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1

Voisine, R., F. Côté, J. Verreault, and A. Porter. "Protein Transfer in Mainstream and Sidestream Cigarette Smoke." Beiträge zur Tabakforschung International/Contributions to Tobacco Research 21, no. 1 (March 1, 2004): 9–14. http://dx.doi.org/10.2478/cttr-2013-0766.

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AbstractProtein transfer in tobacco smoke has been studied using the protease, Savinase™, as a model protein. Mainstream and sidestream smoke were collected from cigarettes to which Savinase had been added at various concentrations. Savinase was extracted from the smoke condensate with an organic solvent system before being precipitated and further identified by denaturing polyacrylamide gel electrophoresis (SDS-PAGE) and Western immunoblotting. The detection limit of the method, based on addition of Savinase to the smoke condensate, was 25 µg in mainstream and 100 µg in sidestream smoke. At a Savinase concentration of 6000 µg per gram of tobacco, the methodology allows the detection of protein transfer as low as 0.009% and 0.054% in mainstream and sidestream smoke, respectively. Using this approach, it was shown that there is no detectable Savinase in the mainstream and sidestream smoke of filtered and unfiltered cigarettes containing up to 6000 µg of Savinase per gram of tobacco. These facts strongly suggest that there is no significant transfer of protein from tobacco into cigarette smoke.
2

Smith, E. M., L. E. Green, D. Mason, T. S. Gunasekera, and D. A. Veal. "Savinase Is a Bactericidal Enzyme." Applied and Environmental Microbiology 69, no. 1 (January 1, 2003): 719–21. http://dx.doi.org/10.1128/aem.69.1.719-721.2003.

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3

Pedersen, Jan T., Ole H. Olsen, Christian Betzel, Susanne Eschenburg, Sven Branner, and Sven Hastrup. "Cavity Mutants of Savinase™." Journal of Molecular Biology 242, no. 3 (September 1994): 193–202. http://dx.doi.org/10.1006/jmbi.1994.1572.

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4

Wu, Shanshan, Tam T. T. N. Nguyen, Olga V. Moroz, Johan P. Turkenburg, Jens E. Nielsen, Keith S. Wilson, Kasper D. Rand, and Kaare Teilum. "Conformational heterogeneity of Savinase from NMR, HDX-MS and X-ray diffraction analysis." PeerJ 8 (June 26, 2020): e9408. http://dx.doi.org/10.7717/peerj.9408.

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Background Several examples have emerged of enzymes where slow conformational changes are of key importance for function and where low populated conformations in the resting enzyme resemble the conformations of intermediate states in the catalytic process. Previous work on the subtilisin protease, Savinase, from Bacillus lentus by NMR spectroscopy suggested that this enzyme undergoes slow conformational dynamics around the substrate binding site. However, the functional importance of such dynamics is unknown. Methods Here we have probed the conformational heterogeneity in Savinase by following the temperature dependent chemical shift changes. In addition, we have measured changes in the local stability of the enzyme when the inhibitor phenylmethylsulfonyl fluoride is bound using hydrogen-deuterium exchange mass spectrometry (HDX-MS). Finally, we have used X-ray crystallography to compare electron densities collected at cryogenic and ambient temperatures and searched for possible low populated alternative conformations in the crystals. Results The NMR temperature titration shows that Savinase is most flexible around the active site, but no distinct alternative states could be identified. The HDX shows that modification of Savinase with inhibitor has very little impact on the stability of hydrogen bonds and solvent accessibility of the backbone. The most pronounced structural heterogeneities detected in the diffraction data are limited to alternative side-chain rotamers and a short peptide segment that has an alternative main-chain conformation in the crystal at cryo conditions. Collectively, our data show that there is very little structural heterogeneity in the resting state of Savinase and hence that Savinase does not rely on conformational selection to drive the catalytic process.
5

van Wassenaar, Pieter D. "Substrate specificity of savinase toward β-casein." Journal of Protein Chemistry 11, no. 4 (August 1992): 370. http://dx.doi.org/10.1007/bf01673725.

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6

Kukhtyn, Mykola, Khrystyna Kravcheniuk, Ludmila Beyko, Yulia Horiuk, Oleksandr Skliar, and Serhii Kernychnyi. "STUDY OF THE INFLUENCE OF SAVINASE®EVITY16L ENZYME ON BIOFILMS FORMATION OF STAPHYLOCOCCUS AUREUS ON STAINLESS STEEL WITH DIFFERENT ROUGHNESS." EUREKA: Life Sciences 2 (March 31, 2019): 26–32. http://dx.doi.org/10.21303/2504-5695.2019.00858.

