Characteristics of the Proteolytic Enzymes Produced by Lactic Acid Bacteria

Over the past several decades, we have observed a very rapid development in the biotechnological use of lactic acid bacteria (LAB) in various branches of the food industry. All such areas of activity of these bacteria are very important and promise enormous economic and industrial successes. LAB are...

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Published inMolecules (Basel, Switzerland) Vol. 26; no. 7; p. 1858
Main Authors Kieliszek, Marek, Pobiega, Katarzyna, Piwowarek, Kamil, Kot, Anna M
Format Journal Article
LanguageEnglish
Published Switzerland MDPI AG 25.03.2021
MDPI
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Abstract Over the past several decades, we have observed a very rapid development in the biotechnological use of lactic acid bacteria (LAB) in various branches of the food industry. All such areas of activity of these bacteria are very important and promise enormous economic and industrial successes. LAB are a numerous group of microorganisms that have the ability to ferment sugars into lactic acid and to produce proteolytic enzymes. LAB proteolytic enzymes play an important role in supplying cells with the nitrogen compounds necessary for their growth. Their nutritional requirements in this regard are very high. Lactic acid bacteria require many free amino acids to grow. The available amount of such compounds in the natural environment is usually small, hence the main function of these enzymes is the hydrolysis of proteins to components absorbed by bacterial cells. Enzymes are synthesized inside bacterial cells and are mostly secreted outside the cell. This type of proteinase remains linked to the cell wall structure by covalent bonds. Thanks to advances in enzymology, it is possible to obtain and design new enzymes and their preparations that can be widely used in various biotechnological processes. This article characterizes the proteolytic activity, describes LAB nitrogen metabolism and details the characteristics of the peptide transport system. Potential applications of proteolytic enzymes in many industries are also presented, including the food industry.
AbstractList Over the past several decades, we have observed a very rapid development in the biotechnological use of lactic acid bacteria (LAB) in various branches of the food industry. All such areas of activity of these bacteria are very important and promise enormous economic and industrial successes. LAB are a numerous group of microorganisms that have the ability to ferment sugars into lactic acid and to produce proteolytic enzymes. LAB proteolytic enzymes play an important role in supplying cells with the nitrogen compounds necessary for their growth. Their nutritional requirements in this regard are very high. Lactic acid bacteria require many free amino acids to grow. The available amount of such compounds in the natural environment is usually small, hence the main function of these enzymes is the hydrolysis of proteins to components absorbed by bacterial cells. Enzymes are synthesized inside bacterial cells and are mostly secreted outside the cell. This type of proteinase remains linked to the cell wall structure by covalent bonds. Thanks to advances in enzymology, it is possible to obtain and design new enzymes and their preparations that can be widely used in various biotechnological processes. This article characterizes the proteolytic activity, describes LAB nitrogen metabolism and details the characteristics of the peptide transport system. Potential applications of proteolytic enzymes in many industries are also presented, including the food industry.
Author Kot, Anna M
Pobiega, Katarzyna
Piwowarek, Kamil
Kieliszek, Marek
AuthorAffiliation Department of Food Biotechnology and Microbiology, Institute of Food Sciences, Warsaw University of Life Sciences—SGGW, Nowoursynowska 159 C, 02-776 Warsaw, Poland; katarzyna_pobiega@sggw.edu.pl (K.P.); kamil_piwowarek@sggw.edu.pl (K.P.); anna_kot@sggw.edu.pl (A.M.K.)
AuthorAffiliation_xml – name: Department of Food Biotechnology and Microbiology, Institute of Food Sciences, Warsaw University of Life Sciences—SGGW, Nowoursynowska 159 C, 02-776 Warsaw, Poland; katarzyna_pobiega@sggw.edu.pl (K.P.); kamil_piwowarek@sggw.edu.pl (K.P.); anna_kot@sggw.edu.pl (A.M.K.)
Author_xml – sequence: 1
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  orcidid: 0000-0002-5836-4865
  surname: Kieliszek
  fullname: Kieliszek, Marek
  organization: Department of Food Biotechnology and Microbiology, Institute of Food Sciences, Warsaw University of Life Sciences-SGGW, Nowoursynowska 159 C, 02-776 Warsaw, Poland
– sequence: 2
  givenname: Katarzyna
  orcidid: 0000-0003-3532-8666
  surname: Pobiega
  fullname: Pobiega, Katarzyna
  organization: Department of Food Biotechnology and Microbiology, Institute of Food Sciences, Warsaw University of Life Sciences-SGGW, Nowoursynowska 159 C, 02-776 Warsaw, Poland
– sequence: 3
  givenname: Kamil
  surname: Piwowarek
  fullname: Piwowarek, Kamil
  organization: Department of Food Biotechnology and Microbiology, Institute of Food Sciences, Warsaw University of Life Sciences-SGGW, Nowoursynowska 159 C, 02-776 Warsaw, Poland
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  surname: Kot
  fullname: Kot, Anna M
  organization: Department of Food Biotechnology and Microbiology, Institute of Food Sciences, Warsaw University of Life Sciences-SGGW, Nowoursynowska 159 C, 02-776 Warsaw, Poland
BackLink https://www.ncbi.nlm.nih.gov/pubmed/33806095$$D View this record in MEDLINE/PubMed
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Cites_doi 10.3390/microorganisms5020027
10.1111/j.1365-2958.1994.tb01271.x
10.1128/jb.171.5.2789-2794.1989
10.1016/B978-0-12-813280-7.00005-0
10.3390/ijms20071777
10.1111/jfpp.14192
10.1016/j.idairyj.2011.05.002
10.1039/C8FO01749B
10.1093/femsle/fnaa102
10.1016/j.foodres.2019.01.024
10.1016/j.lwt.2017.03.042
10.1016/j.foodres.2018.12.008
10.1080/10498850.2019.1639872
10.1093/femsle/fnx167
10.1016/j.jcs.2019.03.001
10.1007/s10068-018-0423-0
10.1007/s12010-017-2427-2
10.1007/s00253-019-09844-6
10.1073/pnas.220308797
