Abstract
Enzymes are proteins that act as highly efficient catalysts in biochemical reactions. This catalytic capability is what makes enzymes unique and they work efficiently, rapidly, and are biodegradable. The use of enzymes frequently results in many benefits that cannot be obtained with traditional chemical treatments. These often include higher product quality and lower manufacturing cost, less waste, and reduced energy consumption. Industrial enzymes represent the heart of biotechnology processes and biotechnology (Whitehurst and van Oort 2009; Sabalza et al. 2014)
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References
Agboola S, Chen S, Zhao J (2004) Formation of bitter peptides during ripening of ovine milk cheese made with different coagulants. Dairy Sci Technol 84:567–578. https://doi.org/10.1051/lait:2004032
Almeida CM, Simões I (2018) Cardoon-based rennets for cheese production. Appl Microbiol Biotechnol 102:4675–4686. https://doi.org/10.1007/s00253-018-9032-3
Andallu B, Varadacharyulu NC (2003) Antioxidant role of mulberry (Morus indica L. cv. Anantha) leaves in streptozotocin-diabetic rats. Clin Chim Acta 338:3–10. https://doi.org/10.1016/S0009-8981(03)00322-X
Andallu B, Suryakantham V, Lakshmi Srikanthi B, Kesava Reddy G (2001) Effect of mulberry (Morus indica L.) therapy on plasma and erythrocyte membrane lipids in patients with type 2 diabetes. Clin Chim Acta 314:47–53. https://doi.org/10.1016/S0009-8981(01)00632-5
Andreu D, Carreño C, Linde C et al (1999) Identification of an anti-mycobacterial domain in NK-lysin and granulysin. Biochem J 344(Pt 3):845–849
Antão CM, Malcata FX (2005) Plant serine proteases: biochemical, physiological and molecular features. Plant Physiol Biochem 43:637–650. https://doi.org/10.1016/J.PLAPHY.2005.05.001
Arima K, Uchikoba T, Yonezawa H et al (2000a) Isolation and characterization of a serine protease from the sprouts of Pleioblastus hindsii Nakai. Phytochemistry 54:559–565. https://doi.org/10.1016/S0031-9422(00)00075-3
Arima K, Uchikoba T, Yonezawa H et al (2000b) Cucumisin-like protease from the latex of Euphorbia supina. Phytochemistry 53:639–644. https://doi.org/10.1016/S0031-9422(99)00605-6
Asakura T, Watanabe H, Abe K, Arai S (1997) Oryzasin as an aspartic proteinase occurring in rice seeds: purification, characterization, and application to milk clotting. J Agric Food Chem 45:1070–1075. https://doi.org/10.1021/JF960582X
Asano N, Yamashita T, Yasuda K et al (2001) Polyhydroxylated alkaloids isolated from mulberry trees (Morus alba L.) and silkworms (Bombyx mori L.). J Agric Food Chem 49:4208–4213
Asif-Ullah M, Kim K-S, Yu YG (2006) Purification and characterization of a serine protease from Cucumis trigonus Roxburghi. Phytochemistry 67:870–875. https://doi.org/10.1016/J.PHYTOCHEM.2006.02.020
Azarkan M, El Moussaoui A, van Wuytswinkel D et al (2003) Fractionation and purification of the enzymes stored in the latex of Carica papaya. J Chromatogr B 790:229–238. https://doi.org/10.1016/S1570-0232(03)00084-9
Bailey AJ, Light ND (1989) Connective tissue in meat and meat products. Livest Prod Sci 27:263–264. https://doi.org/10.1016/0301-6226(91)90102-V
Barrett AJ (1994) Classification of peptidases. Methods Enzymol 244:1–15. https://doi.org/10.1016/0076-6879(94)44003-4
Barrett AJ, Rawlings ND, Woessner JF (1998) Handbook of proteolytic enzymes. Elsevier, Amsterdam
Bartel B, Fink GR (1995) ILR1, an amidohydrolase that releases active indole-3-acetic acid from conjugates. Science 268:1745–1748
Bartling D, Nosek J (1994) Molecular and immunological characterization of leucine aminopeptidase in Arabidopsis thaliana: a new antibody suggests a semi-constitutive regulation of a phylogenetically old enzyme. Plant Sci 99:199–209. https://doi.org/10.1016/0168-9452(94)90177-5
Batkin S, Taussig S, Szekerczes J (1988) Modulation of pulmonary metastasis (Lewis lung carcinoma) by bromelain, an extract of the pineapple stem (Ananas comosus). Cancer Investig 6:241–242. https://doi.org/10.3109/07357908809077053
Beers EP, Woffenden BJ, Zhao C (2000) Plant proteolytic enzymes: possible roles during programmed cell death. Plant Mol Biol 44:399–415. https://doi.org/10.1023/A:1026556928624
Bhalerao R, Keskitalo J, Sterky F et al (2003) Gene expression in autumn leaves. Plant Physiol 131:430–442. https://doi.org/10.1104/pp.012732
Bölter B, Nada A, Fulgosi H, Soll J (2006) A chloroplastic inner envelope membrane protease is essential for plant development. FEBS Lett 580:789–794. https://doi.org/10.1016/j.febslet.2005.12.098
Brodelius PE, Cordeiro MC, Pais MS (1995) Aspartic proteinases (cyprosins) from Cynara Cardunculus spp. Flavescens cv. cardoon; purification, characterisation, and tissue-specific expression. Springer, Boston, pp 255–266
Bruhn H (2005) A short guided tour through functional and structural features of saposin-like proteins. Biochem J 389:249–257. https://doi.org/10.1042/BJ20050051
