碱性蛋白酶洗涤性能的影响因素

doi:10.3969/j.issn.1001-1803.2021.11.011

Abstract

Abstract:

Alkaline protease is one of the most widely used enzymes in liquid detergents. It has a wide range of peptide bond hydrolysis selectivity and can degrade a variety of protein souls. However, unlike the biological environment, various inactivation factors in the harsh liquid detergent environment may lead to the denaturation, performance degradation and cost increase of alkaline protease. Understanding these influencing factors in the complex liquid protease environment is necessary for further improving the washing performance of alkaline protease. This paper firstly addresses the main inactivation factors of alkaline protease in liquid detergent, such as autolysis inactivation and the effect of chelating agent, bleaching agent and surfactant. Special attention is paid to the interaction between surfactant and alkaline protease. Finally, the development of surfactant types and compounding technology in liquid detergent formulation in the future is prospected.

Key words: alkaline protease, chelating agent, bleaching agent, surfactant, liquid laundry detergent, denaturation and inactivation

CLC Number:

TQ649

Wang Penghui,Wang Weixian,Yang Tao,Zeng Hui,Rui Zebao,Li Donghua,Huang Ping. Influencing factors on washing performance of alkaline protease in liquid detergent[J].China Surfactant Detergent & Cosmetics, 2021, 51(11): 1109-1117.

