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IUB No. Enzyme Name Source Approved in EC 1,4-Alpha-Glucan Bacillus Subtilis JECFA, Denmark, France, Brazil, 2.4.1.18 Branching Enzyme USA (GRAS Notice No

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  • IUB No.
  • Enzyme name
  • Source
  • Approved in

EC 2.4.1.18
1,4-alpha-glucan branching enzyme

Bacillus subtilis

JECFA, Denmark, France, Brazil, USA (GRAS Notice No. GRN 00274)

  • Alpha-acetolactate Bacillus subtilis expressed in
  • USA 21 CFR 173.115

decarboxylase

Bacillus brevis

EC 3.2.1.1 Alpha amylase

Aspergillus niger

Australia/New Zealand, Canada, France, Brazil, Mexico, USA (GRN 89)

Aspergillus oryzae

Australia/New Zealand, Canada, France, Brazil, Mexico, USA (GRN 90)

Bacillus amyloliquefaciens Bacillus licheniformis

Australia and New Zealand, Canada, Mexico, Brazil, USA 21 CFR 184.1148

Belgium, France, China, Japan, Denmark, Australia and New Zealand, Canada, Mexico, Brazil

Bacillus licheniformis expressed Australia/New Zealand, Canada,

in Bacillus licheniformis

France, Brazil, Denmark, Mexico, USA GRAS Notice No. GRN 000079, JECFA

Bacillus licheniformis and Bacillus amyloliquefaciens expressed in Bacillus licheniformis

GRAS Notice No. GRN 00022, Brazil, Mexico

Bacillus amyloliquefaciens expressed in Bacillus licheniformis

Brazil, Denmark, France

Bacillus megaterium expressed

JECFA, Canada, Brazil, Mexico

in Bacillus subtilis Bacillus stearothermophilus

JECFA, Canada, Brazil, Mexico, USA 21 CFR 184.1012

Bacillus stearothermophilus expressed in Bacillus licheniformis

Australia/New Zealand, Canada, France, Brazil, Denmark, Mexico, Japan, GRAS Notice No. GRN 000024

Bacillus stearothermophilus expressed in Bacillus subtilis

Australia/New Zealand, Canada, France, Brazil, Denmark, Mexico

Bacillus stearothermophilus (Geobacillus stearothermophilus)

Australia/New Zealand, Canada, France, Europa, Brazil, Mexico, USA (GRN 594)

Bacillus subtilis

Australia and New Zealand, Canada, Mexico, Brazil, USA 21 CFR 184.1148

Rhizopus delemar Rhizopus oryzae

Brazil Brazil, Mexico, USA GRAS Notice No. GRN 000090

Thermoccocales expressed in

Brazil, USA (GRN126)

Pseudomonas fluorecens Rhizomucor pusillus expressed in Aspergillus niger

Brazil, Denmark, France, Mexico, Australia and New Zealand.

Thermoactinomyces vulgaris expressed in B. subtilis

Alicyclobacillus pohliae expressed in Bacillus subtillis

Canada, Denmark, Mexico USA (GRAS Notice No. GRN 604) France

Cytophaga sp. expressed in Bacillus licheniformis

Aspergillus kawachii expressed in Trichoderma reesei

Barley malt, malted cereals

Pseudomonas fluorecens Trichoderma reesei

USA 21 CFR 184.1443a Canada, France Denmark, France
EC 4.1.1.5 Alfa-acetolactate decarboxylase

Bacillus brevis expressed in Bacillus subtilis

Australia/New Zealand, Canada, France, Europe, JECFA, Brazil, Denmark

Bacillus brevis expressed in Bacillus licheniformis

Brazil, Denmark, France, Mexico, Canada, GRAS Notice No. GRN 00587,

Bacillus subtilis

Australia, Denmark

Bacillus amyloliquefaciens

Australia Denmark

Bacillus licheniformis Aspergillus niger

EC 3.2.1.1 Alphagalactosidase
Brazil, Mexico, New Zealand, Australia

Mortierella vinacea

Brazil, Mexico, USA 21 CFR 173.145

Saccharomyces carlsbergensis

Brazil, Mexico
EC 3.2.1.133
Maltogenic amylase

Bacillus stearothermophilus expressed in Bacillus licheniformis

Brazil, Australia, Canada, China, France, JECFA, Japan, Denmark, Mexico, USA (GRN 751)

Bacillus stearothermophilus expressed in Bacillus subtilis

Brazil, Mexico, Canada, China, France, JECFA, USA (GRN 746 y GRN 751)