10.1007/s00253-017-8264-y
10.1016/S0958-6946(03)00073-6
10.1016/j.idairyj.2009.09.007
10.1099/00221287-138-7-1353
10.1099/13500872-145-2-437
10.1089/ind.2018.0032
10.1128/AEM.71.10.6260-6266.2005
10.3389/fbioe.2019.00110
10.1016/j.chom.2012.02.006
10.1023/A:1002036906922
10.1021/bi981712t
10.1002/fsn3.27
10.1016/j.ifset.2019.102192
10.1128/AEM.71.11.7152-7163.2005
10.1128/JB.186.6.1648-1657.2004
10.1128/AEM.66.12.5316-5321.2000
10.1021/jf202176d
10.1016/j.foodres.2017.10.044
10.1038/s41598-017-09124-1
10.1016/j.foodres.2016.08.042
10.1300/J030v01n01_05
10.1111/j.1574-6976.1993.tb00018.x
10.1128/jb.177.12.3472-3478.1995
10.1007/s00253-018-09586-x
10.1128/JB.183.12.3614-3622.2001
10.1007/s13594-016-0292-3
10.1016/j.foodchem.2019.126035
10.1016/j.procbio.2019.10.029
10.17113/ftb.58.03.20.6598
10.1074/jbc.270.4.1569
10.1016/j.ijfoodmicro.2016.08.007
10.1016/j.lwt.2019.108779
10.1080/10408398.2016.1147418
10.1016/j.ijbiomac.2019.01.081
10.1128/jb.177.16.4652-4657.1995
10.1016/j.idairyj.2014.01.008
10.1007/s12649-020-01145-8
10.1007/s11033-019-05022-z
10.1021/acs.jafc.6b03379
10.1111/nbu.12334
10.1111/j.1472-765X.2009.02748.x
10.3389/fmicb.2017.02285
10.1016/j.mec.2020.e00133
10.1007/s00253-014-6258-6
10.1128/jb.173.14.4517-4525.1991
10.2174/1389201020666190416151129
10.3168/jds.S0022-0302(93)77540-2
10.1128/aem.61.11.3934-3939.1995
10.1111/j.1365-2958.2004.04136.x
10.3389/fmicb.2018.01978
10.1046/j.1365-2958.2001.02470.x
10.1016/j.lwt.2020.110365
10.1186/s40104-017-0153-9
10.1128/AEM.66.11.4772-4778.2000
10.3389/fmicb.2013.00030
10.1016/j.fbio.2017.11.003
10.1074/jbc.M502349200
10.1128/AEM.02395-08
10.1007/s00253-006-0427-1
10.1016/j.idairyj.2019.04.004
10.1124/pr.115.010991
10.1016/j.ijbiomac.2019.04.169
10.1111/1541-4337.12455
10.1016/j.polar.2019.04.003
10.1007/BF02931617
10.1016/j.ijfoodmicro.2006.10.026
10.1016/B978-0-12-813280-7.00008-6
10.1016/j.genrep.2020.100771
10.1007/BF00395933
10.1186/s12866-017-1125-0
10.1016/j.lwt.2020.109064
10.1016/j.cbpa.2019.12.006
10.1016/j.tifs.2018.07.003
10.1111/ijfs.14915
10.1016/j.ifset.2020.102399
10.1128/jb.171.5.2795-2802.1989
10.1093/ajcn/73.2.365s
10.1111/1541-4337.12676
10.3390/v12111316
10.1128/aem.58.1.78-84.1992
10.1007/s00253-018-9537-9
10.3390/fermentation5040096
10.3389/fimmu.2019.03019
10.3390/foods9101399
10.1016/j.femsle.2004.08.023
10.1155/2018/7957269
10.1111/jam.13779
10.1128/AEM.69.10.5802-5811.2003
10.1128/aem.63.6.2213-2217.1997
10.1080/10826068.2012.656869
10.1007/s00217-018-3100-x
10.1074/jbc.REV119.010155
10.2174/1389201017666161229154324
10.1186/s40104-019-0323-z
10.2174/0929866524666161123111333
10.1016/j.procbio.2019.11.030
10.1016/0958-6946(95)00029-1
10.1016/j.idairyj.2018.06.010
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Issue 7
Keywords lactic acid bacteria
proteolytic enzymes
proteolysis
Language English
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References ref_93
Sun (ref_8) 2020; 89
Krasnowska (ref_108) 2004; 1
Renault (ref_95) 2001; 183
Sarabhai (ref_116) 2020; 137
ref_98
Scarnato (ref_113) 2017; 81
Kok (ref_64) 1993; 76
Worsztynowicz (ref_99) 2019; 66
ref_17
Requena (ref_41) 2019; 96
Genay (ref_57) 2009; 75
Pokora (ref_126) 2013; 1
(ref_105) 2017; 183
Foucaud (ref_80) 1995; 177
Topisirovic (ref_52) 2010; 50
Vermeulen (ref_74) 2005; 71
Guo (ref_49) 2016; 64
Chang (ref_53) 2014; 38
Silva (ref_120) 2017; 55
Jensen (ref_83) 2010; 20
Zeng (ref_77) 2017; 364
Lim (ref_28) 2019; 10
Haandrikman (ref_63) 1989; 171
Kycia (ref_16) 2019; 20
ref_24
Vos (ref_67) 1989; 171
Serror (ref_89) 2001; 40
Connolly (ref_121) 2019; 121
Kok (ref_73) 1995; 5
ref_20
Aguilar (ref_72) 2019; 18
Saa (ref_112) 2019; 119
ref_27
Sanders (ref_125) 2018; 43
Miclo (ref_54) 2012; 60
Puligundla (ref_117) 2020; 64
Fira (ref_71) 2006; 51
Martorana (ref_111) 2018; 244
Siezen (ref_61) 1999; 76
Gitton (ref_82) 2005; 71
Morel (ref_96) 2001; 3
Wu (ref_19) 2020; 122
Gniewosz (ref_15) 2017; 18
Weiher (ref_44) 2012; 11
Holck (ref_65) 1992; 138
Ramachandran (ref_31) 2016; 68
Nordin (ref_2) 2019; 20
Morel (ref_97) 1999; 145
Kok (ref_119) 2019; 103
Ji (ref_23) 2021; 20
Haard (ref_123) 1992; 1
Cirlini (ref_18) 2020; 118
Lozo (ref_58) 2011; 21
Pastar (ref_70) 2003; 69
Lorenzo (ref_109) 2018; 79
Kavitake (ref_14) 2018; 21
Detmers (ref_78) 2000; 97
(ref_13) 2018; 2018
Mamo (ref_33) 2018; 2018
(ref_50) 2020; 367
Marson (ref_122) 2020; 91
Detmers (ref_79) 1998; 37
Sato (ref_102) 2018; 103
Nakajima (ref_81) 1997; 63
Liu (ref_86) 2017; 7
Vido (ref_94) 2004; 186
Sun (ref_10) 2019; 133
Hebert (ref_43) 2000; 66
Wang (ref_9) 2019; 103
Matti (ref_11) 2019; 28
Wu (ref_69) 2017; 57
Arshad (ref_107) 2016; 2
Brown (ref_87) 2017; 7
Othman (ref_12) 2017; 8
Mahajan (ref_38) 2010; 3
Garault (ref_60) 2000; 66
Kenny (ref_5) 2003; 13
Li (ref_55) 2019; 103
Brown (ref_66) 2017; 24
Villegas (ref_56) 2015; 99
Sims (ref_34) 2004; 239
Biscola (ref_103) 2018; 125
Razzaq (ref_6) 2019; 7
Haandrikman (ref_62) 1991; 173
Sharma (ref_7) 2019; 15
Sandoval (ref_1) 2020; 55
Hermans (ref_39) 2020; 11
Sarabhai (ref_114) 2019; 87
Daliri (ref_37) 2018; 27
Griffiths (ref_84) 2013; 4
Petranovic (ref_90) 2004; 53
Reid (ref_46) 1995; 61
Bruinenberg (ref_68) 1992; 58
Wiebenga (ref_101) 2016; 237
Moghaddam (ref_115) 2020; 21
Kunji (ref_45) 1996; 70
Solieri (ref_51) 2018; 85
Kunji (ref_88) 1995; 270
Holzapfel (ref_21) 2001; 73
Do (ref_3) 2020; 295
Zhao (ref_30) 2016; 89
Pritchard (ref_48) 1993; 12
ref_106
Galia (ref_92) 2016; 96
Navarre (ref_59) 1994; 14
Saidi (ref_26) 2020; 58
Gurumallesh (ref_32) 2019; 128
Orive (ref_118) 2020; 11
ref_42
Cichosz (ref_25) 2006; 46
Ewert (ref_35) 2018; 9
ref_40
Ahmad (ref_104) 2019; 43
Munir (ref_100) 2019; 57
Worsztynowicz (ref_22) 2020; 312
(ref_75) 2020; 10
Guan (ref_85) 2017; 101
Kieliszek (ref_29) 2012; 42
Geurts (ref_91) 2005; 280
Bansal (ref_36) 2019; 46
Juillard (ref_47) 1995; 177
Ma (ref_76) 2018; 9
Zotta (ref_110) 2007; 115
Savijoki (ref_4) 2006; 71
Hou (ref_124) 2017; 8
References_xml – ident: ref_40
  doi: 10.3390/microorganisms5020027
– volume: 14
  start-page: 115
  year: 1994
  ident: ref_59
  article-title: Proteolytic cleavage and cell wall anchoring at the LPXTG motif of surface proteins in Gram-positive bacteria
  publication-title: Mol. Microbiol.