Buchanan-Wollaston V (1997) The molecular biology of leaf senescence. J Exp Bot 48:181–199. https://doi.org/10.1093/jxb/48.2.181
de Carvalho MHC, D’Arcy-Lameta A, Roy-Macauley H et al (2001) Aspartic protease in leaves of common bean (Phaseolus vulgaris L.) and cowpea (Vigna unguiculata L. Walp): enzymatic activity, gene expression and relation to drought susceptibility. FEBS Lett 492:242–246. https://doi.org/10.1016/S0014-5793(01)02259-1
Casamitjana-Martınez E, Hofhuis HF, Xu J et al (2003) Root-specific CLE19 overexpression and the sol1/2 suppressors implicate a CLV-like pathway in the control of arabidopsis root meristem maintenance. Curr Biol 13:1435–1441. https://doi.org/10.1016/S0960-9822(03)00533-5
Chao WS, Gu Y-Q, Pautot V et al (1999) Leucine aminopeptidase RNAs, proteins, and activities increase in response to water deficit, salinity, and the wound signals systemin, methyl jasmonate, and abscisic acid. Plant Physiol 120:979–992. https://doi.org/10.1104/PP.120.4.979
Chao WS, Pautot V, Holzer FM, Walling LL (2000) Leucine aminopeptidases: the ubiquity of LAP-N and the specificity of LAP-A. Planta 210:563–573. https://doi.org/10.1007/s004250050045
Chen M, Choi Y, Voytas DF, Rodermel S (2000) Mutations in the Arabidopsis VAR2 locus cause leaf variegation due to the loss of a chloroplast FtsH protease. Plant J 22:303–313. https://doi.org/10.1046/j.1365-313x.2000.00738.x
Chen G, Bi YR, Li N (2005) EGY1 encodes a membrane-associated and ATP-independent metalloprotease that is required for chloroplast development. Plant J 41:364–375. https://doi.org/10.1111/j.1365-313X.2004.02308.x
Chen J, Burke JJ, Velten J, Xin Z (2006) FtsH11 protease plays a critical role in Arabidopsis thermotolerance. Plant J 48:73–84. https://doi.org/10.1111/j.1365-313X.2006.02855.x
Cheon BS, Kim YH, Son KS et al (2000) Effects of prenylated flavonoids and biflavonoids on lipopolysaccharide-induced nitric oxide production from the mouse macrophage cell line RAW 264.7. Planta Med 66:596–600. https://doi.org/10.1055/s-2000-8621
Coffeen WC, Wolpert TJ (2004) Purification and characterization of serine proteases that exhibit caspase-like activity and are associated with programmed cell death in Avena sativa. Plant Cell Online 16:857–873. https://doi.org/10.1105/tpc.017947
Combier J-P, Vernié T, de Billy F et al (2007) The MtMMPL1 early nodulin is a novel member of the matrix metalloendoproteinase family with a role in Medicago truncatula infection by Sinorhizobium meliloti. Plant Physiol 144:703–716. https://doi.org/10.1104/pp.106.092585
Cordeiro MC, Pais MS, Brodelius PE (1994) Tissue-specific expression of multiple forms of cyprosin (aspartic proteinase) in flowers of Cynara cardunculus. Physiol Plant 92:645–653. https://doi.org/10.1111/j.1399-3054.1994.tb03035.x
Davies DR (1990) The structure and function of the aspartic proteinases. Annu Rev Biophys Biophys Chem 19:189–215. https://doi.org/10.1146/annurev.bb.19.060190.001201
Davies RT, Goetz DH, Lasswell J et al (1999) IAR3 encodes an auxin conjugate hydrolase from Arabidopsis. Plant Cell 11:365–376. https://doi.org/10.1105/TPC.11.3.365
Delorme VG, McCabe PF, Kim DJ, Leaver CJ (2000) A matrix metalloproteinase gene is expressed at the boundary of senescence and programmed cell death in cucumber. Plant Physiol 123:917–927
van der Hoorn RAL (2008) Plant proteases: from phenotypes to molecular mechanisms. Annu Rev Plant Biol 59:191–223. https://doi.org/10.1146/annurev.arplant.59.032607.092835
Déry O, Corvera CU, Steinhoff M, Bunnett NW (1998) Proteinase-activated receptors: novel mechanisms of signaling by serine proteases. Am J Physiol Physiol 274:C1429–C1452. https://doi.org/10.1152/ajpcell.1998.274.6.C1429
Distefano S, Palma J, McCarthy I, del Rio L (1999) Proteolytic cleavage of plant proteins by peroxisomal endoproteases from senescent pea leaves. Planta 209:308–313
Doi E, Shibata D, Matoba T, Yonezawa D (1980) Characterization of pepstatin-sensitive acid protease in resting rice seeds. Agric Biol Chem 44:741–747. https://doi.org/10.1080/00021369.1980.10864028
Doi K, Kojima T, Fujimoto Y (2000) Mulberry leaf extract inhibits the oxidative modification of rabbit and human low density lipoprotein. Biol Pharm Bull 23:1066–1071. https://doi.org/10.1248/bpb.23.1066
Doi K, Kojima T, Makino M et al (2001) Studies on the constituents of the leaves of Morus alba L. Chem Pharm Bull 49:151–153. https://doi.org/10.1248/cpb.49.151
Domingos A, Cardoso PC, Xue Z et al (2000) Purification, cloning and autoproteolytic processing of an aspartic proteinase from Centaurea calcitrapa. Eur J Biochem 267:6824–6831. https://doi.org/10.1046/j.1432-1327.2000.01780.x
Domsalla A, Melzig M (2008) Occurrence and properties of proteases in plant lattices. Planta Med 74:699–711. https://doi.org/10.1055/s-2008-1074530