Pseudomonas stutzeri expressed in Bacillus licheniformis

Australia and New Zealand, Canada, Mexico, Brazil

Geobacillus stearothermophilus  Canada, China, France, JECFA, expressed in Bacillus subtilis

Aspergillus niger var. awamori Aspergillus niger

Japan, Australia, Denmark, Brazil, Mexico, USA (GRN 751)

  • Canada, Brazil
  • EC 3.2.1.3 Amyloglucosidase

or Glucoamylase
Australia and New Zealand, Canada, France, Brazil, Mexico, Japan, Denmark, USA (GRN 89)

Aspergillus niger expressed in Aspergillus niger

Brazil, Mexico, Australia and New Zealand, Canada, Mexico, USA (GRN 751)

Aspergillus oryzae Rhizopus arrhizus

JECFA, Australia and New Zealand, Canada, France, Brazil, Mexico, USA (GRN 90)

Australia and New Zealand, Canada, Brazil, Mexico

Rhizopus delemar Rhizopus niveus

Australia and New Zealand, Brazil Mexico, Australia and New Zealand, Brazil, USA 21 CFR 173.110

Rhizopus oryzae

Mexico, Australia and New Zealand, Brazil, USA (GRN 90)

Talaromyces emersonii expressed in Aspergillus niger

Brazil, Canada, China, Denmark, France, Mexico

Trichoderma reesei

Brazil
Trametes cingulata expressed in Denmark, France

Aspergillus niger Trichoderma reesei expressed

Brazil, USA (GRN 372), JECFA

in Trichoderma reesei Gloeophyllum trebeum

Brazil, Denmark, France, Mexico

expressed in Aspergillus niger Rhizopus delemar var. multiplicisporus

Aspergillus fumigatus expressed Mexico in Trichoderma reesei

Fusarium verticilloides expressed in Trichoderma reesei

Mexico

Penicillium oxalicum expressed in Aspergillus niger

Denmark, Mexico, Canada

Glucoamylase de Aspergillus niger 41SAM2-54

EC 2.4.1.25
Amylomaltase

Thermus thermophilus expressed in Bacillus amyloliquefaciens

Australia/New Zealand, Canada, USA (GRN 507)

Aspergillus oryzae

USA (GRAS Notice GRN No. 274) USA (GRN 274)

Aspergillus oryzae Bacillus amyloliquefaciens

Australia

Aminoglycoside 3′- Eschericha coli expressed in phosphotransferas Eschericha coli

e II
USA (21 CFR 173.170)

Eschericha coli expressed in Eschericha coli

USA 21 CFR 173.170

  • EC
  • Aminopeptidase

Lactococcus lactis

USA GRAS 3445, Brazil,

  • 3.4.11.1
  • Australia/New Zealand, Canada

  • Aspergillus oryzae
  • Australia/New Zealand, China,

France, Denmark, USA (GRN 90)

Lactococcus lactis (Streptococcus lactis)

Aspergillus melleus

USA 21 CFR 184.1985 China, Denmark, France, Japan Japan
EC 3.5.4.6 AMP deaminase

Streptomyces murinus

EC 3.2.1.55

Arabinofuranosidas Talaromyces pinophilus

Denmark, Mexico, USA (GRN

  • 000680)
  • e

expressed in Trichoderma reesei

Aspergillus niger

Australia, China, France, JECFA
EC 3.5.1.1 Asparaginase

Aspergillus niger expressed in Aspergillus niger

Australia/New Zealand, Brazil, Canada, China, Denmark, France, JECFA, Mexico, USA (GRN 214)

Aspergillus oryzae expressed in Australia/New Zealand Brazil,

Aspergillus oryzae

Mexico, Europe, Denmark, France, Canada, China, JECFA, Mexico, USA (GRN 201)

Pyrococcus furiosus expressed in Bacillus subtilis

Australia/New Zealand Brazil, Mexico, Europe, Denmark, Canada, USA (GRN 476), France

Aspergillus niger

Australia

Aspergillus oryzae

JECFA, Denmark, France, Brazil

Bacillus subtilis

Denmark, France, Brazil

  • EC 3.4.23
  • Aspartic protease

Cynara cardunculus L.