  doi: 10.1111/j.1365-2958.1994.tb01271.x
  contributor:
    fullname: Navarre
– volume: 171
  start-page: 2789
  year: 1989
  ident: ref_63
  article-title: Identification of a gene required for maturation of an extracellular lactococcal serine proteinase
  publication-title: J. Bacteriol.
  doi: 10.1128/jb.171.5.2789-2794.1989
  contributor:
    fullname: Haandrikman
– ident: ref_98
  doi: 10.1016/B978-0-12-813280-7.00005-0
– ident: ref_27
  doi: 10.3390/ijms20071777
– volume: 43
  start-page: e14192
  year: 2019
  ident: ref_104
  article-title: Optimization of a protease extraction using a statistical approach for the production of an alternative meat tenderizer from Spondias cytherea roots
  publication-title: J. Food Process. Preserv.
  doi: 10.1111/jfpp.14192
  contributor:
    fullname: Ahmad
– volume: 21
  start-page: 863
  year: 2011
  ident: ref_58
  article-title: Comparative analysis of β-casein proteolysis by PrtP proteinase from Lactobacillus paracasei subsp. paracasei BGHN14, PrtR proteinase from Lactobacillus rhamnosus BGT10 and PrtH proteinase from Lactobacillus helveticus BGRA43
  publication-title: Int. Dairy J.
  doi: 10.1016/j.idairyj.2011.05.002
  contributor:
    fullname: Lozo
– volume: 9
  start-page: 5989
  year: 2018
  ident: ref_35
  article-title: Improving the colloidal and sensory properties of a caseinate hydrolysate using particular exopeptidases
  publication-title: Food Funct.
  doi: 10.1039/C8FO01749B
  contributor:
    fullname: Ewert
– volume: 367
  start-page: fnaa102
  year: 2020
  ident: ref_50
  article-title: Differences in the expression of cell envelope proteinases (CEP) in two Lactobacillus paracasei probiotic strains
  publication-title: FEMS Microbiol. Lett.
  doi: 10.1093/femsle/fnaa102
– volume: 119
  start-page: 510
  year: 2019
  ident: ref_112
  article-title: Metabolomic approach to study the impact of flour type and fermentation process on volatile profile of bakery products
  publication-title: Food Res. Int.
  doi: 10.1016/j.foodres.2019.01.024
  contributor:
    fullname: Saa
– volume: 81
  start-page: 101
  year: 2017
  ident: ref_113
  article-title: New bread formulation with improved rheological properties and longer shelf-life by the combined use of transglutaminase and sourdough
  publication-title: LWT Food Sci. Technol.
  doi: 10.1016/j.lwt.2017.03.042
  contributor:
    fullname: Scarnato
– volume: 121
  start-page: 524
  year: 2019
  ident: ref_121
  article-title: Characterisation of the in vitro bioactive properties of alkaline and enzyme extracted brewers’ spent grain protein hydrolysates
  publication-title: Food Res. Int.
  doi: 10.1016/j.foodres.2018.12.008
  contributor:
    fullname: Connolly
– volume: 66
  start-page: 61
  year: 2019
  ident: ref_99
  article-title: Identification and partial characterization of proteolytic activity of Enterococcus faecalis relevant to their application in the dairy industry
  publication-title: Acta Biochim. Pol.
  contributor:
    fullname: Worsztynowicz
– volume: 28
  start-page: 781
  year: 2019
  ident: ref_11
  article-title: Isolation, Screening, and identification of proteolytic lactic acid bacteria from indigenous Chao product
  publication-title: J. Aquat. Food Prod. Technol.
  doi: 10.1080/10498850.2019.1639872
  contributor:
    fullname: Matti
– volume: 364
  start-page: 167
  year: 2017
  ident: ref_77
  article-title: Characterization of a lactose-responsive promoter of ATP-binding cassette (ABC) transporter gene from Lactobacillus acidophilus 05–172
  publication-title: FEMS Microbiol. Lett.
  doi: 10.1093/femsle/fnx167
  contributor:
    fullname: Zeng
– volume: 87
  start-page: 59
  year: 2019
  ident: ref_114
  article-title: Targeted degradation of gluten proteins in wheat flour by prolyl endoprotease and its utilization in low immunogenic pasta for gluten sensitivity population
  publication-title: J. Cereal Sci.
  doi: 10.1016/j.jcs.2019.03.001
  contributor:
    fullname: Sarabhai
– volume: 27
  start-page: 1781
  year: 2018
  ident: ref_37
  article-title: Antihypertensive peptides from whey proteins fermented by lactic acid bacteria
  publication-title: Food Sci. Biotechnol.
  doi: 10.1007/s10068-018-0423-0
  contributor:
    fullname: Daliri
– volume: 183
  start-page: 1
  year: 2017
  ident: ref_105
  article-title: Bacterial and fungal proteolytic enzymes: Production, catalysis and potential applications
  publication-title: Appl. Biochem. Biotechnol.
  doi: 10.1007/s12010-017-2427-2
– volume: 103
  start-page: 5243
  year: 2019
  ident: ref_9
  article-title: Lactic acid bacteria isolated from dairy products as potential producers of lipolytic, proteolytic and antibacterial proteins
  publication-title: Appl. Microbiol. Biotechnol.
