111/j.1699-0463.1970.tb04365.x.

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36

Fossum, Kåre. "PROTEOLYTIC ENZYMES AND BIOLOGICAL INHIBITORS." Acta Pathologica Microbiologica Scandinavica Section B Microbiology and Immunology 78B, no. 6 (August 15, 2009): 755–59. http://dx.doi.org/10.1111/j.1699-0463.1970.tb04366.x.

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37

Fossum, Kåre. "PROTEOLYTIC ENZYMES AND BIOLOGICAL INHIBITORS." Acta Pathologica Microbiologica Scandinavica Section B Microbiology and Immunology 79B, no. 1 (August 15, 2009): 117–22. http://dx.doi.org/10.1111/j.1699-0463.1971.tb00041.x.

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38

Aretz, Werner, Klaus P. Koller, and GÃ¼nther Riess. "Proteolytic enzymes from recombinantStreptomyces lividansTK24." FEMS Microbiology Letters 65, no. 1-2 (November 1989): 31–35. http://dx.doi.org/10.1111/j.1574-6968.1989.tb03592.x.

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39

Lagunoff, D., and E. P. Benditt. "PROTEOLYTIC ENZYMES OF MAST CELLS*." Annals of the New York Academy of Sciences 103, no. 1 (December 15, 2006): 185–98. http://dx.doi.org/10.1111/j.1749-6632.1963.tb53698.x.

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40

Neurath, H. "Proteolytic enzymes, past and future." Proceedings of the National Academy of Sciences 96, no. 20 (September 28, 1999): 10962–63. http://dx.doi.org/10.1073/pnas.96.20.10962.

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41

Michaud, Dominique. "Gel electrophoresis of proteolytic enzymes." Analytica Chimica Acta 372, no. 1-2 (October 1998): 173–85. http://dx.doi.org/10.1016/s0003-2670(98)00349-3.

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42

Hooper, NM. "Proteolytic Enzymes: A Practical Approach." Biochemical Education 18, no. 1 (January 1990): 56. http://dx.doi.org/10.1016/0307-4412(90)90039-q.

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Turner, A. J. "Proteolytic enzymes: A practical approach." FEBS Letters 275, no. 1-2 (November 26, 1990): 241. http://dx.doi.org/10.1016/0014-5793(90)81484-6.

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44

Nadel, J. A., and R. A. Stockley. "Proteolytic enzymes and airway diseases." European Respiratory Journal 12, no. 6 (December 1, 1998): 1250–51. http://dx.doi.org/10.1183/09031936.98.12061250.

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Opdenakker, Ghislain, and Stefan Masure. "Proteolytic enzymes: A practical approach." Cell 62, no. 6 (September 1990): 1039–40. http://dx.doi.org/10.1016/0092-8674(90)90380-w.

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46

Bohdziewicz, Jolanta. "Ultrafiltration of technical proteolytic enzymes." Process Biochemistry 29, no. 2 (January 1994): 109–18. http://dx.doi.org/10.1016/0032-9592(94)80003-0.

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47

Tomczyk, Łukasz, Grzegorz Leśnierowski, and Renata Cegielska-Radziejewska. "Lysozyme Modification Using Proteolytic Enzymes." Molecules 28, no. 17 (August 26, 2023): 6260. http://dx.doi.org/10.3390/molecules28176260.

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The lysozyme in the chicken egg white consists of various bioactive amino acids. However, these compounds are inactive when they are in the sequence of parent proteins. They become active only when isolated from these proteins. The aim of this study was to modify lysozyme with proteolytic enzymes under specific conditions of the reaction environment so as to obtain active biopeptides. The physicochemical properties of the resulting preparations were also assessed. Our study showed that the modification of lysozyme with hydrolytic enzymes (pepsin and trypsin) under strictly specified conditions resulted in obtaining biopeptide preparations with new and valuable properties, as compared with native lysozyme. After the enzymatic modification of lysozyme, two structural fractions were distinguished in the composition of the resulting preparations—the monomeric fraction and the peptide fraction. The modified lysozyme exhibited high surface hydrophobicity and high total antibacterial activity despite the decrease in the hydrolytic activity. Modification of lysozyme with hydrolytic enzymes, especially pepsin, resulted in preparations with very good antioxidative properties.

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48

Neurath, Hans. "The versatility of proteolytic enzymes." Journal of Cellular Biochemistry 32, no. 1 (1986): 35–49. http://dx.doi.org/10.1002/jcb.240320105.