USA (GRAS Notice GRN No. 551)

Cynara cardunculus L. Bacillus licheniformis

USA (GRN 551)

  • Denmark
  • EC 3.2.1.2 Beta-amylase

Bacillus cereus

Brazil

Bacillus megaterium Bacillus subtilis

Brazil Brazil

Bacillus flexus expressed in Bacillus licheniformis

Brazil, Mexico, Denmark, France, USA (GRAS)

Cebeda

21 CFR 184.1443a
EC 3.2.1.6 Beta-glucanase

Aspergillus aculeatus

Australia/New Zealand, Brazil, Canada, China, Denmark, France, Mexico

Aspergillus niger Bacillus subtilis

Brazil, Canada, France Brazil, Canada, France

Disporotrichum

Brazil, Canada, USA (GRN 482)

dimorphosphorum Humicola insolens

Brazil, Canada, France. USA (GRN 195)

Penicillium emersonii

Brazil

Talaromyces emersonii

Brazil, Canada, France, USA (GRN 479), Australia

Trichoderma harzianum Trichoderma longibrachiatum Trichoderma reesei

Brazil, Canada, France Brazil Brazil, Canada, France, Australia, JECFA

Penicillium funiculosum

USA (GRN 584) USA (GRN 592)

Bacillus subtilis expressed in Bacillus subtilis

Rasamsonia composticola Aspergillus niger

Beta-glucosidase or cellobiase
Brazil Brazil

Trichoderma harzianum Trichoderma reesei Apergillus niger

Brazil
EC 3.2.1.21 E.C.
Beta-glucosidase Bromelain
Brazil, USA (GRN 750)

Ananas comosus

USA 21 CFR 184.1024
3.4.22.32

A. bracteatus L. Bacillus licheniformis

USA 21 CFR 184.1024

  • Mexico
  • EC 3.2.1.3 Carbohydrase

Rhizopus oryzae

USA (GRAS Notice GRN No. 90, 21 CFR 173.130)

Aspergillus niger Rhizopus oryzae

USA 21 CFR 173.120 JECFA, Mexico, Brazil, USA (GRAS Notice GRN No. 90)
EC 3.2.1.3 Diastase

  • 3.4.16.5
  • Carboxypeptidase
  • Aspergillus niger expressed in Canada, Denmark, France, Mexico,

C

Aspergillus niger Aspergillus niger

Russia, USA (GRN 435) Australia/New Zealand, Brazil, Canada, China, France, USA (GRN 89), Mexico
EC 1.11.1.6
Catalase

Micrococcus lysodeicticus (micrococcus juteus)

USA 21 CFR 173.135, Canada, JECFA, Brazil, Mexico

Aspergillus niger expressed in Aspergillus niger

Australia/New Zealand, USA (GRN 89)

Bovine liver Aspergillus niger

USA 21 CFR 184.1034 Brazil, Mexico, Australia, New Zeland, Canada, JECFA, USA (GRN 89)
EC 3.2.1.4 Cellulase

Aspergillus oryzae

Brazil, USA (GRN 90)

Penicillium funiculosum Rhizopus delemar

Brazil, JECFA, USA (GRN 584) Brazil Brazil Brazil Brazil

Rhizopus oryzae Sporotrichum dimorphosporum Thielavia terrestris Trichoderma longibrachiatum

Brazil, Australia/New Zealand, Canada, China, Denmark, France, Mexico

Trichoderma reesei

Brazil, Canada, USA 21 CFR 184.1250

Rasamsonia (Talaromyces) emersonii

JECFA, USA (GRAS GRN 479)

Trichoderma viride

Australia

  • EC
  • Cyclodextrin

Bacillus licheniformis

Denmark, France

  • 2.4.1.19
  • glucanotransferase

Paenibacillus macerans

Australia

Thermoanaerobacter sp. expressed in Bacillus licheniformis Arthrobacter globiformis expressed in E. coli K-12 W3110

China, Denmark, France

  • USA (GRN 624)
  • EC

5.1.3.30
D-Allulose 3- epimerase

  • EC
  • Dextranase

Bacillus subtilis

Brazil
3.2.1.11

Chaetomium erraticum

Brazil, Australia, New Zeland, Brazil, Denmark, USA GRAS GRN 000027

Chaetomium gracile Klebsiella aerogenes

Brazil Brazil

Penicillium funiculosum

Brazil

Penicillium lilacinum

Brazil

Branching enzyme Rhodothermus obamensis

Brazil
Milk clotting enzymes

Endothia parasitica

USA 21 CFR 173.150

Bacillus cereus

USA 21 CFR 173.150 USA 21 CFR 173.150 USA 21 CFR 173.150

Mucor pusillus Lindt Mucor miehei Cooney et Emerson

Aspergillus oryzae Aspergillus niger

USA 21 CFR 173.150

  • Brazil
  • Esterase

Mucor miehei

Australia, New Zeland, Brazil, Denmark, USA 21 CFR 173.140

  • Brazil
  • EC 3.1.3.8 Phytase

Aspergillus niger Aspergillus niger expressed in Aspergillus niger Ficus

Brazil, Australia, France, JECFA

  • USA 21 CFR 184.1316
  • Ficin

EC 2.3.1.43
Phosfatidylcoline sterol O- acyltransferase

Aeromonas salmonicida expressed in Bacillus licheniformis

Brazil, Australia, GRAS GRN 265

  • EC 3.1.4.1 Phosphodiesterase Leptographium procerum
  • Denmark, France, USA (GRN 505)