  doi: 10.1007/s00253-019-09844-6
  contributor:
    fullname: Wang
– volume: 46
  start-page: 66
  year: 2006
  ident: ref_25
  article-title: Aktywność peptydazowa wybranych szczepów Lactobacillus
  publication-title: Żywność Nauk. Technol. Jakość
  contributor:
    fullname: Cichosz
– volume: 97
  start-page: 12487
  year: 2000
  ident: ref_78
  article-title: Combinatorial peptide libraries reveal the ligand-binding mechanism of the oligopeptide receptor OppA of Lactococcus lactis
  publication-title: Proc. Natl. Acad. Sci. USA
  doi: 10.1073/pnas.220308797
  contributor:
    fullname: Detmers
– volume: 101
  start-page: 3991
  year: 2017
  ident: ref_85
  article-title: Microbial response to environmental stresses: From fundamental mechanisms to practical applications
  publication-title: Appl. Microbiol. Biotechnol.
  doi: 10.1007/s00253-017-8264-y
  contributor:
    fullname: Guan
– volume: 13
  start-page: 509
  year: 2003
  ident: ref_5
  article-title: Growth phase and growth medium effects on the peptidase activities of Lactobacillus helveticus
  publication-title: Int. Dairy J.
  doi: 10.1016/S0958-6946(03)00073-6
  contributor:
    fullname: Kenny
– volume: 20
  start-page: 149
  year: 2010
  ident: ref_83
  article-title: Variation in aminopeptidase and aminotransferase activities of six cheese related Lactobacillus helveticus strains
  publication-title: Int. Dairy J.
  doi: 10.1016/j.idairyj.2009.09.007
  contributor:
    fullname: Jensen
– volume: 138
  start-page: 1353
  year: 1992
  ident: ref_65
  article-title: Cloning, sequencing and expression of the gene encoding the cell-envelope-associated proteinase from Lactobacillus paracasei subsp. paracasei NCDO 151
  publication-title: J. Gen. Microbiol.
  doi: 10.1099/00221287-138-7-1353
  contributor:
    fullname: Holck
– volume: 145
  start-page: 437
  year: 1999
  ident: ref_97
  article-title: Characterization of a prolidase from Lactobacillus delbrueckii subsp. bulgaricus CNRZ 397 with an unusual regulation of biosynthesis
  publication-title: Microbiology
  doi: 10.1099/13500872-145-2-437
  contributor:
    fullname: Morel
– volume: 15
  start-page: 69
  year: 2019
  ident: ref_7
  article-title: A review on microbial alkaline protease: An essential tool for various industrial approaches
  publication-title: Ind. Biotechnol.
  doi: 10.1089/ind.2018.0032
  contributor:
    fullname: Sharma
– volume: 71
  start-page: 6260
  year: 2005
  ident: ref_74
  article-title: Functional characterization of the proteolytic system of Lactobacillus sanfranciscensis DSM 20451T during growth in sourdough
  publication-title: Appl. Environ. Microbiol.
  doi: 10.1128/AEM.71.10.6260-6266.2005
  contributor:
    fullname: Vermeulen
– volume: 7
  start-page: 110
  year: 2019
  ident: ref_6
  article-title: Microbial proteases applications
  publication-title: Front. Bioeng. Biotechnol.
  doi: 10.3389/fbioe.2019.00110
  contributor:
    fullname: Razzaq
– volume: 11
  start-page: 387
  year: 2012
  ident: ref_44
  article-title: Lactocepin secreted by Lactobacillus exerts anti-inflammatory effects by selectively degrading proinflammatory chemokines
  publication-title: Cell Host Microbe
  doi: 10.1016/j.chom.2012.02.006
  contributor:
    fullname: Weiher
– volume: 76
  start-page: 139
  year: 1999
  ident: ref_61
  article-title: Multi-domain, cell-envelope proteinases of lactic acid bacteria
  publication-title: Antonie van Leeuwenhoek
  doi: 10.1023/A:1002036906922
  contributor:
    fullname: Siezen
– volume: 37
  start-page: 16671
  year: 1998
  ident: ref_79
  article-title: Kinetics and specificity of peptide uptake by the oligopeptide transport system of Lactococcus lactis
  publication-title: Biochemistry
  doi: 10.1021/bi981712t
  contributor:
    fullname: Detmers
– volume: 1
  start-page: 184
  year: 2013
  ident: ref_126
  article-title: Biological and functional properties of proteolytic enzyme-modified egg protein by-products
  publication-title: Food Sci. Nutr.
  doi: 10.1002/fsn3.27
  contributor:
    fullname: Pokora
– volume: 57
  start-page: 102192
  year: 2019
  ident: ref_100
  article-title: Effects of high pressure, microwave and ultrasound processing on proteins and enzyme activity in dairy systems—A review
  publication-title: Innov. Food Sci. Emerg. Technol.
  doi: 10.1016/j.ifset.2019.102192
  contributor:
    fullname: Munir
– volume: 71
  start-page: 7152
  year: 2005
  ident: ref_82
  article-title: Proteomic signature of Lactococcus lactis NCDO763 cultivated in milk
  publication-title: Appl. Environ. Microbiol.
  doi: 10.1128/AEM.71.11.7152-7163.2005
  contributor:
    fullname: Gitton
– volume: 1
  start-page: 84
  year: 2004
  ident: ref_108
  article-title: Próba wykorzystania enzymów pochodzenia mikrobiologicznego do degradacji surowców zwierzęcych bogatych w tkankę łączną
  publication-title: ŻYWNOŚĆ. Nauk. Technol. Jakość
  contributor:
    fullname: Krasnowska
– volume: 186
  start-page: 1648
  year: 2004
  ident: ref_94
  article-title: Proteome analyses of heme-dependent respiration in Lactococcus lactis: Involvement of the proteolytic system
  publication-title: J. Bacteriol.
  doi: 10.1128/JB.186.6.1648-1657.2004
  contributor:
    fullname: Vido
– volume: 66
  start-page: 5316
  year: 2000
  ident: ref_43
  article-title: Nutritional requirements and nitrogen-dependent regulation of proteinase activity of Lactobacillus helveticus CRL 1062
  publication-title: Appl. Environ. Microbiol.
  doi: 10.1128/AEM.66.12.5316-5321.2000
  contributor:
    fullname: Hebert
– volume: 60
  start-page: 554
  year: 2012
  ident: ref_54
  article-title: Variability of hydrolysis of β-, α s1-, and α s2-caseins by 10 strains of Streptococcus thermophilus and resulting bioactive peptides
  publication-title: J. Agric. Food Chem.
  doi: 10.1021/jf202176d
  contributor:
    fullname: Miclo
– volume: 103
  start-page: 253
  year: 2018
  ident: ref_102
  article-title: Microbial proteases: Production and application in obtaining protein hydrolysates
  publication-title: Food Res. Int.