Dryjanski M, Otlewski J, Polanowski A, Wilusz T (1990) Serine proteinase from cucurbita ficifolia seed; purification, properties, substrate specificity and action on native squash trypsin inhibitor (CMTI I). Biol Chem Hoppe Seyler 371:889–896. https://doi.org/10.1515/bchm3.1990.371.2.889
Dubey VK, Pande M, Singh BK, Jagannadham MV (2007) Papain-like proteases: applications of their inhibitors. Afr J Biotechnol 6:1077–1086. https://doi.org/10.4314/ajb.v6i9.57108
Dunn BM (2002) Structure and mechanism of the pepsin-like family of aspartic peptidases. Chem Rev 102:4431–4458. https://doi.org/10.1002/chin.200306266
Estelle M (2001) Proteases and cellular regulation in plants. Curr Opin Plant Biol 4:254–260. https://doi.org/10.1016/S1369-5266(00)00169-2
Esteves CLC, Lucey JA, Pires EMV (2001) Mathematical modelling of the formation of rennet-induced gels by plant coagulants and chymosin. J Dairy Res 68(3):499–510. https://doi.org/10.1017/S0022029901005027
Esteves CLC, Lucey JA, Wang T, Pires EMV (2003) Effect of pH on the gelation properties of skim milk gels made from plant coagulants and chymosin. J Dairy Sci 86:2558–2567. https://doi.org/10.3168/JDS.S0022-0302(03)73850-8
Faro C, Gal S (2005) Aspartic proteinase content of the arabidopsis genome. Curr Protein Pept Sci 6:493–500. https://doi.org/10.2174/138920305774933268
Faro CJ, Moir AJG, Pires EV (1992) Specificity of a milk clotting enzyme extracted from the thistle Cynara cardunculus L.: Action on oxidised insulin and k-casein. Biotechnol Lett 14:841–846. https://doi.org/10.1007/BF01029150
Feijoo-Siota L, Villa TG (2011) Native and biotechnologically engineered plant proteases with industrial applications. Food Bioprocess Technol 4:1066–1088. https://doi.org/10.1007/s11947-010-0431-4
Fernández-Salguero J, Prados F, Calixto F et al (2003) Use of recombinant cyprosin in the manufacture of Ewe’s milk cheese. J Agric Food Chem 51:7426–7430. https://doi.org/10.1021/jf034573h
Fontanini D, Jones B (2002) SEP-1 - a subtilisin-like serine endopeptidase from germinated seeds of Hordeum vulgare L. cv. Morex. Planta 215:885–893. https://doi.org/10.1007/s00425-002-0823-4
Foroughi F, Keshavarz T, Evans CS (2006) Specificities of proteases for use in leather manufacture. J Chem Technol Biotechnol 81:257–261. https://doi.org/10.1002/jctb.1367
García-Lorenzo M, Sjödin A, Jansson S, Funk C (2006) Protease gene families in populus and arabidopsis. BMC Plant Biol 6:30. https://doi.org/10.1186/1471-2229-6-30
Garcia-Martinez JL, Moreno J (1986) Proteolysis of ribulose-1,5-bisphosphate carboxylase/oxygenase in Citrus leaf extracts. Physiol Plant 66:377–383. https://doi.org/10.1111/j.1399-3054.1986.tb05938.x
Genelhu MS, Zanini MS, Veloso IF et al (1998) Use of a cysteine proteinase from Carica candamarcensis as a protective agent during DNA extraction. Braz J Med Biol Res 31:1129–1132
Glathe S, Kervinen J, Nimtz M et al (1998) Transport and activation of the vacuolar aspartic proteinase phytepsin in barley (Hordeum vulgare L.). J Biol Chem 273:31230–31236. https://doi.org/10.1074/JBC.273.47.31230
Golldack D, Popova OV, Dietz K-J (2002) Mutation of the matrix metalloproteinase At2-MMP inhibits growth and causes late flowering and early senescence in Arabidopsis. J Biol Chem 277:5541–5547. https://doi.org/10.1074/jbc.M106197200
González-Rábade N, Badillo-Corona JA, Aranda-Barradas JS (2011) Production of plant proteases in vivo and in vitro--a review. Biotechnol Adv 29:983–996. https://doi.org/10.1016/J.BIOTECHADV.2011.08.017
Graham JS, Xiong J, Gillikin JW (1991) Purification and developmental analysis of a metalloendoproteinase from the leaves of glycine max. Plant Physiol 97:786–792. https://doi.org/10.1104/PP.97.2.786
Groover A, Jones A (1999) Tracheary element differentiation uses a novel mechanism coordinating programmed cell death and secondary cell wall synthesis. Plant Physiol 119:375–384
Gu Y-Q, Holzer FM, Walling LL (1999) Overexpression, purification and biochemical characterization of the wound-induced leucine aminopeptidase of tomato. Eur J Biochem 263:726–735. https://doi.org/10.1046/j.1432-1327.1999.00548.x
Guevara MG, Oliva CR, Machinandiarena M, Daleo GR (1999) Purification and properties of an aspartic protease from potato tuber that is inhibited by a basic chitinase. Physiol Plant 106:164–169. https://doi.org/10.1034/j.1399-3054.1999.106203.x
Guevara MG, Daleo GR, Oliva CR (2001) Purification and characterization of an aspartic protease from potato leaves. Physiol Plant 112:321–326. https://doi.org/10.1034/j.1399-3054.2001.1120304.x
Guevara MG, Oliva CR, Huarte M, Daleo GR (2002) An aspartic protease with antimicrobial activity is induced after infection and wounding in intercellular fluids of potato tubers. Eur J Plant Pathol 108:131–137. https://doi.org/10.1023/A:1015049629736