USA (GRAS GRN 574)
I
EC 3.1.4.11
Phosphoinositide phospholipase C

Pseudomonas fluorescens Pseudomonas fluorescens gene

extracted from soil sample

Pseudomonas sp-62186 expressed in Bacillus licheniformis

Denmark, USA (GRAS GRN 728), Canada, Mexico

  • EC
  • Phospholipase A1
  • Fusarium venenatum expressed Brazil, USA (GRN 142), Australia,

3.1.1.32

in Aspergillus oryzae

Canada, China, Denmark, France, Mexico

Talaromyces leycettanus expressed in Aspergillus niger Streptomyces violaceoruber

Denmark, France, USA (GRN 651) Brazil, USA (GRN 145) USA (GRN 524)
EC 3.1.1.4 Phospholipase A2

A. nishimurae (ex fumigatus) expressed in T. reesei Aspergillus niger

Australia, Canada, China, Denmark, France, Japan

S. violaceoruber expressed in Streptomyces violaceoruber

USA (GRN 212) USA (GRN 183)

Porcine pancreas expressed in Aspergillus niger

A. nishimurae (ex fumigatus)

expressed in
France, USA GRAS #524, Mexico
EC 3.1.4.3 Phospholipase C

Pichia pastoris

Brazil, Argentina, Canada, China, France, JECFA, Mexico, USA (GRAS GRN 204)

Bacillus thuringiensis expressed Denmark, USA GRN (689), Canada

in Bacillus licheniformis Pseudomonas sp. 62186 expressed in Bacillus licheniformis

Canada, Denmark, USA (GRN 728)

Pichia pastoris gene extracted from soil sample

EC 3.2.1.6 Glucanase

Aspergillus niger

Canada Canada

Bacillus amyloliquefaciens Bacillus subtillis Rasamsonia emersonii (Talaromyces emersonii)

Canada Canada

Humicola insolens

Australia/New Zealand, Brazil, China, Denmark, France, Mexico, Canada, USA (GRN 195)

Trichoderma reesei

JECFA, Australia e Brazil

(longibrachiatum) expressed in Trichoderma reesei (longibrachiatum)

Bacillus amyloliquefaciens expressed in Bacillus amyloliquefaciens

Australia, China, France Australia, Brazil

Geosmithia emersonii Trichoderma reesei

  • Australia/New
  • Zealand,
  • Brazil,

Canada, France, JECFA, China, Singapore, South Korea

Trichoderma harzianum

Brazil, China, JECFA, USA (GRN 149),
EC 3.2.1.39
Glucanase

Streptomyces violaceoruber expressed in Streptomyces violaceoruber

JECFA, USA (GRAS GRN 728), Brazil, Japan

  • EC
  • Glucanase (beta)

Disporotrichum

Canada
3.2.1.58

dimorphosporum

EC 3.2.1.6 endo-1,3(4)-β-

T. reesei expressed in T. reesei  France, Denmark, Australia, USA

  • glucanase
  • 21 CFR

  • EC 5.3.1.5 Glucose isomerase Actinoplanes missourienses
  • Autralia, New Zeland, Canada,

JECFA, France, Brazil, Mexico

Bacillus coagulans

Autralia, New Zeland, Canada, JECFA, France, Brazil, Mexico, USA 21 CFR 184.1372 Brazil, Mexico

Microbacterium arborensens Streptomyces albus

Brazil

Streptomyces murinus

Brazil, Australia, New Zealand, Canada, Denmark, France, Mexico

Streptomyces olivaceus

Brazil, USA 21 CFR 184.1372 Brazil, USA 21 CFR 184.1372

Streptomyces olivochromogenes

Streptomyces rubiginosus Streptomyces violaceoniger

Brazil, USA 21 CFR 184.1372 Brazil

Penicillium chrysogenum

Denmark, France

expressed in Aspergillus niger Actinoplanes missouriensis Aspergillus niger

USA 21 CFR 184.1372 Brazil, China, Australia and New Zealand, USA (GRN 89)