  doi: 10.1016/j.foodres.2017.10.044
  contributor:
    fullname: Sato
– volume: 7
  start-page: 1
  year: 2017
  ident: ref_87
  article-title: YebC, a putative transcriptional factor involved in the regulation of the proteolytic system of Lactobacillus
  publication-title: Sci. Rep.
  doi: 10.1038/s41598-017-09124-1
  contributor:
    fullname: Brown
– volume: 89
  start-page: 39
  year: 2016
  ident: ref_30
  article-title: Formation of taste-active amino acids, amino acid derivatives and peptides in food fermentations–A review
  publication-title: Food Res. Int.
  doi: 10.1016/j.foodres.2016.08.042
  contributor:
    fullname: Zhao
– volume: 1
  start-page: 17
  year: 1992
  ident: ref_123
  article-title: A review of proteotlytic enzymes from marine organisms and their application in the food industry
  publication-title: J. Aquat. Food Prod. Technol.
  doi: 10.1300/J030v01n01_05
  contributor:
    fullname: Haard
– volume: 12
  start-page: 179
  year: 1993
  ident: ref_48
  article-title: The physiology and biochemistry of the proteolytic system in lactic acid bacteria
  publication-title: FEMS Microbiol. Rev.
  doi: 10.1111/j.1574-6976.1993.tb00018.x
  contributor:
    fullname: Pritchard
– volume: 177
  start-page: 3472
  year: 1995
  ident: ref_47
  article-title: The extracellular P(I)-type proteinase of Lactococcus lactis hydrolyzes β-casein into more than one hundred different oligopeptides
  publication-title: J. Bacteriol.
  doi: 10.1128/jb.177.12.3472-3478.1995
  contributor:
    fullname: Juillard
– volume: 103
  start-page: 2731
  year: 2019
  ident: ref_55
  article-title: Soluble Lactobacillus delbrueckii subsp. bulgaricus 92059 PrtB proteinase derivatives for production of bioactive peptide hydrolysates from casein
  publication-title: Appl. Microbiol. Biotechnol.
  doi: 10.1007/s00253-018-09586-x
  contributor:
    fullname: Li
– volume: 183
  start-page: 3614
  year: 2001
  ident: ref_95
  article-title: Transcriptional pattern of genes coding for the proteolytic system of Lactococcus lactis and evidence for coordinated regulation of key enzymes by peptide supply
  publication-title: J. Bacteriol.
  doi: 10.1128/JB.183.12.3614-3622.2001
  contributor:
    fullname: Renault
– volume: 96
  start-page: 623
  year: 2016
  ident: ref_92
  article-title: Acquisition of PrtS in Streptococcus thermophilus is not enough in certain strains to achieve rapid milk acidification
  publication-title: Dairy Sci. Technol.
  doi: 10.1007/s13594-016-0292-3
  contributor:
    fullname: Galia
– volume: 312
  start-page: 126035
  year: 2020
  ident: ref_22
  article-title: Integrated approach for obtaining bioactive peptides from whey proteins hydrolysed using a new proteolytic lactic acid bacteria
  publication-title: Food Chem.
  doi: 10.1016/j.foodchem.2019.126035
  contributor:
    fullname: Worsztynowicz
– volume: 89
  start-page: 37
  year: 2020
  ident: ref_8
  article-title: Production, purification and biochemical characterization of the microbial protease produced by Lactobacillus fermentum R6 isolated from Harbin dry sausages
  publication-title: Process Biochem.
  doi: 10.1016/j.procbio.2019.10.029
  contributor:
    fullname: Sun
– volume: 58
  start-page: 1
  year: 2020
  ident: ref_26
  article-title: Polyphasic characterisation of non-starter lactic acid bacteria from Algerian raw Camel’s milk and their technological aptitudes
  publication-title: Food Technol. Biotechnol.
  doi: 10.17113/ftb.58.03.20.6598
  contributor:
    fullname: Saidi
– volume: 270
  start-page: 1569
  year: 1995
  ident: ref_88
  article-title: Transport of β-casein-derived peptides by the oligopeptide transport system is a crucial step in the proteolytic pathway of Lactococcus lactis
  publication-title: J. Biol. Chem.
  doi: 10.1074/jbc.270.4.1569
  contributor:
    fullname: Kunji
– volume: 237
  start-page: 17
  year: 2016
  ident: ref_101
  article-title: Protease and lipase activities of fungal and bacterial strains derived from an artisanal raw ewe’s milk cheese
  publication-title: Int. J. Food Microbiol.
  doi: 10.1016/j.ijfoodmicro.2016.08.007
  contributor:
    fullname: Wiebenga
– volume: 118
  start-page: 108779
  year: 2020
  ident: ref_18
  article-title: Application of lactic acid fermentation to elderberry juice: Changes in acidic and glucidic fractions
  publication-title: LWT
  doi: 10.1016/j.lwt.2019.108779
  contributor:
    fullname: Cirlini
– volume: 57
  start-page: 3661
  year: 2017
  ident: ref_69
  article-title: High γ-aminobutyric acid production from lactic acid bacteria: Emphasis on Lactobacillus brevis as a functional dairy starter
  publication-title: Crit. Rev. Food Sci. Nutr.
  doi: 10.1080/10408398.2016.1147418
  contributor:
    fullname: Wu
– volume: 2018
  start-page: 5063185
  year: 2018
  ident: ref_13
  article-title: Food-origin lactic acid bacteria may exhibit probiotic properties: Review
  publication-title: Biomed Res. Int.
– volume: 128
  start-page: 254
  year: 2019
  ident: ref_32
  article-title: A systematic reconsideration on proteases
  publication-title: Int. J. Biol. Macromol.
  doi: 10.1016/j.ijbiomac.2019.01.081
  contributor:
    fullname: Gurumallesh
– volume: 177
  start-page: 4652
  year: 1995
  ident: ref_80
  article-title: Specificity of peptide transport systems in Lactococcus lactis: Evidence for a third system which transports hydrophobic di- and tripeptides
  publication-title: J. Bacteriol.
  doi: 10.1128/jb.177.16.4652-4657.1995
  contributor:
    fullname: Foucaud
– volume: 38
  start-page: 104
  year: 2014
  ident: ref_53
  article-title: Use of a free form of the Streptococcus thermophilus cell envelope protease PrtS as a tool to produce bioactive peptides
  publication-title: Int. Dairy J.
  doi: 10.1016/j.idairyj.2014.01.008
  contributor:
    fullname: Chang
– volume: 11
  start-page: 5307
  year: 2020
  ident: ref_118
  article-title: Brewers’ spent yeast and grain protein hydrolysates as second-generation feedstuff for aquaculture feed
  publication-title: Waste Biomass Valoriz.