Figures/Tables 7

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References 48

[1]	Mukherjee J, Majumder A B, Gupta M N. Adding an appropriate amino acid during crosslinking results in more stable crosslinked enzyme aggregates[J]. Analytical Biochemistry, 2016, 507:27-32. doi: 10.1016/j.ab.2016.05.012 pmid: 27237371
[2]	Wang J, Zhang J, Zhang Y. Study on the behavior of alkaline protease at air-water interface[J]. China Surfactant Detergent & Cosmetics, 2015, 45(9): 490-494.
[3]	Stoner M R, Dale D A, Gualfetti P J, et al. Protease autolysis in heavy-duty liquid detergent formulations: effects of thermodynamic stabilizers and protease inhibitors[J]. Enzyme Microb Technol, 2004, 34(2): 114-125. doi: 10.1016/j.enzmictec.2003.09.008
[4]	Han X Q, Damodaran S. Stability of protease Q against autolysis and in sodium dodecyl sulfate and urea solutions[J]. Biochemical and Biophysical Research Communications, 1997, 240(3): 839-843. pmid: 9398655
[5]	Mechri S, Bouacem K, Jaouadi N Z, et al. Identification of a novel protease from the thermophilic Anoxybacillus kamchatkensis M1V and its application as laundry detergent additive[J]. Extremophiles, 2019, 23(6): 687-706. doi: 10.1007/s00792-019-01123-6
[6]	Ozturk N C, Kazan D, Denizci A A, et al. The influence of copper on alkaline protease stability toward autolysis and thermal inactivation[J]. Engineering in Life Sciences, 2012, 12(6): 662-671. doi: 10.1002/elsc.v12.6
[7]	Laszlo K, Szava A, Simon L M. Stabilization of various alpha-chymotrypsin forms in aqueous-organic media by additives[J]. Journal of Molecular Catalysis B: Enzymatic, 2001, 16(3/4): 141-146. doi: 10.1016/S1381-1177(01)00053-4
[8]	Dorau R, Gorbe T, Humble M S. Improved enantioselectivity of subtilisin carlsberg towards secondary alcohols by protein engineering[J]. Chembiochem, 2018, 19(4): 338-346. doi: 10.1002/cbic.v19.4
[9]	Russell D, Oldham N J, Davis B G. Site-selective chemical protein glycosylation protects from autolysis and proteolytic degradation[J]. Carbohydrate Research, 2009, 344(12): 1508-1514. doi: 10.1016/j.carres.2009.06.033 pmid: 19608158
[10]	Yu Y, Zhao J, Bayly A E. Development of surfactants and builders in detergent formulations[J]. Chinese Journal of Chemical Engineering, 2008, 16(4): 517-527. doi: 10.1016/S1004-9541(08)60115-9
[11]	Koohsaryan E, Anbia M, Maghsoodlu M. Application of zeolites as non‐phosphate detergent builders: A review[J]. Journal of Environmental Chemical Engineering, 2020, 8(5): 104287. doi: 10.1016/j.jece.2020.104287
[12]	Gotoh K, Horibe K, Mei Y, et al. Effects of water hardness on textile detergency performance in aqueous cleaning systems[J]. Journal of Oleo Science, 2016, 65(2): 123-133. doi: 10.5650/jos.ess15168
[13]	Sharma A K, Kikani B A, Singh S P. Biochemical, thermodynamic and structural characteristics of a biotechnologically compatible alkaline protease from a haloalkaliphilic, Nocardiopsis dassonvillei OK-18[J]. International Journal of Biological Macromolecules, 2020, 153:680-696. doi: S0141-8130(20)31164-8 pmid: 32145232
[14]	Ksiazek M, Karim A Y, Bryzek D, et al. Mirolase, a novel subtilisin-like serine protease from the periodontopathogen Tannerella forsythia[J]. Biological Chemistry, 2015, 396(3): 261-275. doi: 10.1515/hsz-2014-0256
[15]	Li J, Zhang J, Zhao Y X. Progress in research work field with respect to effects of metal ions on protease[J]. China Surfactant Detergent & Cosmetics, 2017, 47(6): 345-351.
[16]	Zhang J, Wang J, Zhao Y, et al. Study on the interaction between calcium ions and alkaline protease of bacillus[J]. International Journal of Biological Macromolecules, 2019, 124:121-130. doi: S0141-8130(18)34153-9 pmid: 30471394
[17]	Gohel S D, Singh S P. Thermodynamics of a Ca²⁺-dependent highly thermostable alkaline protease from a haloalkliphilic actinomycete[J]. International Journal of Biological Macromolecules, 2015, 72:421-429. doi: 10.1016/j.ijbiomac.2014.08.008 pmid: 25150113
[18]	Lund H, Kaasgaard S G, Skagerlind P, et al. Protease and amylase stability in the presence of chelators used in laundry detergent applications: correlation between chelator properties and enzyme stability in liquid detergents[J]. Journal of Surfactants and Detergents, 2012, 15(3): 265-276. doi: 10.1007/s11743-011-1318-8
[19]	Bakhtiar S, Andersson M M, Gessesse A, et al. Stability characteristics of a calcium-independent alkaline protease from Nesterenkonia sp.[J]. Enzyme Microb Technol, 2003, 32(5): 525-531. doi: 10.1016/S0141-0229(02)00336-8
[20]	Veltman O R, Vriend G, Van Den Burg B, et al. Engineering thermolysin-like proteases whose stability is largely independent of calcium[J]. FEBS Letters, 1997, 405(2): 241-244. pmid: 9089298
[21]	Haddar A, BougateF A, Agrebi R, et al. A novel surfactant-stable alkaline serine-protease from a newly isolated Bacillus mojavensis A21. Purification and characterization[J]. Process Biochemistry, 2009, 44(1): 29-35. doi: 10.1016/j.procbio.2008.09.003
[22]	Ghorbel B, SellamI-Kamoun A, Nasri M. Stability studies of protease from Bacillus cereus BG1[J]. Enzyme Microb Technol, 2003, 32(5): 513-518. doi: 10.1016/S0141-0229(03)00004-8
[23]	Crudden J J, Parker B A, Lazzaro J V. The properties and applications of N-acyl ED3A chelating surfactants[J]. Industrial Applications of Surfactants IV, 1999: 130-150.
[24]	Rischmiller M S, Smith K R, Peters S B, et al. Enzyme-containing detergent and presoak composition and methods of using[M]. Canada: Thomson Reuters, 2018: 350-351.