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Microbial films formation on the dairy equipment creates a serious problem, because they are difficult to eliminate by washing and disinfecting means that results in contaminating dairy products by microorganisms. The aim of the work was to study the influence of Savinase®Evity 16L proteolytic enzyme on the process of destructing biofilms, formed by Staphylococcus aureus on stainless steel with different surface roughness. It has been established, that surface roughness of stainless steel influences the process of Savinase®Evity 16L enzyme penetration in a hollow and prevents the destruction of the biofilm matrix, created by Staphylococcus aureus. It has been revealed, that after the influence of a proteolytic enzyme on Staphylococcus aureus biofilms, created on steel with roughness 0,16±0,018 mcm, the density decreased in 4,0 times (р≤0,05), comparing with a condition before processing. At roughness 0,63±0,087 mcm the density of formed biofilms decreased at the effect of Savinase®Evity 16L in 3,3times (р≤0,05) and the biofilm was characterized as a weak one. At the same time at stainless steel surfaces with roughness 2,68–0,95mcm, the density of biofilms decreased in 2,3–2,1times (р≤0,05), comparing with a condition before processing, and they were characterized as ones of the middle density. It has been also revealed, that the degradation intensity of biofilms under the influence of Savinase®Evity 16L enzyme at roughness 2,68–0,95 mcm was 1,7–1,9 times (р≤0,05) lower than at the surface with roughness 0,16±0,018 mcm. So, the revealed degradation features of a biofilm, created by Staphylococcus aureus at surfaces of stainless steel of different roughness at the influence of Savinase®Evity 16L proteolytic enzyme give a possibility to substantiate the addition of proteolytic enzymes to the composition of washing means for dairy production. It is also offered to process the surface to the roughness no more than 0,63 mcm for producing food steel for raising the effectiveness of biofilms destruction by enzymes and for the sanitary processing.
7

N., Wafaa, H. A. Elbarbary, E. M. A. Ibrahim, H. A. Mohamed, and H. Jenssen. "EFFECT OF ENZYME TYPE AND HYDROLYSIS TIME ON ANTIBACTERIAL AND ANTIOXIDANT ACTIVITY OF WHEY PROTEIN HYDROLYSATES." IRAQI JOURNAL OF AGRICULTURAL SCIENCES 53, no. 6 (December 29, 2022): 1340–57. http://dx.doi.org/10.36103/ijas.v53i6.1650.

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There is an elevated need for novel antimicrobial preservatives in the food industry, and hydrolysis of waste products from the same sector has for decades been viewed as a potential source of these. In the current study we have purified bovine whey protein using size-exclusion chromatography (SEC), and hydrolyzed it by trypsin, pepsin, alcalase, savinase, and neutrase at different times 30, 60, 120, 240, and 300 min. The highest active time hydrolysate was subsequently fractionated by SEC, monitored for antibacterial and antioxidant activities, and characterized using UHPLC-MS/MS. Alcalase and savinase displayed higher degree of hydrolysis, higher antibacterial activity in their hydrolysates at 60 and 30 min, respectively compared to the other enzymes. The alcalase hydrolysates exhibited significantly the highest antioxidant activity rescuing 89% of the yeast cell from Hydrogen peroxide induced oxidative stress at 120 minutes. Proteomic analysis of the highly active fractions identified peptides from α-lactalbumin with structural similarity to known antioxidant peptides. Thus, our results support the using food grade enzymes like alcalase and savinase in the food industry.
8

Pfeuti, Osborne, Shoveller, Ignatz, and Bureau. "Development of a Novel Enzymatic Pretreatment for Improving the Digestibility of Protein in Feather Meal." AgriEngineering 1, no. 4 (October 7, 2019): 475–84. http://dx.doi.org/10.3390/agriengineering1040034.

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This study describes the process of developing an enzymatic pretreatment to improvethe nutritional value of feather meal (FeM). In a first experiment, a full factorial design was used toexamine the effects of various incubation conditions on the solubilization of nitrogen in FeM. Weincubated FeM for 3 h with various levels of a commercial alkaline serine protease (Savinase®16L), sodium sulphite (Na2SO3), and digestion buffer. A Savinase® 16L level of 3% (%FeM v/w),Na2SO3 level of 3% (%FeM w/w), and digestion buffer level of 500% (%FeM w/w) were identifiedas the optimal conditions. Under these optimal conditions, 45% of the nitrogen in FeM wassolubilized. In a second experiment, we evaluated the effect of more economically sustainableincubation conditions on the in vitro digestibility of protein (pepsin-HCl digestibility andmultistep protein evaluation) in FeM. Two FeMs were incubated with 0.5% Savinase® 16L (%FeMv/w), 2% Na2SO3 (%FeM w/w), and 200% buffer (%FeM w/w) for 24 h. The pretreatment improvedpepsin-HCl digestibility by 7%–16% and the total tract degradable protein content by 14%–50%.Accordingly, this novel pretreatment could be applied in the animal feed industry to improve thenutritional value of FeM.
9

Lin, Hai Tao, Fang Jiang, Hui Su, and Jiwei Huang. "Study on Cashmere Fibers Shrink-Proofing by Enzyme Based on Fuzz Mathematics Method." Advanced Materials Research 236-238 (May 2011): 2830–35. http://dx.doi.org/10.4028/www.scientific.net/amr.236-238.2830.

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Cashmere shrink-proofing effect by enzyme can't achieve ideal shrink-proof effect, so hydrogen peroxide + Savinase protease combined treatment was selected to treat cashmere fiber. In this paper, the included angle cosine method was used to determine the empowerment weight, and used the fuzzy matter-element analysis to fuzzy comprehensive evaluation of the experimental index, the optimum conditions is: hydrogen peroxide pretreatment temperature 35 °C, time 45min, H2O2 40ml / L, pH 9, pyrophosphate 5g / L, the temperature of enzyme treatment 35 °C, time 25min, concentration 40ml / L, pH 9. After cashmere fibers were treated in hydrogen peroxide and Savinase protease combined treatment, cashmere’s Shrink-proofing is well.
10

Vinther, Anders, Jørgen Petersen, and Henrik Søeberg. "Capillary electrophoretic determination of the protease Savinase in cultivation broth." Journal of Chromatography A 608, no. 1-2 (September 1992): 205–10. http://dx.doi.org/10.1016/0021-9673(92)87125-r.