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Lavie, G., Z. Leib, and C. Servadio. "The mechanism of human NK cell-mediated cytotoxicity. Mode of action of surface-associated proteases in the early stages of the lytic reaction." Journal of Immunology 135, no. 2 (August 1, 1985): 1470–76. http://dx.doi.org/10.4049/jimmunol.135.2.1470.

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Abstract The possible involvement of cell surface-associated proteolytic enzymes in human NK cell-mediated cytotoxicity and the mechanism by which such enzymes exert their activity have been studied. The treatment of intact cells with 3H-DFP under restricted conditions that predominantly bind surface-associated enzymes resulted in the labeling of five to six enzyme bands. Among these were a 35,000-dalton enzyme, which may be a previously identified trypsin-like proteinase engaged in cytotoxicity, and a 58,000-dalton elastase. The latter seems not to be involved in the reaction, as potent inhibitors of this enzyme have negligible effect on cytotoxicity. Of the membrane-associated enzymes, those engaged in cytotoxicity seem to be concealed from the external environment, as pretreatment of the effector cells with protease inhibitors such as trasylol and PMSF have no effect on the reaction. Immediately upon addition of the target cells and the initiation of cytotoxicity, the reaction becomes highly sensitive to inhibitors for a limited time interval of 2 to 5 min when trasylol is employed and 5 to 10 min when TPCK is the inhibitor, suggesting that target cell binding triggers the exposure of the enzymes to the external environment, rendering them accessible to the inhibitors. This short sensitivity period parallels the interval in which the reaction is sensitive to the microfilament inhibitor cytochalasin B. As the reaction proceeds, it becomes increasingly resistant to inhibitors of both proteolysis and cytoskeleton, at the same time suggesting that microfilament action and the unraveling of proteases may be processes that bear a close linkage with one another. The surface-associated elastase on the other hand maintains a constitutive mode of activity distinctive and unrelated to that of enzymes engaged in cytotoxicity. These findings suggest the existence on the surface of the NK lymphocyte of a mechanism that associates the receptor for target cells with an array of enclaved proteolytic enzymes via microfilaments. The resting cytotoxic structures become activated as the receptor attaches to the target cell, triggers the exposure of the proteolytic moiety, and initiates the lytic phase of the reaction.

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Borzova, N. V., O. V. Gudzenko, K. V. Avdiyuk, L. D. Varbanets, and L. T. Nakonechna. "Thermophilic Fungi with Glucosidase and Proteolytic Activities." Mikrobiolohichnyi Zhurnal 83, no. 3 (June 17, 2021): 24–34. http://dx.doi.org/10.15407/microbiolj83.03.024.

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The directed search for extremophilic producers in order to obtain hydrolytic enzymes with increased thermal stability has an unconditional practical potential for use in the food and feed industry to improve the quality of the final product. The aim of the work was to study the ability of collection strains of thermophilic fungi to show α-L-rhamnosidase, α-galactosidase, cellulase, β-mannanase, keratinase and caseinolytic activity. Methods. Micromycetes were grown under submerged conditions in test tubes at 42°C for 8–14 days. Enzymatic activities were studied in the culture liquid supernatant. p-Nitrophenyl-α-D-galactopyranoside, naringin, guar gum galactomannan and Na-carboxymethylcellulose were used as substrates to determine α-galactosidase, α-L-rhamnosidase, β-mannanase and cellulase activities, respectively. Casein and crushed defatted feathers were served as substrates for the determination of proteolytic activity. Results. The enzymatic activity of 50 strains of micromycetes belonging to 17 species was investigated. The studied group showed high activity: 94% of the strains had at least one, 34% – two, 26% – from three to five enzyme activities. The most active keratinase producers were Thielavia terrestris 1920 and 62, Rhizomucor tauricus 1909, Chrysosporium thermophilum 2050, Thermoascus thermophilus 92 and Thermoascus aurantiаcus 2052 (10–26 U/mL). The highest α-L-rhamnosidase activity was observed in T. terrestris 62 (0.35 U/mL), and carboxymethylcellulase activity −in Thermomyces lanuginosus 2046. Six strains showed α-galactosidase (0.05–0.2 U/mL) and four strains − β-mannanase (5–130 U/mL) activity. Conclusions. As a result new strains producing proteolytic and glycolytic enzymes were isolated among thermophilic micromycetes. Soil thermophilic micromycetes can be used as producers of proteolytic and glycolytic enzymes. Of particular interest are the cultures of Acremonium thermophilum 1963, Corynascus thermophilum 2050, C. sepedonium 1899 and 65068, T. thermophilus 1946, which are capable of producing complexes of proteases and glycosidases in the culture liquid. This indicates that these strains are promising for use as destructors in various technologies processing of complex raw materials.

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