Guevara MG, Veríssimo P, Pires E et al (2004) Potato aspartic proteases: induction, antimicrobial activity and substrate specificity. J Plant Pathol 86:233–238. https://doi.org/10.2307/41992430
Guevara MG, Almeida C, Mendieta JR et al (2005) Molecular cloning of a potato leaf cDNA encoding an aspartic protease (StAsp) and its expression after P. infestans infection. Plant Physiol Biochem 43:882–889. https://doi.org/10.1016/J.PLAPHY.2005.07.004
Guimarães-Ferreira CA, Rodrigues EG, Mortara RA et al (2007) Antitumor effects in vitro and in vivo and mechanisms of protection against melanoma B16F10-Nex2 cells by fastuosain, a cysteine proteinase from Bromelia fastuosa. Neoplasia 9:723–733
Hartley BS (1960) Proteolytic enzymes. Annu Rev Biochem 29:45–72. https://doi.org/10.1146/annurev.bi.29.070160.000401
Headon DR, Walsh G (1994) The industrial production of enzymes. Biotechnol Adv 12:635–646. https://doi.org/10.1016/0734-9750(94)90004-3
Heimgartner U, Pietrzak M, Geertsen R et al (1990) Purification and partial characterization of milk clotting proteases from flowers of Cynara cardunculus. Phytochemistry 29:1405–1410. https://doi.org/10.1016/0031-9422(90)80090-4
Helliwell CA, Chin-Atkins AN, Wilson IW et al (2001) The arabidopsis AMP1 gene encodes a putative glutamate carboxypeptidase. Plant Cell 13:2115–2125
Hildmann T, Ebneth M, Peña-Cortés H et al (1992) General roles of abscisic and jasmonic acids in gene activation as a result of mechanical wounding. Plant Cell 4:1157–1170. https://doi.org/10.1105/tpc.4.9.1157
Hiraiwa N, Kondo M, Nishimura M, Hara-Nishimura I (1997) An aspartic endopeptidase is involved in the breakdown of propeptides of storage proteins in protein-storage vacuoles of plants. Eur J Biochem 246:133–141. https://doi.org/10.1111/j.1432-1033.1997.00133.x
Huang T-K, McDonald KA (2009) Bioreactor engineering for recombinant protein production in plant cell suspension cultures. Biochem Eng J 45:168–184. https://doi.org/10.1016/J.BEJ.2009.02.008
Huffaker R (1990) Proteolytic activity during senescence of plants. New Phytol 116:199–231. https://doi.org/10.1111/j.1469-8137.1990.tb04710.x
Jang M-H, Kim H, Shin M-C et al (2002) Administration of folium mori extract decreases nitric oxide synthase expression in the hypothalamus of streptozotocin-induced diabetic rats. Jpn J Pharmacol 90:189–192. https://doi.org/10.1254/jjp.90.189
Kaneda M, Tominaga N (1975) J Biochem 78:1287–1296
Kelly GS (1996) Bromelain: a literature review and discussion of its therapeutic applications. Altern Med Rev 11:243–257
Kervinen J, Tobin GJ, Costa J et al (1999) Crystal structure of plant aspartic proteinase prophytepsin: inactivation and vacuolar targeting. EMBO J 18:3947–3955. https://doi.org/10.1093/emboj/18.14.3947
Kim K-M, Kim MY, Yun PY et al (2007) Production of multiple shoots and plant regeneration from leaf segments of fig tree (Ficus carica L.). J Plant Biol 50:440–446. https://doi.org/10.1007/BF03030680
Kleef R, Delohery TM, Bovbjerg DH (1996) Selective modulation of cell adhesion molecules on lymphocytes by bromelain protease 5. Pathobiology 64:339–346. https://doi.org/10.1159/000164070
La Valle JB, Krinsky DL, Hawkins EB (2000) Natural therapeutics pocket guide, 2nd edn. Lexi-Comp, Hudson
Laplaze L, Ribeiro A, Franche C et al (2000) Characterization of a Casuarina glauca nodule-specific subtilisin-like protease gene, a homolog of Alnus glutinosa ag12. Mol Plant-Microbe Interact 13:113–117. https://doi.org/10.1094/MPMI.2000.13.1.113
Lawrie R (1985) Meat science. Pergamon, London
Lee KL, Albee KL, Bernasconi RJ, Edmunds T (1997) Complete amino acid sequence of ananain and a comparison with stem bromelain and other plant cysteine proteases. Biochem J 327(Pt 1):199–202
Leipner J, Iten F, Saller R (2001) Therapy with proteolytic enzymes in rheumatic disorders. BioDrugs 15:779–789
Lindholm P, Kuittinen T, Sorri O et al (2000) Glycosylation of phytepsin and expression of dad1, dad2 and ost1 during onset of cell death in germinating barley scutella. Mech Dev 93:169–173. https://doi.org/10.1016/S0925-4773(00)00254-9
Liu Y, Dammann C, Bhattacharyya MK (2001) The matrix metalloproteinase gene GmMMP2 is activated in response to pathogenic infections in soybean. Plant Physiol 127:1788–1797
López LMI, Sequeiros C, Natalucci CL et al (2000) Purification and Characterization of Macrodontain I, a Cysteine Peptidase from Unripe Fruits of Pseudananas macrodontes (Morr.) Harms (Bromeliaceae). Protein Expr Purif 18:133–140. https://doi.org/10.1006/prep.1999.1165
Losada Cosmes E (1999) Importancia de las enzimas en el asma ocupacional. http://www.alergoaragon.org/1999/tercera2.html. Accessed 1 Jun 2018
Lotti T, Mirone V, Imbimbo C et al (1993) Controlled clinical studies of nimesulide in the treatment of urogenital inflammation. Drugs 46(Suppl 1):144–146