[25]	Grune T, Klotz L O, Gieche J, et al. Protein oxidation and proteolysis by the nonradical oxidants singlet oxygen or peroxynitrite[J]. Free Radical Biology and Medicine, 2001, 30(11): 1243-1253. pmid: 11368922
[26]	Estévez M. Protein carbonyls in meat systems: A review[J]. Meat Science, 2011, 89(3): 259-279. doi: 10.1016/j.meatsci.2011.04.025 pmid: 21621336
[27]	Xiong Y L, Blanchard S P, Ooizumi T, et al. Hydroxyl radical and ferryl-generating systems promote gel network formation of myofibrillar protein[J]. Journal of Food Science, 2010, 75(2): 215-221. doi: 10.1111/j.1750-3841.2009.01511.x
[28]	Zhang B, Yang Y, Luo B, et al. Effects of different foods on blood glucose and lipid in type 2 diabetes mellitus in a rat model[J]. Journal of Surgical Research, 2018, 229:254-261. doi: S0022-4804(18)30128-8 pmid: 29936998
[29]	Hammami A, Hamdi M, Abdelhedi O, et al. Surfactant- and oxidant-stable alkaline proteases from Bacillus invictae: Characterization and potential applications in chitin extraction and as a detergent additive[J]. International Journal of Biological Macromolecules, 2017, 96:272-281. doi: S0141-8130(16)32119-5 pmid: 27988295
[30]	Von Der Osten C, Branner S, Hastrup S, et al. Protein engineering of subtilisins to improve stability in detergent formulations[J]. Journal of Biotechnology, 1993, 28(1): 55-68. pmid: 7763525
[31]	Cheng K C, Khoo Z S, Lo N W, et al. Design and performance optimisation of detergent product containing binary mixture of anionic-nonionic surfactants[J]. Heliyon, 2020, 6(5): e03861. doi: 10.1016/j.heliyon.2020.e03861
[32]	Otzen D. Protein-surfactant interactions: A tale of many states[J]. Biochimica Et Biophysica Acta-Proteins and Proteomics, 2011, 1814(5): 562-591. doi: 10.1016/j.bbapap.2011.03.003
[33]	Holmberg K. Interactions between surfactants and hydrolytic enzymes[J]. Colloid Surf B-Biointerfaces, 2018, 168:169-177. doi: 10.1016/j.colsurfb.2017.12.002
[34]	Wu M N, Li L, Xia Y H, et al. Improvement of proteases stability in liquid laundry detergent[J]. China Surfactant Detergent & Cosmetics, 2019, 49(2): 103-107.
[35]	Ghosh S. Interaction of trypsin with sodium dodecyl sulfate in aqueous medium: A conformational view[J]. Colloid Surf B-Biointerfaces, 2008, 66(2): 178-186. doi: 10.1016/j.colsurfb.2008.06.011
[36]	Russell G L, Britton L N. Use of certain alcohol ethoxylates to maintain protease stability in the presence of anionic surfactants[J]. Journal of Surfactants and Detergents, 2002, 5(1): 5-10. doi: 10.1007/s11743-002-0198-9
[37]	Guncheva M, Stippler E. Effect of four commonly used dissolution media surfactants on pancreatin proteolytic activity[J]. AAPS PharmSciTech, 2017, 18(4): 1402-1407. doi: 10.1208/s12249-016-0618-8 pmid: 27586964
[38]	Sinha R, Khare S K. Characterization of detergent compatible protease of a halophilic Bacillus sp. EMB9: Differential role of metal ions in stability and activity[J]. Bioresource Technology, 2013, 145:357-361. doi: 10.1016/j.biortech.2012.11.024
[39]	David A, Singh Chauhan P, Kumar A, et al. Coproduction of protease and mannanase from Bacillus nealsonii PN-11 in solid state fermentation and their combined application as detergent additives[J]. International Journal of Biological Macromolecules, 2018, 108:1176-1184. doi: 10.1016/j.ijbiomac.2017.09.037
[40]	Verma S K, Ghosh K K, Verma R, et al. Surface, conformational and catalytic activity approach of ot-chymotrypsin and trypsin in micellar media[J]. Colloids and Surfaces A: Physicochemical and Engineering Aspects, 2015, 470:188-193. doi: 10.1016/j.colsurfa.2015.01.070
[41]	Raval V H, Pillai S, Rawal C M, et al. Biochemical and structural characterization of a detergent-stable serine alkaline protease from seawater haloalkaliphilic bacteria[J]. Process Biochemistry, 2014, 49(6): 955-962. doi: 10.1016/j.procbio.2014.03.014
[42]	Giehm L, Oliveira C L P, Christiansen G, et al. SDS-induced fibrillation of α-synuclein: an alternative fibrillation pathway[J]. Journal of Molecular Biology, 2010, 401(1): 115-133. doi: 10.1016/j.jmb.2010.05.060 pmid: 20540950
[43]	Andersen K K, Oliveira C L, Larsen K L, et al. The role of decorated SDS micelles in sub-CMC protein denaturation and association[J]. Journal of Molecular Biology, 2009, 391(1): 207-226. doi: 10.1016/j.jmb.2009.06.019 pmid: 19523473
[44]	Otzen D E, Oliveberg M. Burst-phase expansion of native protein prior to global unfolding in SDS11Edited by A. R. Fersht[J]. Journal of Molecular Biology, 2002, 315(5): 1231-1240. doi: 10.1006/jmbi.2001.5300
[45]	Chakraborty A, Basak S. Effect of surfactants on casein structure: A spectroscopic study[J]. Colloid Surf B: Biointerfaces, 2008, 63(1): 83-90. doi: 10.1016/j.colsurfb.2007.11.005
[46]	Turro N J, Lei X G, Ananthapadmanabhan K P, et al. Spectroscopic probe analysis of protein-surfactant interactions: the BSA/SDS system[J]. Langmuir, 1995, 11(7): 2525-2233. doi: 10.1021/la00007a035
[47]	Reynolds J A, Tanford C. The gross conformation of protein-sodium dodecyl sulfate complexes[J]. The Journal of Biological Chemistry, 1970, 245(19): 5161-5165. doi: 10.1016/S0021-9258(18)62831-5
[48]	Shirahama K. Free-boundary electrophoresis of sodium dodecyl sulfate-protein polypeptide comlexes with special reference to SDS-polyacrylamide gel electrophoresis[J]. J Biochem, 1974, 75(2): 309-328. pmid: 4837445