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11

Lange, Gudrun, Christian Betzel, Sven Branner, and Keith S. Wilson. "Crystallographic Studies of Savinase, a Subtilisin-like Proteinase, at pH 10.5." European Journal of Biochemistry 224, no. 2 (September 1994): 507–18. http://dx.doi.org/10.1111/j.1432-1033.1994.00507.x.

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12

Gron, Hanne, Lene M. Bech, and Klaus Breddam. "A Salt Dependent Increase in the Catalytic Activity of the Subtilisin Savinase." Protein & Peptide Letters 1, no. 2 (September 1994): 106–13. http://dx.doi.org/10.2174/0929866501666220424134356.

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The proteolytic activity of the subtilisin Savinase is, with some substrates, radically enhanced at increased ionic strength. At some substrate positions the incorporation of more hydrophobic amino acid residues enhances the beneficial effects of salt addition. At other positions only the incorporation of charged amino acid residues leads to a significant change in the salt dependency. When the substrates are optimized with respect to hydrophobic interactions the enhancing effect of salt. declines. This demonstrates that the beneficial (rate enhancing) effects of salt addition cannot always be accounted for by simple models, e.g., the traditional "salting out" model.
13

Devita, Liza, Hanifah Nuryani Lioe, Mala Nurilmala, and Maggy T. Suhartono. "The Bioactivity Prediction of Peptides from Tuna Skin Collagen Using Integrated Method Combining In Vitro and In Silico." Foods 10, no. 11 (November 9, 2021): 2739. http://dx.doi.org/10.3390/foods10112739.

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The hydrolysates and peptide fractions of bigeye tuna (Thunnus obesus) skin collagen have been successfully studied. The hydrolysates (HPA, HPN, HPS, HBA, HBN, HBS) were the result of the hydrolysis of collagen using alcalase, neutrase, and savinase. The peptide fractions (PPA, PPN, PPS, PBA, PBN, PBS) were the fractions obtained following ultrafiltration of the hydrolysates. The antioxidant activities of the hydrolysates and peptide fractions were studied using the DPPH method. The effects of collagen types, enzymes, and molecular sizes on the antioxidant activities were analyzed using profile plots analysis. The amino acid sequences of the peptides in the fraction with the highest antioxidant activity were analyzed using LC-MS/MS. Finally, their bioactivity and characteristics were studied using in silico analysis. The hydrolysates and peptide fractions provided antioxidant activity (6.17–135.40 µmol AAE/g protein). The lower molecular weight fraction had higher antioxidant activity. Collagen from pepsin treatment produced higher activity than that of bromelain treatment. The fraction from collagen hydrolysates by savinase treatment had the highest activity compared to neutrase and alcalase treatments. The peptides in the PBN and PPS fractions of <3 kDa had antidiabetic, antihypertensive and antioxidant activities. In conclusion, they have the potential to be used in food and health applications.
14

Imai, S. "The effect of the proteolytic enzyme savinase on human plantar skin in vitro." Archives of Dermatological Research 283, no. 6 (September 1991): 377–81. http://dx.doi.org/10.1007/bf00371819.

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15

Remerowski, M. Lyndsay, Henri A. M. Pepermans, Cornelis W. Hilbers, and Frank J. M. Ven. "Backbone Dynamics of the 269-residue Protease Savinase Determined from 15N-NMR Relaxation Measurements." European Journal of Biochemistry 235, no. 3 (February 1996): 629–40. http://dx.doi.org/10.1111/j.1432-1033.1996.00629.x.

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16

Nasiripourdori, Adak, Hossein Naderi-Manesh, Bijan Ranjbar, and Khosro Khajeh. "Co-solvent effects on structure and function properties of savinase: Solvent-induced thermal stabilization." International Journal of Biological Macromolecules 44, no. 4 (May 2009): 311–15. http://dx.doi.org/10.1016/j.ijbiomac.2008.09.018.

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17

Christiansen, Torben, Søren Michaelsen, Mogens Wümpelmann, and Jens Nielsen. "Production of savinase and population viability ofBacillus clausiiduring high-cell-density fed-batch cultivations." Biotechnology and Bioengineering 83, no. 3 (May 28, 2003): 344–52. http://dx.doi.org/10.1002/bit.10675.

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18

Frankaer, Christian G., Olga V. Moroz, Johan P. Turkenburg, Stein I. Aspmo, Majbritt Thymark, Esben P. Friis, Kenny Stahl, Jens E. Nielsen, Keith S. Wilson, and Pernille Harris. "Analysis of an industrial production suspension ofBacillus lentussubtilisin crystals by powder diffraction: a powerful quality-control tool." Acta Crystallographica Section D Biological Crystallography 70, no. 4 (March 21, 2014): 1115–23. http://dx.doi.org/10.1107/s1399004714001497.