Maidment JM, Moore D, Murphy GP et al (1999) Matrix metalloproteinase homologues from Arabidopsis thaliana. Expression and activity. J Biol Chem 274:34706–34710. https://doi.org/10.1074/JBC.274.49.34706
Mandal MK, Fischer R, Schillberg S, Schiermeyer A (2010) Biochemical properties of the matrix metalloproteinase NtMMP1 from Nicotiana tabacum cv. BY-2 suspension cells. Planta 232:899–910. https://doi.org/10.1007/s00425-010-1221-y
Massova I, Kotra LP, Fridman R, Mobashery S (1998) Matrix metalloproteinases: structures, evolution, and diversification. FASEB J 12:1075–1095. https://doi.org/10.1096/fasebj.12.12.1075
McGeehan G, Burkhart W, Anderegg R et al (1992) Sequencing and characterization of the soybean leaf metalloproteinase: structural and functional similarity to the matrix metalloproteinase family. Plant Physiol 99:1179–1183. https://doi.org/10.1104/PP.99.3.1179
Meichtry J, Amrhein N, Schaller A (1999) Characterization of the subtilase gene family in tomato (Lycopersicon esculentum Mill.). Plant Mol Biol 39:749–760. https://doi.org/10.1023/A:1006193414434
Melis GB (1990) Clinical experience with methoxybutropate vs. bromelin in the treatment of female pelvic inflammation. Minerva Ginecol 42:309–312
Mello VJ, Gomes MTR, Lemos FO et al (2008) The gastric ulcer protective and healing role of cysteine proteinases from Carica candamarcensis. Phytomedicine 15:237–244. https://doi.org/10.1016/J.PHYMED.2007.06.004
Mendieta JR, Pagano MR, Muñoz FF et al (2006) Antimicrobial activity of potato aspartic proteases (StAPs) involves membrane permeabilization. Microbiology 152:2039–2047. https://doi.org/10.1099/mic.0.28816-0
Michalek M, Leippe M (2015) Mechanistic insights into the lipid interaction of an ancient saposin-like protein. Biochemistry 54:1778–1786. https://doi.org/10.1021/acs.biochem.5b00094
Miller A (1982) Improved sausage casing. US patent 3(666) 844
Munford RS, Sheppard PO, O’Hara PJ (1995) Saposin-like proteins (SAPLIP) carry out diverse functions on a common backbone structure. J Lipid Res 36:1653–1663
Muñoz FF, Mendieta JR, Pagano MR et al (2010) The swaposin-like domain of potato aspartic protease (StAsp-PSI) exerts antimicrobial activity on plant and human pathogens. Peptides 31:777–785. https://doi.org/10.1016/J.PEPTIDES.2010.02.001
Mutlu A, Chen X, Reddy SM, Gal S (1999) The aspartic proteinase is expressed in Arabidopsis thaliana seeds and localized in the protein bodies. Seed Sci Res 9:75–84. https://doi.org/10.1017/S0960258599000082
Nomura T (1999) The chemistry and biosynthesis of isoprenylated flavonoids from moraceous plants. Pure Appl Chem 71:1115–1118. https://doi.org/10.1351/pac199971061115
O’Brien JS, Kishimoto Y (1991) Saposin proteins: structure, function, and role in human lysosomal storage disorders. FASEB J 5:301–308. https://doi.org/10.1096/FASEBJ.5.3.2001789
Otsuki N, Dang NH, Kumagai E et al (2010) Aqueous extract of Carica papaya leaves exhibits anti-tumor activity and immunomodulatory effects. J Ethnopharmacol 127:760–767. https://doi.org/10.1016/J.JEP.2009.11.024
Pak JH, Liu CY, Huangpu J, Graham JS (1997) Construction and characterization of the soybean leaf metalloproteinase cDNA 1. FEBS Lett 404:283–288. https://doi.org/10.1016/S0014-5793(97)00141-5
Panavas T, Pikula A, Reid PD et al (1999) Identification of senescence-associated genes from daylily petals. Plant Mol Biol 40:237–248. https://doi.org/10.1023/A:1006146230602
Pardo M, López LMI, Canals F et al (2000) Purification of balansain I, an endopeptidase from unripe fruits of Bromelia balansae Mez (Bromeliaceae). J Agric Food Chem 48:3795–3800. https://doi.org/10.1021/JF0002488
Pautot V, Holzer FM, Reisch B, Walling LL (1993) Leucine aminopeptidase: an inducible component of the defense response in Lycopersicon esculentum (tomato). Proc Natl Acad Sci U S A 90:9906–9910. https://doi.org/10.1073/PNAS.90.21.9906
Pautot V, Holzer FM, Chaufaux J, Walling LL (2001) The induction of tomato leucine aminopeptidase genes (LapA) after Pseudomonas syringae pv. tomato infection is primarily a wound response triggered by coronatine. Mol Plant-Microbe Interact 14:214–224. https://doi.org/10.1094/MPMI.2001.14.2.214
Planta RJ, Calixto F, Pais MS (2000) Production by yeast of aspartic proteinases from plant origin with sheep’s, cow’s, goat’s milk, etc. clotting and proteolytic activity. Patent EP1196542 (WO0075283), Lisboa, Portugal
Polanowski A, Wilusz T, Kolaczkowska M, Wieczorek M, Wilimowska-Pelc A (1985) Purification and characterization of aspartic proteinases from Cucumis sativus and Cucurbita maxima seeds. In: Kostka V (ed) Aspartic proteinases and their inhibitors. Walter de Gruyter, New York, pp 49–52
Popovič T, Puizdar V, Brzin J (2002) A novel subtilase from common bean leaves. FEBS Lett 530:163–168. https://doi.org/10.1016/S0014-5793(02)03453-1
Priolo N, del Valle SM, Arribére MC et al (2000) Isolation and characterization of a cysteine protease from the latex of Araujia hortorum fruits. J Protein Chem 19:39–49. https://doi.org/10.1023/A:1007042825783