Aspergillus oryzae

Brazil, Mexico, Denmark, USA GRAS GRN 000106

Aspergillus niger expressed in Aspergillus niger

Brazil Brazil

Aspergillus niger expressed in Aspergillus oryzae Penicillium amagasakiense

Brazil

Streptomyces rubiginosus expressed in Streptomyces rubiginosus

Mexico

  • EC 1.1.3.4 Glucose oxidase
  • Australia/New Zealand, Brazil,

Canada, China, Denmark, France, Mexico, USA (GRN 89)

Aspergillus niger

USA (GRN 106)

Aspergillus oryzae Aspergillus niger expressed in Aspergillus niger

Aspergillus niger expressed in Australia/New Zealand, Brazil,
Canada, China, Denmark, France, Mexico, USA (GRN 106)

Aspergillus oryzae Penicillium amagasakiense Penicillium

chrysogenum Brazil, Denmark, France

expressed in Aspergillus niger Penicillium expressed in T. reesei amagasakiense

France, Denmark, Canada, USA GRAS #707

  • EC
  • Glutaminase

Chryseobacterium proteolyticum  Brazil, USA (GRAS GRN 000267),

  • 3.5.1.44
  • France

Bacillus licheniformis expressed USA (GRN 774) in Bacillus licheniformis

Protein-glutaminase from Chryseobacterium proteolyticum  Canada AE-PG

EC 3.2.1.32
Hemicellulase endo-1,3-β- xylanase

Humicola insolens

Australia, Nueva Zelanda
Hemicellulase

Aspergillus niger Aspergillus oryzae Bacillus subtilis

Australia, Nueva Zelanda, Brazil Brazil Australia, Nueva Zelanda, Canada, Brazil

Rhizopus delemar Rhizopus oryzae

Brazil Brazil

Sporotrichum dimorphosporum Trichoderma reesei

Brazil

  • EC 3.2.1.8 Hemicellulase
  • Australia, Nueva Zelanda, Brazil

EC 3.2.1.78

Bacillus amyloliquefaciens Bacillus amyloliquefaciens

Australia, Nueva Zelanda Australia
EC 1.1.3.5 Hexose oxidase

EC 3.2.1.7 Inulinase

Chondrus crispus expressed in Hansenula polymorpha Aspergillus niger

Brazil, JECFA, Mexico Australia, Nueva Zelanda, France, Brazil, China, Mexico, USA (GRN 89)

Kluyveromyces fragilis

Brazil, Mexico

Sporotrichum dimorphosporum Aspergillus niger

Brazil, Mexico

  • Brazil
  • EC
  • Invertase

3.2.1.26

Bacillus subtilis

Brazil

Kluyveromyces fragilis

Brazil, USA (GRAS Notice GRN No. 88)

Saccharomyces carlsbergensis Saccharomyces cerevisiae

Brazil Mexico, Brazil, Australia, New Zealand, Canada, Denmark, France, USA (GRAS Notice GRN No. 88), JECFA

Protaminobacter rubrum

Brazil
EC 3.2.1.68 EC 1.10.3.2 EC
Isoamylase Laccase Lactase

Pseudomonas amyloderamosa

GRN No. 85

Myceliphthora thermophila expressed in Aspergillus oryzae  No.122)

Brazil, USA (GRAS Notice GRN

Bacillus subtilis Aspergillus niger Aspergillus oryzae

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  • Investigating the Impact of Mpapr1, an Aspartic Protease from the Yeast Metschnikowia Pulcherrima, on Wine Properties

    Investigating the Impact of Mpapr1, an Aspartic Protease from the Yeast Metschnikowia Pulcherrima, on Wine Properties