代表性螯合剂	类型	蛋白酶	与钙离子的结合度	参考文献
EDTA	有机型	Bacillus mojavensis A21 protease	较强	[21]
柠檬酸盐	有机型	Bacillus lentus	较弱	[18]
硼酸盐	无机型	Bacillus cereus BG1 protease	一般	[22]
N-酰基ED3A	有机型	Subtilisin Carlsberg	较强	[23]
NTA（氨三乙酸）	有机型	Subtilisin Carlsberg	较弱	[11]
N-羟乙基亚胺二乙酸	有机型	Subtilisin Carlsberg	很强	[10]
聚丙烯酸	高分子型	Subtilisin Carlsberg	很强	[24]
马来酸-丙烯酸共聚物	高分子型	Subtilisin Carlsberg	很强	[11]

表面活性剂	种类	蛋白酶	稳定性的影响	参考文献
SDS	阴离子型	Trypsin	很强	[35]
LAS	阴离子型	Subtilisin Carlsberg	很强	[36]
AES	阴离子型	Purafect Prime	一般	[34]
Trion X-100	非离子型	Bacillus invictae	很弱	[29]
Twenn-80	非离子型	Pancreatic proteases	很弱	[37]
APEs	非离子型	Subtilisin Carlsberg	较弱	[10]
AEO	非离子型	Bacillus sp. EMB9 protease	较弱	[38]
CTAB	阳离子型	Bacillus nealsonii PN-11 protease	较强	[39]
甜菜碱类	两性离子型	α-chymotrypsin	一般	[40]

Influencing factors on washing performance of alkaline protease in liquid detergent

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