Puente XS, Sánchez LM, Overall CM, López-Otín C (2003) Human and mouse proteases: a comparative genomic approach. Nat Rev Genet 4:544–558. https://doi.org/10.1038/nrg1111
Radlowski M, Kalinowski A, Adamczyk J et al (1996) Proteolytic activity in the maize pollen wall. Physiol Plant 98:172–178. https://doi.org/10.1111/j.1399-3054.1996.tb00689.x
Ragster LV, Chrispeels MJ (1979) Azocoll-digesting proteinases in soybean leaves: characteristics and changes during leaf maturation and senescence. Plant Physiol 64:857–862. https://doi.org/10.1104/PP.64.5.857
Ramalho-Santos M, Veríssimo P, Faro C, Pires E (1996) Action on bovine αs1-casein of cardosins A and B, aspartic proteinases from the flowers of the cardoon Cynara cardunculus L. Biochim Biophys Acta 1297:83–89. https://doi.org/10.1016/0167-4838(96)00103-3
Ramalho-Santos M, Pissarra J, Veríssimo P et al (1997) Cardosin A, an abundant aspartic proteinase, accumulates in protein storage vacuoles in the stigmatic papillae of Cynara cardunculus L. Planta 203:204–212. https://doi.org/10.1007/s004250050183
Rao MB, Tanksale AM, Ghatge MS, Deshpande VV (1998) Molecular and biotechnological aspects of microbial proteases. Microbiol Mol Biol Rev 62:597–635
Ratnaparkhe SM, Egertsdotter EMU, Flinn BS (2009) Identification and characterization of a matrix metalloproteinase (Pta1-MMP) expressed during Loblolly pine (Pinus taeda) seed development, germination completion, and early seedling establishment. Planta 230:339–354. https://doi.org/10.1007/s00425-009-0949-8
Rawlings ND, Barrett AJ (1994) Families of serine peptidases. Methods Enzymol 244:19–61. https://doi.org/10.1016/0076-6879(94)44004-2
Rawlings ND, Salvesen G (2013) Handbook of proteolytic enzymes, 3rd edn. Academic, Cambridge
Rawlings ND, Barrett AJ, Bateman A (2010) MEROPS: the peptidase database. Nucleic Acids Res 38:D227–D233. https://doi.org/10.1093/nar/gkp971
Rawlings ND, Waller M, Barrett AJ, Bateman A (2014) MEROPS: the database of proteolytic enzymes, their substrates and inhibitors. Nucleic Acids Res 42:D503–D509. https://doi.org/10.1093/nar/gkt953
Reis PJM, Malcata FX (2011) Current state of Portuguese dairy products from ovine and caprine milks. Small Rumin Res 101:122–133. https://doi.org/10.1016/j.smallrumres.2011.09.032
Ribeiro A, Akkermans AD, van Kammen A et al (1995) A nodule-specific gene encoding a subtilisin-like protease is expressed in early stages of actinorhizal nodule development. Plant Cell 7:785–794. https://doi.org/10.1105/TPC.7.6.785
Rodrigo I, Vera P, Conejero V (1989) Degradation of tomato pathogenesis-related proteins by an endogenous 37-kDa aspartyl endoproteinase. Eur J Biochem 184:663–669. https://doi.org/10.1111/j.1432-1033.1989.tb15064.x
Rodrigo I, Vera P, Van Loon LC, Conejero V (1991) Degradation of tobacco pathogenesis-related proteins: evidence for conserved mechanisms of degradation of pathogenesis-related proteins in plants. Plant Physiol 95:616–622. https://doi.org/10.1104/PP.95.2.616
Roseiro LB, Andrew Wilbey R, Barbosa M (2003a) Serpa Cheese: technological, biochemical and microbiological characterisation of a PDO ewe’s milk cheese coagulated with Cynara cardunculus L. Lait 83:469–481. https://doi.org/10.1051/lait:2003026
Roseiro LB, Barbosa M, Ames JM, Wilbey RA (2003b) Cheesemaking with vegetable coagulants-the use of Cynara L. for the production of ovine milk cheeses. Int J Dairy Technol 56:76–85. https://doi.org/10.1046/j.1471-0307.2003.00080.x
Rowan AD, Buttle DJ, Barrett AJ (1990) The cysteine proteinases of the pineapple plant. Biochem J 266:869–875
Rudenskaya GN, Bogdanova EA, Revina LP et al (1995) Macluralisin - a serine proteinase from fruits of Maclura pomifera (Raf.) Schneid. Planta 196:174–179. https://doi.org/10.1007/BF00193231
Rudenskaya GN, Bogacheva AM, Preusser A et al (1998) Taraxalisin - a serine proteinase from dandelion Taraxacum officinale Webb s.l. FEBS Lett 437:237–240. https://doi.org/10.1016/S0014-5793(98)01243-5
Runeberg-Roos P, Törmakängas K, Östman A (1991) Primary structure of a barley-grain aspartic proteinase. A plant aspartic proteinase resembling mammalian cathepsin D. Eur J Biochem 202:1021–1027. https://doi.org/10.1111/j.1432-1033.1991.tb16465.x
Runeberg-Roos P, Kervinen J, Kovaleva V et al (1994) The aspartic proteinase of barley is a vacuolar enzyme that processes probarley lectin in vitro. Plant Physiol 105:321–329. https://doi.org/10.1104/PP.105.1.321
Sabalza M, Christou P, Capell T (2014) Recombinant plant-derived pharmaceutical proteins: current technical and economic bottlenecks. Biotechnol Lett 36:2367–2379. https://doi.org/10.1007/s10529-014-1621-3
Sakamoto W, Tamura T, Hanba-Tomita Y et al (2002) The VAR1 locus of Arabidopsis encodes a chloroplastic FtsH and is responsible for leaf variegation in the mutant alleles. Genes Cells 7:769–780. https://doi.org/10.1046/j.1365-2443.2002.00558.x