    THÈSE EN COTUTELLE PRÉSENTÉE POUR OBTENIR LE GRADE DE DOCTEUR DE L’UNIVERSITÉ DE BORDEAUX ET DE L’UNIVERSITÉ DE STELLENBOSCH ÉCOLE DOCTORALE DES SCIENCES DE LA VIE ET DE LA SANTÉ SPÉCIALITÉ ŒNOLOGIE FACULTY OF AGRISCIENCES Par Louwrens THERON ETUDE DE L’IMPACT DE MPAPR1, UNE PROTEASE ASPARTIQUE DE LA LEVURE METSCHNIKOWIA PULCHERRIMA, SUR LES PROPRIETES DU VIN Sous la direction de Benoit DIVOL et de Marina BELY Soutenue le 27 janvier 2017 Membres du jury: Mme. LE HENAFF-LE MARREC Claire, Professeur à l’université de Bordeaux Président M. MARANGON Matteo, Chargé de recherche à l’université de Padoue Rapporteur Mme. CAMARASA Carole, Chargée de recherche à l’INRA de Montpellier Rapporteur M. BAUER Florian, Professeur à l’université de Stellenbosch Examinateur Titre : Etude de l’impact de MpAPr1, une protéase aspartique de la levure Metschnikowia pulcherrima, sur les propriétés du vin Résumé : L'élimination des protéines est une étape clé lors de la production du vin blanc afin d'éviter l'apparition éventuelle d'un voile inoffensif mais inesthétique. Des solutions de rechange à l'utilisation de la bentonite sont activement recherchées en raison des problèmes technologiques, organoleptiques et de durabilité associés à son utilisation. Dans cette étude, MpAPr1, une protéase aspartique extracellulaire préalablement isolée et partiellement caractérisée à partir de la levure Metschnikowia pulcherrima, a été clonée et exprimée de manière hétérologue dans la levure Komagataella pastoris. Les propriétés enzymatiques de MpAPr1 ont été initialement caractérisées dans un extrait brut. Après plusieurs essais faisant appel à différentes techniques, MpAPr1 a été purifié avec succès par chromatographie échangeusede cations.
  • (A) Enzymes Derived from Animal Sources

    (A) Enzymes Derived from Animal Sources

    ANNEX (new entries are highlighted in yellow) PERMITTED ENZYMES (A) Enzymes derived from animal sources Enzyme EC Number Source Catalase 1.11.1.6 Bovine liver Lactoperoxidase 1.11.1.7 Bovine milk Bovine stomach; salivary glands or forestomach of calf, kid or lamb; porcine Lipase, triacylglycerol 3.1.1.3 or bovine pancreas Lysozyme 3.2.1.17 Egg whites Pancreatin (or pancreatic elastase) 3.4.21.36 Pancreas of the hog or ox Pepsin 3.4.23.1 Bovine or porcine stomach Phospholipase A2 3.1.1.4 Porcine pancreas Aqueous extracts from the fourth stomach of calves, kids, lambs, and adult Rennet 3.4.23.4 bovine animals, sheep and goats Thrombin 3.4.21.5 Bovine or porcine blood Trypsin 3.4.21.4 Porcine or bovine pancreas (B) Enzymes derived from plant sources Enzyme EC Number Source Alpha–amylase 3.2.1.1 Malted cereals Actinidin 3.4.22.14 Kiwifruit (Actinidia deliciosa) Malted cereals Beta-Amylase 3.2.1.2 Sweet potato (Ipomoea batatas) Bromelain 3.4.22.4 Pineapple fruit/stem (Ananas comosus and Ananas bracteatus (L)) Ficin 3.4.22.3 Ficus spp. Lipoxidase 1.13.11.12 Soyabean whey or meal Papain 3.4.22.2 Carica papaya (L) (Fam. Caricaceae) (C) Enzymes derived from microbial sources EC Enzyme Production organism Donor organism Donor gene Number 1,4-alpha-glucan branching 1,4-alpha-glucan branching 2.4.1.18 Bacillus subtilis Rhodothermus obamensis enzyme enzyme Alpha-acetolactate decarboxylase 4.1.1.5 Bacillus amyloliquefaciens Bacillus subtilis Bacillus subtilis Bacillus brevis Alpha-acetolactate decarboxylase Alpha-amylase 3.2.1.1 Aspergillus niger1 Aspergillus
  • Arabidopsis Thaliana Atypical Aspartic Proteases Involved in Primary Root Development and Lateral Root Formation

    Arabidopsis Thaliana Atypical Aspartic Proteases Involved in Primary Root Development and Lateral Root Formation

    André Filipe Marques Soares RLR1 and RLR2, two novel Arabidopsis thaliana atypical aspartic proteases involved in primary root development and lateral root formation 2016 Thesis submitted to the Institute for Interdisciplinary Research of the University of Coimbra to apply for the degree of Doctor in Philosophy in the area of Experimental Biology and Biomedicine, specialization in Molecular, Cell and Developmental Biology This work was conducted at the Center for Neuroscience and Cell Biology (CNC) of University of Coimbra and at Biocant - Technology Transfer Association, under the scientific supervision of Doctor Isaura Simões and at the Department of Biochemistry of University of Massachusetts, Amherst, under the scientific supervision of Doctor Alice Y. Cheung. Part of this work was also performed at the Department of Applied Genetics and Cell Biology, University of Natural Resources and Life Sciences, Vienna, under the scientific supervision of Doctor Herta Steinkellner and also at the Central Institute for Engineering, Electronics and Analytics, ZEA-3, Forschungszentrum Jülich, Jülich, under the schientific supervision of Doctor Pitter F. Huesgen. André Filipe Marques Soares was a student of the Doctoral Programme in Experimental Biology and Biomedicine coordinated by the Center for Neuroscience and Cell Biology (CNC) of the University of Coimbra and a recipient of the fellowship SFRH/BD/51676/2011 from the Portuguese Foundation for Science and Technology (FCT). The execution of this work was supported by a PPP grant of the German Academic Exchange Service with funding from the Federal Ministry of Education and Research (Project-ID 57128819 to PFH) and the Fundação para a Ciência e a Tecnologia (FCT) (grant: Scientific and Technological Bilateral Agreement 2015/2016 to IS) Agradecimentos/Acknowledgments Esta tese e todo o percurso que culminou na sua escrita não teriam sido possíveis sem o apoio, o carinho e a amizade de várias pessoas que ainda estão ou estiveram presentes na minha vida.
  • Handbook of Proteolytic Enzymes Second Edition Volume 1 Aspartic and Metallo Peptidases