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A microcrystalline suspension ofBacillus lentussubtilisin (Savinase) produced during industrial large-scale production was analysed by X-ray powder diffraction (XRPD) and X-ray single-crystal diffraction (MX). XRPD established that the bulk microcrystal sample representative of the entire production suspension corresponded to space groupP212121, with unit-cell parametersa= 47.65,b= 62.43,c= 75.74 Å, equivalent to those for a known orthorhombic crystal form (PDB entry 1ndq). MX using synchrotron beamlines at the Diamond Light Source with beam dimensions of 20 × 20 µm was subsequently used to study the largest crystals present in the suspension, with diffraction data being collected from two single crystals (∼20 × 20 × 60 µm) to resolutions of 1.40 and 1.57 Å, respectively. Both structures also belonged to space groupP212121, but were quite distinct from the dominant form identified by XRPD, with unit-cell parametersa= 53.04,b = 57.55,c= 71.37 Å anda= 52.72,b= 57.13,c= 65.86 Å, respectively, and refined toR= 10.8% andRfree= 15.5% and toR= 14.1% andRfree= 18.0%, respectively. They are also different from any of the forms previously reported in the PDB. A controlled crystallization experiment with a highly purified Savinase sample allowed the growth of single crystals of the form identified by XRPD; their structure was solved and refined to a resolution of 1.17 Å with anRof 9.2% and anRfreeof 11.8%. Thus, there are at least three polymorphs present in the production suspension, albeit with the 1ndq-like microcrystals predominating. It is shown how the two techniques can provide invaluable and complementary information for such a production suspension and it is proposed that XRPD provides an excellent quality-control tool for such suspensions.
19

Andrea, Torres, Ferrándiz Marcela, Capablanca Lucía, Franco Esther, Mira Elena, and Moldovan Simona. "Microencapsulation of Lipase and Savinase Enzymes by Spray Drying Using Arabic Gum as Wall Material." Journal of Encapsulation and Adsorption Sciences 06, no. 04 (2016): 161–73. http://dx.doi.org/10.4236/jeas.2016.64012.

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Wang, Ping, Qiang Wang, Li Cui, Xuerong Fan, Jiugang Yuan, and Murong Gao. "A comparative evaluation of the action of savinase and papain to the cutinase-pretreated wool." Fibers and Polymers 11, no. 4 (July 2010): 586–92. http://dx.doi.org/10.1007/s12221-010-0586-9.

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21

Betzel, Christian, Silke Klupsch, Gerlind Papendorf, Sven Hastrup, Sven Branner, and Keith S. Wilson. "Crystal structure of the alkaline proteinase Savinase™ from Bacillus lentus at 1.4 Å resolution." Journal of Molecular Biology 223, no. 2 (January 1992): 427–45. http://dx.doi.org/10.1016/0022-2836(92)90662-4.

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22

Bautista-Expósito, Sara, Elena Peñas, Montserrat Dueñas, José Manuel Silván, Juana Frias, and Cristina Martínez-Villaluenga. "Individual contributions of Savinase and Lactobacillus plantarum to lentil functionalization during alkaline pH-controlled fermentation." Food Chemistry 257 (August 2018): 341–49. http://dx.doi.org/10.1016/j.foodchem.2018.03.044.

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23

Georgieva, Dessislava Nikolova, Peter Nikolov, Veneta Ivanova, Adriana Gusterova, and Christian Betzel. "Fluorescence properties of Savinase®: the X-ray structure in the region of the tryptophyl residues." Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy 55, no. 11 (September 1999): 2309–19. http://dx.doi.org/10.1016/s1386-1425(99)00098-0.

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24

Arlian, L. G., D. L. Vyszenski-Moher, J. A. Merski, H. L. Ritz, T. L. Nusair, and E. R. Wilson. "Antigenic and Allergenic Characterization of the Enzymes Alcalase and Savinase by Crossed Immunoelectrophoresis and Crossed Radioimmunoelectrophoresis." International Archives of Allergy and Immunology 91, no. 3 (1990): 278–84. http://dx.doi.org/10.1159/000235128.

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25

Maste, Marc C. L., Willem Norde, and Antonie J. W. G. Visser. "Adsorption-Induced Conformational Changes in the Serine Proteinase Savinase: A Tryptophan Fluorescence and Circular Dichroism Study." Journal of Colloid and Interface Science 196, no. 2 (December 1997): 224–30. http://dx.doi.org/10.1006/jcis.1997.5205.

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26

Bekiroglu, Hatice, Gorkem Ozulku, and Osman Sagdic. "Effects of Casein Hydrolysate Prepared with Savinase on the Quality of Bread Made by Frozen Dough." Foods 12, no. 20 (October 20, 2023): 3845. http://dx.doi.org/10.3390/foods12203845.