Salas CE, Gomes MTR, Hernandez M, Lopes MTP (2008) Plant cysteine proteinases: evaluation of the pharmacological activity. Phytochemistry 69:2263–2269. https://doi.org/10.1016/J.PHYTOCHEM.2008.05.016
Sampaio PN, Fortes AM, Cabral JMS et al (2008) Production and characterization of recombinant cyprosin B in Saccharomyces cerevisiae (W303-1A) strain. J Biosci Bioeng 105:305–312. https://doi.org/10.1263/JBB.105.305
Sanchez-Moran E, Jones GH, Franklin FCH, Santos JL (2004) A puromycin-sensitive aminopeptidase is essential for meiosis in Arabidopsis thaliana. Plant Cell Online 16:2895–2909. https://doi.org/10.1105/tpc.104.024992
Sarkkinen P, Kalkkinen N, Tilgmann C et al (1992) Aspartic proteinase from barley grains is related to mammalian lysosomal cathepsin D. Planta 186:317–323. https://doi.org/10.1007/BF00195311
Schall VT, Vasconcellos MC, Rocha RS et al (2001) The control of the schistosome-transmitting snail Biomphalaria glabrata by the plant Molluscicide Euphorbia splendens var. hislopii (syn milli Des. Moul): a longitudinal field study in an endemic area in Brazil. Acta Trop 79:165–170. https://doi.org/10.1016/S0001-706X(01)00126-7
Schaller A (2004) A cut above the rest: the regulatory function of plant proteases. Planta 220:183–197. https://doi.org/10.1007/s00425-004-1407-2
Schaller A, Bergey DR, Ryan CA (1995) Induction of wound response genes in tomato leaves by bestatin, an inhibitor of aminopeptidases. Plant Cell 7:1893–1898. https://doi.org/10.1105/tpc.7.11.1893
Schiermeyer A, Hartenstein H, Mandal MK et al (2009) A membrane-bound matrix metalloproteinase from Nicotiana tabacum cv. BY-2 is induced by bacterial pathogens. BMC Plant Biol 9:83. https://doi.org/10.1186/1471-2229-9-83
Seker S, Beyenal H, Tanyolac A (1999) Modeling milk clotting activity in the continuous production of microbial rennet from Mucor miehei. J Food Sci 64:525–529. https://doi.org/10.1111/j.1365-2621.1999.tb15076.x
Silva SV, Malcata FX (1999) On the activity and specificity of cardosin B, a plant proteinase, on ovine caseins. Food Chem 67:373–378. https://doi.org/10.1016/S0308-8146(99)00126-0
Silva SV, Malcata FX (2000) Action of cardosin A from Cynara humilis on ovine and caprine caseinates. J Dairy Res 67:449–454
Silva SV, Malcata FX (2005) Partial identification of water-soluble peptides released at early stages of proteolysis in sterilized ovine cheese-like systems: influence of type of coagulant and starter. J Dairy Sci 88:1947–1954. https://doi.org/10.3168/jds.S0022-0302(05)72870-8
Silva SV, Xavier Malcata F (1998) Proteolysis of ovine caseins by cardosin A, an aspartic acid proteinase from Cynara cardunculus L. Lait 78:513–519. https://doi.org/10.1051/lait:1998548
Silva SV, Allmere T, Xavier Malcata F, Andrén A (2003) Comparative studies on the gelling properties of cardosins extracted from Cynara cardunculus and chymosin on cow’s skim milk. Int Dairy J 13:559–564. https://doi.org/10.1016/S0958-6946(03)00075-X
Simões I, Faro C (2004) Structure and function of plant aspartic proteinases. Eur J Biochem 271:2067–2075. https://doi.org/10.1111/j.1432-1033.2004.04136.x
Singh VK, Patel AK, Moir AJ, Jagannadham MV (2008) Indicain, a dimeric serine protease from Morus indica cv. K2. Phytochemistry 69:2110–2119. https://doi.org/10.1016/J.PHYTOCHEM.2008.05.005
Sjögren LLE, Stanne TM, Zheng B et al (2006) Structural and functional insights into the chloroplast ATP-dependent Clp protease in arabidopsis. Plant Cell Online 18:2635–2649. https://doi.org/10.1105/tpc.106.044594
Sousa M, Malcata F (1997) Comparison of plant and animal rennets in terms of microbiological, chemical, and proteolysis characteristics of ovine cheese. J Agric Food Chem 45:74–81. https://doi.org/10.1021/JF9506601
Sousa MJ, Malcata FX (1998) Proteolysis of ovine and caprine caseins in solution by enzymatic extracts from flowers of cynara cardunculus. Enzym Microb Technol 22:305–314. https://doi.org/10.1016/S0141-0229(97)00173-7
Sousa M, Malcata F (2002) Advances in the role of a plant coagulant (Cynara cardunculus) in vitro and during ripening of cheeses from several milk species. Lait 82:151–170. https://doi.org/10.1051/lait:2002001
Souza CAM, de-Carvalho RR, Kuriyama SN et al (1997) Study of the embryofeto-toxicity of Crown-of-Thorns (Euphorbia milii) latex, a natural molluscicide. Braz J Med Biol Res 30:1325–1332. https://doi.org/10.1590/S0100-879X1997001100011
St. Angelo AJ, Ory RL, Hansen HJ (1969) Localization of an acid proteinase in hempseed. Phytochemistry 8:1135–1138. https://doi.org/10.1016/S0031-9422(00)85547-8
St. Angelo AJ, Ory RL, Hansen HJ (1970) Properties of a purified proteinase from hempseed. Phytochemistry 9:1933–1938. https://doi.org/10.1016/S0031-9422(00)85342-X