    Handbook of Proteolytic Enzymes Second Edition Volume 1 Aspartic and Metallo Peptidases

    Handbook of Proteolytic Enzymes Second Edition Volume 1 Aspartic and Metallo Peptidases Alan J. Barrett Neil D. Rawlings J. Fred Woessner Editor biographies xxi Contributors xxiii Preface xxxi Introduction ' Abbreviations xxxvii ASPARTIC PEPTIDASES Introduction 1 Aspartic peptidases and their clans 3 2 Catalytic pathway of aspartic peptidases 12 Clan AA Family Al 3 Pepsin A 19 4 Pepsin B 28 5 Chymosin 29 6 Cathepsin E 33 7 Gastricsin 38 8 Cathepsin D 43 9 Napsin A 52 10 Renin 54 11 Mouse submandibular renin 62 12 Memapsin 1 64 13 Memapsin 2 66 14 Plasmepsins 70 15 Plasmepsin II 73 16 Tick heme-binding aspartic proteinase 76 17 Phytepsin 77 18 Nepenthesin 85 19 Saccharopepsin 87 20 Neurosporapepsin 90 21 Acrocylindropepsin 9 1 22 Aspergillopepsin I 92 23 Penicillopepsin 99 24 Endothiapepsin 104 25 Rhizopuspepsin 108 26 Mucorpepsin 11 1 27 Polyporopepsin 113 28 Candidapepsin 115 29 Candiparapsin 120 30 Canditropsin 123 31 Syncephapepsin 125 32 Barrierpepsin 126 33 Yapsin 1 128 34 Yapsin 2 132 35 Yapsin A 133 36 Pregnancy-associated glycoproteins 135 37 Pepsin F 137 38 Rhodotorulapepsin 139 39 Cladosporopepsin 140 40 Pycnoporopepsin 141 Family A2 and others 41 Human immunodeficiency virus 1 retropepsin 144 42 Human immunodeficiency virus 2 retropepsin 154 43 Simian immunodeficiency virus retropepsin 158 44 Equine infectious anemia virus retropepsin 160 45 Rous sarcoma virus retropepsin and avian myeloblastosis virus retropepsin 163 46 Human T-cell leukemia virus type I (HTLV-I) retropepsin 166 47 Bovine leukemia virus retropepsin 169 48
  • EUROPEAN COMMISSION Brussels, 28 April 2020 REGISTER of FOOD

    EUROPEAN COMMISSION Brussels, 28 April 2020 REGISTER of FOOD

    EUROPEAN COMMISSION DIRECTORATE-GENERAL FOR HEALTH AND FOOD SAFETY Food and feed safety, innovation Food processing technologies and novel foods Brussels, 28 April 2020 REGISTER OF FOOD ENZYMES TO BE CONSIDERED FOR INCLUSION IN THE UNION LIST Article 17 of Regulation (EC) No 1332/20081 provides for the establishment of a Register of all food enzymes to be considered for inclusion in the Union list. In accordance with that Article, the Register includes all applications which were submitted within the initial period fixed by that Regulation and which comply with the validity criteria laid down in accordance with Article 9(1) of (EC) No 1331/2008 establishing a common authorisation procedure for food additives, food enzymes and food flavourings2. The Register therefore lists all valid food enzyme applications submitted until 11 March 2015 except those withdrawn by the applicant before that date. Applications submitted after that date are not included in the Register but will be processed in accordance with the Common Authorisation Procedure. The entry of a food enzyme in the Register specifies the identification, the name, the source of the food enzyme as provided by the applicant and the EFSA question number under which the status of the Authority’s assessment can be followed3. As defined by Article 3 of Regulation (EC) No 1332/2008, ‘food enzyme’ subject to an entry in the Register, refers to a product that may contain more than one enzyme capable of catalysing a specific biochemical reaction. In the assessment process, such a food enzyme may be linked with several EFSA question numbers.
  • (12) United States Patent (10) Patent No.: US 8,561,811 B2 Bluchel Et Al