  doi: 10.1007/s12649-020-01145-8
  contributor:
    fullname: Orive
– volume: 46
  start-page: 5883
  year: 2019
  ident: ref_36
  article-title: Next generation sequencing, biochemical characterization, metabolic pathway analysis of novel probiotic Pediococcus acidilactici NCDC 252 and it’s evolutionary relationship with other lactic acid bacteria
  publication-title: Mol. Biol. Rep.
  doi: 10.1007/s11033-019-05022-z
  contributor:
    fullname: Bansal
– volume: 64
  start-page: 6985
  year: 2016
  ident: ref_49
  article-title: Characterization of a New Cell Envelope Proteinase PrtP from Lactobacillus rhamnosus CGMCC11055
  publication-title: J. Agric. Food Chem.
  doi: 10.1021/acs.jafc.6b03379
  contributor:
    fullname: Guo
– volume: 43
  start-page: 212
  year: 2018
  ident: ref_125
  article-title: Probiotics for human use
  publication-title: Nutr. Bull.
  doi: 10.1111/nbu.12334
  contributor:
    fullname: Sanders
– volume: 50
  start-page: 43
  year: 2010
  ident: ref_52
  article-title: The presence of prtP proteinase gene in natural isolate Lactobacillus plantarum BGSJ3-18
  publication-title: Lett. Appl. Microbiol.
  doi: 10.1111/j.1472-765X.2009.02748.x
  contributor:
    fullname: Topisirovic
– volume: 8
  start-page: 2285
  year: 2017
  ident: ref_12
  article-title: Extractive Fermentation of lactic acid in lactic acid bacteria cultivation: A review
  publication-title: Front. Microbiol.
  doi: 10.3389/fmicb.2017.02285
  contributor:
    fullname: Othman
– volume: 11
  start-page: e00133
  year: 2020
  ident: ref_39
  article-title: Enhancement of amino acid production and secretion by Lactococcus lactis using a droplet-based biosensing and selection system
  publication-title: Metab. Eng. Commun.
  doi: 10.1016/j.mec.2020.e00133
  contributor:
    fullname: Hermans
– volume: 99
  start-page: 4277
  year: 2015
  ident: ref_56
  article-title: Characterization of the mature cell surface proteinase of Lactobacillus delbrueckii subsp. lactis CRL 581
  publication-title: Appl. Microbiol. Biotechnol.
  doi: 10.1007/s00253-014-6258-6
  contributor:
    fullname: Villegas
– volume: 173
  start-page: 4517
  year: 1991
  ident: ref_62
  article-title: Lactococcal proteinase maturation protein PrtM is a lipoprotein
  publication-title: J. Bacteriol.
  doi: 10.1128/jb.173.14.4517-4525.1991
  contributor:
    fullname: Haandrikman
– volume: 20
  start-page: 489
  year: 2019
  ident: ref_16
  article-title: Effect of pullulan on physicochemical, microbiological, and sensory quality of yogurts
  publication-title: Curr. Pharm. Biotechnol.
  doi: 10.2174/1389201020666190416151129
  contributor:
    fullname: Kycia
– volume: 76
  start-page: 2056
  year: 1993
  ident: ref_64
  article-title: Genetics of proteolytic enzymes of lactococci and their role in cheese flavor development
  publication-title: J. Dairy Sci.
  doi: 10.3168/jds.S0022-0302(93)77540-2
  contributor:
    fullname: Kok
– volume: 61
  start-page: 3934
  year: 1995
  ident: ref_46
  article-title: Involvement of enzyme-substrate charge interactions in the caseinolytic specificity of lactococcal cell envelope-associated proteinases
  publication-title: Appl. Environ. Microbiol.
  doi: 10.1128/aem.61.11.3934-3939.1995
  contributor:
    fullname: Reid
– volume: 53
  start-page: 613
  year: 2004
  ident: ref_90
  article-title: Intracellular effectors regulating the activity of the Lactococcus lactis CodY pleiotropic transaction regulator
  publication-title: Mol. Microbiol.
  doi: 10.1111/j.1365-2958.2004.04136.x
  contributor:
    fullname: Petranovic
– volume: 9
  start-page: 1978
  year: 2018
  ident: ref_76
  article-title: Global transcriptomic analysis and function identification of malolactic enzyme pathway of Lactobacillus paracasei L9 in response to bile stress
  publication-title: Front. Microbiol.
  doi: 10.3389/fmicb.2018.01978
  contributor:
    fullname: Ma
– volume: 40
  start-page: 1227
  year: 2001
  ident: ref_89
  article-title: Pleiotropic transcriptional repressor CodY senses the intracellular pool of branched-chain amino acids in Lactococcus lactis
  publication-title: Mol. Microbiol.
  doi: 10.1046/j.1365-2958.2001.02470.x
  contributor:
    fullname: Serror
– volume: 137
  start-page: 110365
  year: 2020
  ident: ref_116
  article-title: Role of enzymes for improvement in gluten-free foxtail millet bread: It’s effect on quality, textural, rheological and pasting properties
  publication-title: LWT
  doi: 10.1016/j.lwt.2020.110365
  contributor:
    fullname: Sarabhai
– volume: 8
  start-page: 24
  year: 2017
  ident: ref_124
  article-title: Protein hydrolysates in animal nutrition: Industrial production, bioactive peptides, and functional significance
  publication-title: J. Anim. Sci. Biotechnol.
  doi: 10.1186/s40104-017-0153-9
  contributor:
    fullname: Hou
– volume: 66
  start-page: 4772
  year: 2000
  ident: ref_60
  article-title: Streptococcus thermophilus cell wall-anchored proteinase: Release, purification, and biochemical and genetic characterization
  publication-title: Appl. Environ. Microbiol.
  doi: 10.1128/AEM.66.11.4772-4778.2000
  contributor:
    fullname: Garault
– volume: 4
  start-page: 30
  year: 2013
  ident: ref_84
  article-title: Lactobacillus helveticus: The proteolytic system
  publication-title: Front. Microbiol.
  doi: 10.3389/fmicb.2013.00030
  contributor:
    fullname: Griffiths
– volume: 21
  start-page: 34
  year: 2018
  ident: ref_14
  article-title: Recent developments on encapsulation of lactic acid bacteria as potential starter culture in fermented foods–A review
  publication-title: Food Biosci.
  doi: 10.1016/j.fbio.2017.11.003
  contributor:
    fullname: Kavitake
– volume: 280
  start-page: 34332
  year: 2005
  ident: ref_91
  article-title: The Lactococcus lactis CodY regulon: Identification of a conserved cis-regulatory element
  publication-title: J. Biol. Chem.
  doi: 10.1074/jbc.M502349200
  contributor:
    fullname: Geurts
– volume: 75
  start-page: 3238
  year: 2009
  ident: ref_57
  article-title: PrtH2, Not prtH, Is the ubiquitous cell wall proteinase gene in Lactobacillus helveticus
  publication-title: Appl. Environ. Microbiol.