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The effect of casein savinase hydrolysate (CSH) usage on frozen dough (1%, 1.5% and 2%, g/100 g flour) was investigated in terms of rheological, thermal and structural characteristics of wheat doughs and the textural and color properties of corresponding breads. Rheological measurements showed that CSH addition into dough led to a reduction in G′ and G″ values, but a similar trend was not observed in frozen dough samples. The increase in protein band intensity was observed for control dough (CD) after frozen storage (−30 °C, 28 days), while there were no increases in the band intensities of the doughs with CSH. The freezable water content of unfrozen doughs decreased gradually with the addition of CSH, dependent on concentration level. Frozen storage caused a notable reduction in the α-helices structure of the CD sample (p < 0.05) while no significant variation was observed for the doughs containing CSH (p > 0.05). The lowest specific volume reduction and hardness increment were observed for the breads containing 1.5% and 2% CSH. Frozen storage caused a significant reduction in the b* value of bread crust (p < 0.05), while no significant effect was observed for L* and a* value during frozen storage (p > 0.05). Overall, CSH incorporation into frozen dough can be an alternative that could reduce the quality deterioration of frozen bread.
27

Lipin´ska‐Ojrzanowska, Agnieszka, Dominika S>´wierczyn´ska‐Machura, Diana Tymoszuk, Ewa Nowakowska‐S´wirta, and Jolanta Walusiak‐Skorupa. "Occupational Asthma in Female Factory Worker Resulting from Exposure to Savinase in Dishwashing Tablets—A Case Study." Journal of Occupational Health 55, no. 4 (July 2013): 318–21. http://dx.doi.org/10.1539/joh.12-0169-cs.

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Tekle, Sefik, Gorkem Ozulku, Hatice Bekiroglu, and Osman Sagdic. "Effects of Fish Skin Gelatin Hydrolysates Treated with Alcalase and Savinase on Frozen Dough and Bread Quality." Foods 13, no. 1 (December 30, 2023): 139. http://dx.doi.org/10.3390/foods13010139.

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Fish skin gelatin, as a waste product of sea bream, was used to obtain fish gelatin hydrolysate (FGH) with the treatment of alcalase (alc) and savinase (sav). The functional properties of FGHs and their usage possibilities in frozen dough bread making were investigated. FGH treated with alc showed a higher emulsifying stability index (189 min), while FGH treated with sav showed greater foaming capacity (27.8%) and fat-binding capacity (1.84 mL/g). Bread doughs were produced using two FGHs (alc and sav) and their combination (FGH-alc + FGH-sav). Using FGH treated with these enzymes individually was more effective than their combination in terms of polyacrylamide gel electrophoresis (SDS-PAGE) results and bread quality (specific volume and hardness). The addition of FGH into bread dough showed no significant effect on bread dough viscoelasticity (tan δ), while the increment level of tan δ value for control dough was higher than the dough containing FGH after frozen storage (−30 °C for 30 days). The highest freezable water content (FW%) was found in control dough (33.9%) (p < 0.05). The highest specific volume was obtained for control fresh bread and bread with FGH-alc, while the lowest volume was obtained for fresh bread containing FGH-sav (p < 0.05). After frozen storage of the doughs, the bread with FGH-alc showed the highest specific volume. FGH addition caused a significant reduction in the L* (lightness) value of fresh bread samples when compared to control bread (p < 0.05). This study suggested that usage of FGH-alc in bread making decreased the deterioration effect of frozen storage in terms of the specific volume and hardness of bread.
29

Georgieva, Dessislava, Nicolay Genov, Wolfgang Voelter, and Christian Betzel. "Catalytic Efficiencies of Alkaline Proteinases from Microorganisms." Zeitschrift für Naturforschung C 61, no. 5-6 (June 1, 2006): 445–52. http://dx.doi.org/10.1515/znc-2006-5-623.

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Catalytic efficiencies of proteinase K and mesentericopeptidase were determined using series of peptide-4-nitroanilide substrates and compared with those of subtilisin DY, savinase and esperase. For each enzyme the subsites S1-S4 were characterized. The data for the enzyme specificities were related to our high resolution X-ray models of the five enzymes and their complexes with peptides. The catalytic efficiencies of the alkaline proteinases are modulated by the hydrophobicity, solvent accessibility, flexibility and electrostatic effects in the substrate binding sites. The longer and nonpolar S1 loop offers more possibilities for hydrophobic interactions and increases the enzyme efficiency. S2 is a small narrow cleft which limits the possibilities for effective substitutions in P2. The wide specificity of S3 is due to its location on the protein surface of all investigated proteinases. The affinity of S4 for aromatic groups depends on the nature of the residues building the hydrophobic cavity.
30

Garcia-Mora, Patricia, Elena Peñas, Juana Frias, and Cristina Martínez-Villaluenga. "Savinase, the Most Suitable Enzyme for Releasing Peptides from Lentil (Lens culinaris var. Castellana) Protein Concentrates with Multifunctional Properties." Journal of Agricultural and Food Chemistry 62, no. 18 (April 28, 2014): 4166–74. http://dx.doi.org/10.1021/jf500849u.

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31

Bech, L. M., S. Branner, S. Hastrup, and K. Breddam. "Introduction of a free cysteinyl residue at position 68 in the subtilisin Savinase, based on homology with proteinase K." FEBS Letters 297, no. 1-2 (February 3, 1992): 164–66. http://dx.doi.org/10.1016/0014-5793(92)80351-g.

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32

González-Osuna, María Fernanda, Wilfrido Torres-Arreola, Enrique Márquez-Ríos, Francisco Javier Wong-Corral, Eugenia Lugo-Cervantes, José Carlos Rodríguez-Figueroa, Guillermina García-Sánchez, et al. "Antioxidant Activity of Peptide Fractions from Chickpea Globulin Obtained by Pulsed Ultrasound Pretreatment." Horticulturae 9, no. 4 (March 23, 2023): 415. http://dx.doi.org/10.3390/horticulturae9040415.