Stenger S, Hanson DA, Teitelbaum R et al (1998) An antimicrobial activity of cytolytic T cells mediated by granulysin. Science 282:121–125. https://doi.org/10.1126/SCIENCE.282.5386.121
Sutoh K, Kato H, Minamikawa T (1999) Identification and possible roles of three types of endopeptidase from germinated wheat Seeds. J Biochem 126:700–707. https://doi.org/10.1093/oxfordjournals.jbchem.a022506
Takahashi K, Matsumoto K, Nishii W, Muramatsu M, Kubota K, Shibata C, Athauda SBP (2009) Comparative studies on the acid proteinase activities in the digestive fluids of Nepenthes, Cephalotus, Dionaea, and Drosera. Carniv Plant Newsl 38:75–82
Takeda N, Kistner C, Kosuta S et al (2007) Proteases in plant root symbiosis. Phytochemistry 68:111–121. https://doi.org/10.1016/J.PHYTOCHEM.2006.09.022
Tan-Wilson AL, Liu X, Chen R et al (1996) An acidic amino acid-specific protease from germinating soybeans. Phytochemistry 42:313–319. https://doi.org/10.1016/0031-9422(95)00896-9
Targoni OS, Tary-Lehmann M, Lehmann PV (1999) Prevention of murine EAE by oral hydrolytic enzyme treatment. J Autoimmun 12:191–198. https://doi.org/10.1006/JAUT.1999.0271
Taylor AA, Horsch A, Rzepczyk A et al (1997) Maturation and secretion of a serine proteinase is associated with events of late microsporogenesis. Plant J 12:1261–1271. https://doi.org/10.1046/j.1365-313x.1997.12061261.x
Tökés ZA, Woon WC, Chambers SM (1974) Digestive enzymes secreted by the carnivorous plant Nepenthes macferlanei L. Planta 119:39–46. https://doi.org/10.1007/BF00390820
Törmäkangas K, Hadlington JL, Pimpl P et al (2001) A vacuolar sorting domain may also influence the way in which proteins leave the endoplasmic reticulum. Plant Cell 13:2021–2032
Tornero P, Conejero V, Vera P (1997) Identification of a new pathogen-induced member of the subtilisin-like processing protease family from plants. J Biol Chem 272:14412–14419. https://doi.org/10.1074/JBC.272.22.14412
Uchikoba T, Horita H, Kaneda M (1990) Proteases from the sarcocarp of yellow snake-gourd. Phytochemistry 29:1879–1881. https://doi.org/10.1016/0031-9422(90)85032-B
Uchikoba T, Hosoyamada S, Onjyo M et al (2001) A serine endopeptidase from the fruits of Melothria japonica (Thunb.) Maxim. Phytochemistry 57:1–5. https://doi.org/10.1016/S0031-9422(00)00511-2
Uhlig H, Linsmaier-Bednar EM (1998) Industrial enzymes and their applications. Wiley, New York
Vaccaro AM, Salvioli R, Tatti M, Ciaffoni F (1999) Saposins and their interaction with lipids. Neurochem Res 24:307–314. https://doi.org/10.1023/A:1022530508763
Varshavsky A (1996) The N-end rule: functions, mysteries, uses. Proc Natl Acad Sci U S A 93:12142–12149. https://doi.org/10.1073/PNAS.93.22.12142
Verissimo P, Faro C, Moir AJG et al (1996) Purification, characterization and partial amino acid sequencing of two new aspartic proteinases from fresh flowers of Cynara cardunculus L. Eur J Biochem 235:762–768. https://doi.org/10.1111/j.1432-1033.1996.00762.x
Vincent JL, Brewin NJ (2000) Immunolocalization of a cysteine protease in vacuoles, vesicles, and symbiosomes of pea nodule cells. Plant Physiol 123:521–530
Vioque M, Gómez R, Sánchez E et al (2000) Chemical and microbiological characteristics of ewes’ milk cheese manufactured with extracts from flowers of Cynara cardunculus and Cynara humilis as coagulants. J Agric Food Chem 48:451–456
White PC, Cordeiro MC, Arnold D et al (1999) Processing, activity, and inhibition of recombinant cyprosin, an aspartic proteinase from cardoon (Cynara cardunculus). J Biol Chem 274:16685–16693. https://doi.org/10.1074/JBC.274.24.16685
Whitehurst RJ, van Oort M (2009) Enzymes in food technology. Wiley-Blackwell, Oxford
Yadav SC, Pande M, Jagannadham MV (2006) Highly stable glycosylated serine protease from the medicinal plant Euphorbia milii. Phytochemistry 67:1414–1426. https://doi.org/10.1016/J.PHYTOCHEM.2006.06.002
Yamagata H, Masuzawa T, Nagaoka Y et al (1994) Cucumisin, a serine protease from melon fruits, shares structural homology with subtilisin and is generated from a large precursor. J Biol Chem 269:32725–32731
Ye Z-H, Varner JE (1996) Induction of cysteine and serine proteases during xylogenesis in Zinnia elegans. Plant Mol Biol 30:1233–1246. https://doi.org/10.1007/BF00019555
Zasloff M (2002) Antimicrobial peptides of multicellular organisms. Nature 415:389–395. https://doi.org/10.1038/415389a
Zhao C, Johnson BJ, Kositsup B, Beers EP (2000) Exploiting secondary growth in Arabidopsis. Construction of xylem and bark cDNA libraries and cloning of three xylem endopeptidases. Plant Physiol 123:1185–1196
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Sebastián, D., Guevara, M.G., Rocío, T.F., Virginia, T.C. (2018). An Overview of Plant Proteolytic Enzymes. In: Guevara, M., Daleo, G. (eds) Biotechnological Applications of Plant Proteolytic Enzymes. Springer, Cham. https://doi.org/10.1007/978-3-319-97132-2_1
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