  doi: 10.1128/AEM.02395-08
  contributor:
    fullname: Genay
– volume: 71
  start-page: 394
  year: 2006
  ident: ref_4
  article-title: Proteolytic systems of lactic acid bacteria
  publication-title: Appl. Microbiol. Biotechnol.
  doi: 10.1007/s00253-006-0427-1
  contributor:
    fullname: Savijoki
– volume: 96
  start-page: 29
  year: 2019
  ident: ref_41
  article-title: Expression of amino acid converting enzymes and production of volatile compounds by Lactococcus lactis IFPL953
  publication-title: Int. Dairy J.
  doi: 10.1016/j.idairyj.2019.04.004
  contributor:
    fullname: Requena
– volume: 68
  start-page: 1110
  year: 2016
  ident: ref_31
  article-title: Proteinases, their extracellular targets, and inflammatory signaling
  publication-title: Pharmacol. Rev.
  doi: 10.1124/pr.115.010991
  contributor:
    fullname: Ramachandran
– volume: 133
  start-page: 987
  year: 2019
  ident: ref_10
  article-title: Purification and biochemical characteristics of the microbial extracellular protease from Lactobacillus curvatus isolated from Harbin dry sausages
  publication-title: Int. J. Biol. Macromol.
  doi: 10.1016/j.ijbiomac.2019.04.169
  contributor:
    fullname: Sun
– volume: 18
  start-page: 1039
  year: 2019
  ident: ref_72
  article-title: Production of bioactive peptides from lactic acid bacteria: A sustainable approach for healthier foods
  publication-title: Compr. Rev. Food Sci. Food Saf.
  doi: 10.1111/1541-4337.12455
  contributor:
    fullname: Aguilar
– volume: 20
  start-page: 9
  year: 2019
  ident: ref_2
  article-title: Microbial hydrolytic enzymes: In silico studies between polar and tropical regions
  publication-title: Polar Sci.
  doi: 10.1016/j.polar.2019.04.003
  contributor:
    fullname: Nordin
– volume: 51
  start-page: 535
  year: 2006
  ident: ref_71
  article-title: Analysis of the presence of prtR proteinase gene in natural isolates of Lactobacillus rhamnosus
  publication-title: Folia Microbiol.
  doi: 10.1007/BF02931617
  contributor:
    fullname: Fira
– volume: 115
  start-page: 165
  year: 2007
  ident: ref_110
  article-title: Enzymatic activities of lactic acid bacteria isolated from Cornetto di Matera sourdoughs
  publication-title: Int. J. Food Microbiol.
  doi: 10.1016/j.ijfoodmicro.2006.10.026
  contributor:
    fullname: Zotta
– ident: ref_106
  doi: 10.1016/B978-0-12-813280-7.00008-6
– volume: 21
  start-page: 100771
  year: 2020
  ident: ref_115
  article-title: Evaluating the effects of lactic acid bacteria and olive leaf extract on the quality of gluten-free bread
  publication-title: Gene Rep.
  doi: 10.1016/j.genrep.2020.100771
  contributor:
    fullname: Moghaddam
– volume: 70
  start-page: 187
  year: 1996
  ident: ref_45
  article-title: The proteolytic systems of lactic acid bacteria
  publication-title: Antonie van Leeuwenhoek, Int. J. Gen. Mol. Microbiol.
  doi: 10.1007/BF00395933
  contributor:
    fullname: Kunji
– ident: ref_93
  doi: 10.1186/s12866-017-1125-0
– volume: 122
  start-page: 109064
  year: 2020
  ident: ref_19
  article-title: Effects of lactic acid fermentation-based biotransformation on phenolic profiles, antioxidant capacity and flavor volatiles of apple juice
  publication-title: LWT
  doi: 10.1016/j.lwt.2020.109064
  contributor:
    fullname: Wu
– volume: 55
  start-page: 45
  year: 2020
  ident: ref_1
  article-title: Emerging strategies for expanding the toolbox of enzymes in biocatalysis
  publication-title: Curr. Opin. Chem. Biol.
  doi: 10.1016/j.cbpa.2019.12.006
  contributor:
    fullname: Sandoval
– volume: 79
  start-page: 136
  year: 2018
  ident: ref_109
  article-title: Bioactive peptides as natural antioxidants in food products–A review
  publication-title: Trends Food Sci. Technol.
  doi: 10.1016/j.tifs.2018.07.003
  contributor:
    fullname: Lorenzo
– ident: ref_17
  doi: 10.1111/ijfs.14915
– volume: 64
  start-page: 102399
  year: 2020
  ident: ref_117
  article-title: Recent developments in high gravity beer-brewing
  publication-title: Innov. Food Sci. Emerg. Technol.
  doi: 10.1016/j.ifset.2020.102399
  contributor:
    fullname: Puligundla
– volume: 171
  start-page: 2795
  year: 1989
  ident: ref_67
  article-title: A maturation protein is essential for production of active forms of Lactococcus lactis SK11 serine proteinase located in or secreted from the cell envelope
  publication-title: J. Bacteriol.
  doi: 10.1128/jb.171.5.2795-2802.1989
  contributor:
    fullname: Vos
– volume: 73
  start-page: 365S
  year: 2001
  ident: ref_21
  article-title: Taxonomy and important features of probiotic microorganisms in food and nutrition
  publication-title: Am. J. Clin. Nutr.
  doi: 10.1093/ajcn/73.2.365s
  contributor:
    fullname: Holzapfel
– volume: 20
  start-page: 369
  year: 2021
  ident: ref_23
  article-title: Cell-envelope proteinases from lactic acid bacteria: Biochemical features and biotechnological applications
  publication-title: Compr. Rev. Food Sci. Food Saf.
  doi: 10.1111/1541-4337.12676
  contributor:
    fullname: Ji
– ident: ref_20
  doi: 10.3390/v12111316
– volume: 58
  start-page: 78
  year: 1992
  ident: ref_68
  article-title: Proteinase overproduction in Lactococcus lactis strains: Regulation and effect on growth and acidification in milk
  publication-title: Appl. Environ. Microbiol.
  doi: 10.1128/aem.58.1.78-84.1992
  contributor:
    fullname: Bruinenberg
– volume: 55
  start-page: 218
  year: 2017
  ident: ref_120
  article-title: Brewery wastes reuse for protease production by lactic acid bacteria fermentation
  publication-title: Food Technol. Biotechnol.
  contributor:
    fullname: Silva
– volume: 103
  start-page: 1059
  year: 2019
  ident: ref_119
  article-title: Brewing with malted barley or raw barley: What makes the difference in the processes?
  publication-title: Appl. Microbiol. Biotechnol.
  doi: 10.1007/s00253-018-9537-9
  contributor:
    fullname: Kok
– volume: 3
  start-page: 63
  year: 2001
  ident: ref_96
  article-title: Autoregulation of the biosynthesis of the CcpA-like protein, PepR1, in Lactobacillus delbrueckii subsp. bulgaricus
  publication-title: J. Mol. Microbiol. Biotechnol.