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Protein hydrolysates and peptides can show biological activities, and pulsed ultrasound improves bioactivities. Among matrices from which protein hydrolysates can be obtain, chickpea is an excellent source. The objective of this research was to evaluate the effect of pulsed ultrasound on globulin concentrate to obtain chickpea hydrolysate (HGb) and peptide fractions and their bioactivity. Antioxidant activity by ABTS (2,2′-Azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) diammonium salt), FRAP (Ferric Reducing Antioxidant Power) and human erythrocyte assays was determined. The electrophoretic profile, amino acid profile, and antimicrobial activity of hydrolysates were also determined. Two hydrolysates had the highest antioxidant activity: HGb (91.44% ABTS inhibition, 73.04% hemolysis inhibition and 5185.57 µmol TE/g dried sample in FRAP assay) and HGb-20 (48.25% ABTS inhibition, 100% hemolysis inhibition and 2188.53 µmol TE/g dried sample in FRAP assay). Peptide fractions inhibited 100% of the hemolysis on human erythrocytes. The hydrolysates from chickpea proteins obtained with savinase have antioxidant activity through the SET and HAT mechanisms. The application of the obtained compounds for the development of functional foods or for food preservation should be considered.
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Balashev, K., Tz Ivanova, K. Mircheva, and I. Panaiotov. "Savinase proteolysis of insulin Langmuir monolayers studied by surface pressure and surface potential measurements accompanied by atomic force microscopy (AFM) imaging." Journal of Colloid and Interface Science 360, no. 2 (August 2011): 654–61. http://dx.doi.org/10.1016/j.jcis.2011.04.101.

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34

Sørensen, Margrethe, Arne Redsted Rasmussen, and Kim Pilkjær Simonsen. "Enzymatic detection of formalin-fixed museum specimens for DNA analysis and enzymatic maceration of formalin-fixed specimens." Collection Forum 30, no. 1-2 (January 1, 2016): 1–6. http://dx.doi.org/10.14351/0831-4985-30.1.1.

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Abstract A simple enzymatic screening method has been developed to detect whether a tissue sample has been preserved with formalin or with ethanol only because such a method is a useful tool for predicting the quality of genetic test results. The method is based on enzymatic digestion at 55°C at neutral pH. The screening method shows that only ethanol-preserved tissue samples are dissolved, whereas formalin-preserved samples remain undissolved. The method was developed by the incorporation of laboratory rats preserved under controlled conditions in either 4% neutral buffered formalin or 96% ethanol. The method was subsequently tested on wild-living preserved specimens and an archived specimen. The protease enzyme used was Savinase® 16 L, Type EX from Novozymes A/S. The enzymatic screening test demands only simple laboratory equipment. The method is useful for natural history collections in museums where DNA analyses of archived specimens are performed. Wasted time and resources can be avoided through the detection of formalin-fixed specimens because these specimens yield low-quality, damaged DNA. In addition to the screening method, it is shown that formalin-preserved specimens can be macerated by enzymatic digestion under alkaline conditions at 55°C.
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Bautista-Expósito, Sara, Cristina Martínez-Villaluenga, Montserrat Dueñas, Jose Manuel Silván, Juana Frias, and Elena Peñas. "Combination of pH-controlled fermentation in mild acidic conditions and enzymatic hydrolysis by Savinase to improve metabolic health-promoting properties of lentil." Journal of Functional Foods 48 (September 2018): 9–18. http://dx.doi.org/10.1016/j.jff.2018.06.019.

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36

Balashev, Konstantin, Thomas H. Callisen, Allan Svendsen, and Thomas Bjørnholm. "Savinase action on bovine serum albumin (BSA) monolayers demonstrated with measurements at the air–water interface and liquid Atomic Force Microscopy (AFM) imaging." Colloids and Surfaces B: Biointerfaces 88, no. 2 (December 2011): 582–86. http://dx.doi.org/10.1016/j.colsurfb.2011.07.043.

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37

Pedrosa, Nely de Almeida, Cristiano José de Andrade, José Carlos Cunha Petrus, and Alcilene Rodrigues Monteiro. "Sequential Hydrolysis of Chicken Feathers Composed of Ultrasound and Enzymatic Steps: An Enhanced Protein Source with Bioactive Peptides." Biomass 2, no. 4 (September 30, 2022): 237–49. http://dx.doi.org/10.3390/biomass2040016.

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Chicken feather is a massive by-product. Its incorrect disposal can lead to serious environmental impacts. However, chicken feather is a promising low-cost keratin source. Keratin products have a wide application in the food and pharmaceutical industry. Mostly, chicken feathers are hydrolyzed by hydrothermal processes, and then applied into animal feed formulations. Despite the low cost, the hydrothermal hydrolysis leads to uncontrolled and low hydrolysis yield. Therefore, the aim of this work was to develop and optimize a sequential strategy of chicken feathers hydrolysis composed of ultrasound and enzymatic hydrolysis (savinase®) steps. In the first research step an experimental design was built and the optimum hydrolysis condition was obtained at 50 °C and 12.5% (enzyme/chicken feather), using three integrated rectors containing enzyme/substrate and sodium disulfite. Then, the ultrasound probe was added in the experimental apparatus in order to investigate the enzymatic hydrolysis assisted by ultrasound treatment. The enzymatic hydrolysis assisted by ultrasound treatment led to high concentrations of peptides, including a dipeptide (245.1868 m/z). Thus, the sequential hydrolysis strategy composed by two green technologies proposed in this study, enhanced the degree of hydrolysis of chicken feathers, producing bioactive peptides that can be used as ingredients in food products and other sectors.
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Wang, Le, Jinbo Yao, Jiarong Niu, Jianyong Liu, Bo Li, and Mao Feng. "Eco-Friendly and Highly Efficient Enzyme-Based Wool Shrinkproofing Finishing by Multiple Padding Techniques." Polymers 10, no. 11 (October 31, 2018): 1213. http://dx.doi.org/10.3390/polym10111213.

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Wool fibers usually need shrinkproofing finishing. The enzyme process is an eco-friendly technology but the traditional exhaustion treatment usually takes excessive time. This study developed a novel multiple padding shrinkproofing process of wool with Savinase 16L and an organic phosphine compound {[HO(CH2)n]3P, n ∈ (1, 10)}. SEM and XPS analyses were employed to compare the wool treated respectively by exhaustion and by padding to reveal the effect of multiple padding. The results showed that treated wool fiber achieved the requirement of machine-washable (area shrinkage less than 8% according to standard TM 31 5 × 5A) in 2.5 min by the padding process. The padding process can control the adsorbance of enzyme on wool, which makes treatment more uniform and avoids strong damage of the wool. Also, the removal efficiency of the disulfide bond was about 15 times as much as in the exhaustion treatment in 2.5 min. The average catalytic rate of the padding process was 14 times faster than the exhaustion process, and the process time (2.5 min) decreased by 32.5 min compared with the exhaustion process (35 min). Multiple padding techniques can achieve continuous production and replace the environmentally harmful chlorination process. Our results provide the underlying insights needed to guide the research of the enzyme process application.
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Micheelsen, Pernille Ollendorff, Jitka Vévodová, Leonardo De Maria, Peter Rahbek Østergaard, Esben Peter Friis, Keith Wilson, and Michael Skjøt. "Structural and Mutational Analyses of the Interaction between the Barley α-Amylase/Subtilisin Inhibitor and the Subtilisin Savinase Reveal a Novel Mode of Inhibition." Journal of Molecular Biology 380, no. 4 (July 2008): 681–90. http://dx.doi.org/10.1016/j.jmb.2008.05.034.

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40

Georgieva, Dessislava Nikolova, Stanka Stoeva, Wolfgang Voelter, Nicolay Genov, and Christian Betzel. "Differences in the Specificities of the Highly Alkalophilic Proteinases Savinase and Esperase Imposed by Changes in the Rigidity and Geometry of the Substrate Binding Sites." Archives of Biochemistry and Biophysics 387, no. 2 (March 2001): 197–201. http://dx.doi.org/10.1006/abbi.2000.2249.

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41

Jeon, Mi-Jin, and Yong-Woo Jeon. "Enhanced Enzymatic Degradability of Livestock Blood Pretreated with Ultrasonic Technique." Applied Sciences 14, no. 4 (February 19, 2024): 1676. http://dx.doi.org/10.3390/app14041676.

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Livestock blood, a major organic waste generated by the livestock industry, poses a risk of pollution due to its rapid decomposition. However, it is a potential protein source for agricultural purposes due to its protein-rich organic matter. In this study, we conducted studies on an eco-friendly, scalable, and effective protein degradation process using livestock blood to reduce waste and produce an amino acid liquid fertilizer that can be recycled for agricultural use. Ultrasonic technology was applied as a pretreatment method to improve the enzymatic hydrolysis efficiency of proteins in livestock blood, and the optimal conditions that led to 95.91% solubilization rate of hemoglobin were ultrasound duration for 30 min at an ultrasound density of 0.5 W/mL. As a result of hydrolyzing ultrasonically pretreated blood by mixing exo- and endo-type proteolytic enzymes, the optimal combination was a mixture of Savinase® 1% and Flavourzyme® 1%. After 4 h of reaction, the protein concentration was 27.8 mg/mL and the amino acid concentration was confirmed to be 54.6 mg/mL. This is about 4.2 times higher than the amino acid concentration of blood without ultrasound pretreatment, 13.1 mg/mL, and it was confirmed that sonication has a significant effect on improving protein degradation efficiency. As protein degradation increased, the viscosity of blood gradually decreased, suggesting that the physical force applied to the agitator torque diminished during the enzyme reaction; a significant correlation between protein and amino acid concentrations (biological factors) and torque (mechanical factor) was observed. Measuring torque during an enzyme reaction can confirm the extent of the enzyme reaction, so it can be used as an indicator of reaction progress when scaling up the process in the future.
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Christinawati, Evi Lusiana. "ANALISA FAKTOR – FAKTOR YANG MEMPENGARUHI TABUNGAN MASYARAKAT PADA BANK UMUM DENGAN PENDEKATAN MODEL ECM." Jurnal Ekonomi Pembangunan 11, no. 1 (December 1, 2013): 35. http://dx.doi.org/10.22219/jep.v11i1.3729.