  contributor:
    fullname: Morel
– ident: ref_42
  doi: 10.3390/fermentation5040096
– volume: 3
  start-page: 2048
  year: 2010
  ident: ref_38
  article-title: Biological aspects of proteolytic enzymes: A Review
  publication-title: J. Pharm. Res.
  contributor:
    fullname: Mahajan
– volume: 10
  start-page: 3019
  year: 2020
  ident: ref_75
  article-title: Adherence of Lactobacillus salivarius to HeLa cells promotes changes in the expression of the genes involved in biosynthesis of their ligands
  publication-title: Front. Immunol.
  doi: 10.3389/fimmu.2019.03019
– ident: ref_24
  doi: 10.3390/foods9101399
– volume: 2
  start-page: 1261780
  year: 2016
  ident: ref_107
  article-title: Plant and bacterial proteases: A key towards improving meat tenderization, a mini review
  publication-title: Cogent Food Agric.
  contributor:
    fullname: Arshad
– volume: 239
  start-page: 95
  year: 2004
  ident: ref_34
  article-title: Glutamic protease distribution is limited to filamentous fungi
  publication-title: FEMS Microbiol. Lett.
  doi: 10.1016/j.femsle.2004.08.023
  contributor:
    fullname: Sims
– volume: 2018
  start-page: 7957269
  year: 2018
  ident: ref_33
  article-title: The role of microbial aspartic protease enzyme in food and beverage industries
  publication-title: J. Food Qual.
  doi: 10.1155/2018/7957269
  contributor:
    fullname: Mamo
– volume: 125
  start-page: 564
  year: 2018
  ident: ref_103
  article-title: Brazilian artisanal ripened cheeses as sources of proteolytic lactic acid bacteria capable of reducing cow milk allergy
  publication-title: J. Appl. Microbiol.
  doi: 10.1111/jam.13779
  contributor:
    fullname: Biscola
– volume: 69
  start-page: 5802
  year: 2003
  ident: ref_70
  article-title: Identification and genetic characterization of a novel proteinase, PrtR, from the human isolate Lactobacillus rhamnosus BGT10
  publication-title: Appl. Environ. Microbiol.
  doi: 10.1128/AEM.69.10.5802-5811.2003
  contributor:
    fullname: Pastar
– volume: 63
  start-page: 2213
  year: 1997
  ident: ref_81
  article-title: Cloning and functional expression in Escherichia coli of the gene encoding the Di- and tripeptide transport protein of Lactobacillus helveticus
  publication-title: Appl. Environ. Microbiol.
  doi: 10.1128/aem.63.6.2213-2217.1997
  contributor:
    fullname: Nakajima
– volume: 42
  start-page: 476
  year: 2012
  ident: ref_29
  article-title: Purification and characterization of a proteinase from the probiotic Lactobacillus rhamnosus OXY
  publication-title: Prep. Biochem. Biotechnol.
  doi: 10.1080/10826068.2012.656869
  contributor:
    fullname: Kieliszek
– volume: 244
  start-page: 1873
  year: 2018
  ident: ref_111
  article-title: Sourdoughs as a source of lactic acid bacteria and yeasts with technological characteristics useful for improved bakery products
  publication-title: Eur. Food Res. Technol.
  doi: 10.1007/s00217-018-3100-x
  contributor:
    fullname: Martorana
– volume: 295
  start-page: 3347
  year: 2020
  ident: ref_3
  article-title: Uncovering the activities, biological roles, and regulation of bacterial cell wall hydrolases and tailoring enzymes
  publication-title: J. Biol. Chem.
  doi: 10.1074/jbc.REV119.010155
  contributor:
    fullname: Do
– volume: 18
  start-page: 121
  year: 2017
  ident: ref_15
  article-title: The Effect of pullulan on the growth and acidifying activity of selected stool microflora of human
  publication-title: Curr. Pharm. Biotechnol.
  doi: 10.2174/1389201017666161229154324
  contributor:
    fullname: Gniewosz
– volume: 10
  start-page: 1
  year: 2019
  ident: ref_28
  article-title: Comparative studies of versatile extracellular proteolytic activities of lactic acid bacteria and their potential for extracellular amino acid productions as feed supplements
  publication-title: J. Anim. Sci. Biotechnol.
  doi: 10.1186/s40104-019-0323-z
  contributor:
    fullname: Lim
– volume: 24
  start-page: 146
  year: 2017
  ident: ref_66
  article-title: Lactic acid bacteria as cell factories for the generation of bioactive peptides
  publication-title: Protein Pept. Lett.
  doi: 10.2174/0929866524666161123111333
  contributor:
    fullname: Brown
– volume: 91
  start-page: 34
  year: 2020
  ident: ref_122
  article-title: Proteolytic enzymes positively modulated the physicochemical and antioxidant properties of spent yeast protein hydrolysates
  publication-title: Process Biochem.
  doi: 10.1016/j.procbio.2019.11.030
  contributor:
    fullname: Marson
– volume: 7
  start-page: 1
  year: 2017
  ident: ref_86
  article-title: Improving nitrogen source utilization from defatted soybean meal for nisin production by enhancing proteolytic function of Lactococcus lactis F44
  publication-title: Sci. Rep.
  contributor:
    fullname: Liu
– volume: 5
  start-page: 737
  year: 1995
  ident: ref_73
  article-title: Genetic manipulation of the peptidolytic system in lactic acid bacteria
  publication-title: Int. Dairy J.
  doi: 10.1016/0958-6946(95)00029-1
  contributor:
    fullname: Kok
– volume: 85
  start-page: 237
  year: 2018
  ident: ref_51
  article-title: Peptidomic study of casein proteolysis in bovine milk by Lactobacillus casei PRA205 and Lactobacillus rhamnosus PRA331
  publication-title: Int. Dairy J.
  doi: 10.1016/j.idairyj.2018.06.010
  contributor:
    fullname: Solieri
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SecondaryResourceType review_article
Snippet Over the past several decades, we have observed a very rapid development in the biotechnological use of lactic acid bacteria (LAB) in various branches of the...
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StartPage 1858
SubjectTerms Amino acids
Bacteria
Bacterial Proteins - chemistry
Biocatalysts
Biotechnology
Biotechnology industry
Cell walls
Covalent bonds
Dairy industry
Enzymes
Enzymology
Fermentation
Food industry
Genomes
Lactic acid
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Lactobacillales - enzymology
Metabolism
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Nitrogen metabolism
Nutritional requirements
Peptide Hydrolases - chemistry
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Title Characteristics of the Proteolytic Enzymes Produced by Lactic Acid Bacteria
URI https://www.ncbi.nlm.nih.gov/pubmed/33806095
https://www.proquest.com/docview/2548979241/abstract/
https://search.proquest.com/docview/2508566251
https://pubmed.ncbi.nlm.nih.gov/PMC8037685
https://doaj.org/article/ca61523cc25c4ab580449489a6a5b962
Volume 26
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