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To the effect this Research is subject to be menganalisis factor that regard society savings on public bank by use of approaching ECM wields annual data begin year 1985 until years 2009 be utilized this ECM'S approaching with consideration that this model feels equal to word relationship among variable one is analyzed well that in the short term and also on a long term. In theory PDB, savings rate of interest zoom, inflation rate is influential factor to savingses. studi's result in the short term points out that PDB and rate of interest zoom, having for positive and signifikan to society savings, but negative ascendant inflation whereas in the long term PDB interest rate, positive influential inflation rate to society savings. simultan's ala all that variable gets to be utilized big see it gets what far-reaching to society savings, but partially variable memilki's one the most influence dominant is PDB.
43

Weiss, Jernej. "Klavirske skladbe Rista Savina." Musicological Annual 48, no. 2 (December 1, 2012): 217–27. http://dx.doi.org/10.4312/mz.48.2.217-227.

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Klavirske skladbe Rista Savina ne pomenijo težišča v skladateljevi ustvarjalnosti, čeprav njegov klavirski opus nikakor ni majhen. Glede na celoten skladateljev opus Savinove klavirske kompozicije ne zasedajo ključnih pozicij, a ker je Savin pisal klavirsko glasbo v vseh obdobjih svojega skladateljskega ustvarjanja, njihove karakteristike jasno osvetljujejo njegova posamezna ustvarjalna obdobja.
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Neubauer, Henrik. "Baletna glasba Rista Savina." Musicological Annual 48, no. 2 (December 1, 2012): 165–85. http://dx.doi.org/10.4312/mz.48.2.165-185.

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V članku avtor razčlenjuje glasbena dela skladatelja Rista Savina, ki so povezana s plesom oziroma z baletom. Obravnavana so tako tista dela, ki so bila posebej pisana za baletno uprizoritev (baleta Plesna legendica in Čajna punčka), kot tudi Savinove krajše skladbe, ki so po svoji tematiki namenjene plesni izvedbi ali se tej približujejo.
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Levy, R. "Savings? What savings?" BMJ 343, jul05 3 (July 5, 2011): d4035. http://dx.doi.org/10.1136/bmj.d4035.

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46

Abramov, Alexander E., and Maria I. Chernova. "Improving pension savings investing: The case of Russia." Russian Journal of Economics 10, no. 1 (March 29, 2024): 34–59. http://dx.doi.org/10.32609/j.ruje.10.115594.

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Many countries seek to improve their pension systems by introducing corporate and individual savings plans to address the challenges of demography, social security, and economy. However, the establishing of a long-term, reliable savings system encounters multiple impediments. The retrospective analysis of Russian pension reforms offers some recommendations on solving the typical problems faced by reformers. Thus, in 2002 the Russian pension system was implemented by a mandatory savings pillar, which 20 years later the Ministry of Finance substituted by voluntary savings­. As this period appeared shorter than the average life span, this measure proved ­ineffective in increasing pension payouts for future retirees. The frequent regulatory changes and the shrinking workforce coverage as the state prioritized the welfare of the current pension recipients also infringed upon the interests of future retirees. Pension savings investments were further affected by the economic policy aimed at the minimal return requirements which resulted in a more conservative asset allocation strategy and inefficient active management in non-state pension funds. The study demonstrates that policy actions to overcome these impediments and to raise the replacement rates for future retirees should include (a) steady regulations within a pension savings system of no shorter than 40 years; (b) the savings pillar covering no less than 80% of the workforce; and (c) the asset allocation strategy involving a bigger share of equity, longer time horizon and clear benchmarks. These recommendations can be applied to emerging market economies concerned with improving and reforming their pension systems.
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Nagode, Aleš. "Med domom in svetom: pesmi za glas in klavir Rista Savina." Musicological Annual 48, no. 2 (December 1, 2012): 79–89. http://dx.doi.org/10.4312/mz.48.2.79-89.

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Članek ponuja nov pogled na gradivo povezano z ustvarjalnostjo Rista Savina za glas in klavir. Opozarja na nekaj doslej spregledanih skladb ter poskuša z razširjenim naborom dejstev korigirati uveljavljeno kronologijo nastajanja del. Izsledki znatno spreminjajo dosedanje razumevanje Savinove ustvarjalnosti. Njegova opredelitev za slovensko nacionalno gibanje ni bila nenaden zasuk, kot je to veljalo do sedaj, temveč rezultat dolgotrajnega odzivanja na pobude iz kulturnega okolja, v katerem je deloval.
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Kasim, Arena Che. "SAVINGS PATTERNS AMONG Gen Z YOUTHS." International Journal of Psychosocial Rehabilitation 24, no. 4 (February 28, 2020): 4623–33. http://dx.doi.org/10.37200/ijpr/v24i4/pr201562.

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49

Berner, Robert L., and Linda Hogan. "Savings." World Literature Today 63, no. 4 (1989): 723. http://dx.doi.org/10.2307/40145718.

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50

Klyczek, J. P. "Savings." American Journal of Occupational Therapy 47, no. 3 (March 1, 1993): 270. http://dx.doi.org/10.5014/ajot.47.3.270.

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