    (12) United States Patent (10) Patent No.: US 8,561,811 B2 Bluchel Et Al

    USOO8561811 B2 (12) United States Patent (10) Patent No.: US 8,561,811 B2 Bluchel et al. (45) Date of Patent: Oct. 22, 2013 (54) SUBSTRATE FOR IMMOBILIZING (56) References Cited FUNCTIONAL SUBSTANCES AND METHOD FOR PREPARING THE SAME U.S. PATENT DOCUMENTS 3,952,053 A 4, 1976 Brown, Jr. et al. (71) Applicants: Christian Gert Bluchel, Singapore 4.415,663 A 1 1/1983 Symon et al. (SG); Yanmei Wang, Singapore (SG) 4,576,928 A 3, 1986 Tani et al. 4.915,839 A 4, 1990 Marinaccio et al. (72) Inventors: Christian Gert Bluchel, Singapore 6,946,527 B2 9, 2005 Lemke et al. (SG); Yanmei Wang, Singapore (SG) FOREIGN PATENT DOCUMENTS (73) Assignee: Temasek Polytechnic, Singapore (SG) CN 101596422 A 12/2009 JP 2253813 A 10, 1990 (*) Notice: Subject to any disclaimer, the term of this JP 2258006 A 10, 1990 patent is extended or adjusted under 35 WO O2O2585 A2 1, 2002 U.S.C. 154(b) by 0 days. OTHER PUBLICATIONS (21) Appl. No.: 13/837,254 Inaternational Search Report for PCT/SG2011/000069 mailing date (22) Filed: Mar 15, 2013 of Apr. 12, 2011. Suen, Shing-Yi, et al. “Comparison of Ligand Density and Protein (65) Prior Publication Data Adsorption on Dye Affinity Membranes Using Difference Spacer Arms'. Separation Science and Technology, 35:1 (2000), pp. 69-87. US 2013/0210111A1 Aug. 15, 2013 Related U.S. Application Data Primary Examiner — Chester Barry (62) Division of application No. 13/580,055, filed as (74) Attorney, Agent, or Firm — Cantor Colburn LLP application No.
  • Purification and Characterization of an Aspartic Protease from The

    Purification and Characterization of an Aspartic Protease from The

    Electronic Journal of Biotechnology 17 (2014) 89–94 Contents lists available at ScienceDirect Electronic Journal of Biotechnology Purification and characterization of an aspartic protease from the Rhizopus oryzae protease extract, Peptidase R Nai-Wan Hsiao a,1,YehChenb,1,Yi-ChiaKuanb,c, Yen-Chung Lee d, Shuo-Kang Lee b, Hsin-Hua Chan b, Chao-Hung Kao b,⁎ a Institute of Biotechnology, National Changhua University of Education, Changhua 500, Taiwan b Department of Biotechnology, Hungkuang University, Taichung 433, Taiwan c Department of Life Science, National Tsing Hua University, Hsinchu 300, Taiwan d Department of Bioagricultural Science, National Chiayi University, Chiayi 600, Taiwan article info abstract Article history: Background: Aspartic proteases are a subfamily of endopeptidases that are useful in a variety of applications, Received 2 September 2013 especially in the food processing industry. Here we describe a novel aspartic protease that was purified from Accepted 14 January 2014 Peptidase R, a commercial protease preparation derived from Rhizopus oryzae. Available online 17 February 2014 Results: An aspartic protease sourced from Peptidase R was purified to homogeneity by anion exchange chromatography followed by polishing with a hydrophobic interaction chromatography column, resulting in a Keywords: 3.4-fold increase in specificactivity(57.5×103 U/mg) and 58.8% recovery. The estimated molecular weight of Chromatography the purified enzyme was 39 kDa. The N-terminal sequence of the purified protein exhibited 63–75% identity to Endopeptidase – Food processing industry rhizopuspepsins from various Rhizopus species. The enzyme exhibited maximal activity at 75°C in glycine HCl Homogeneity buffer, pH 3.4 with casein as the substrate.
  • Extracellular Acid Protease from Aspergillus Niger I1: Purification and Characterization

    Extracellular Acid Protease from Aspergillus Niger I1: Purification and Characterization

    African Journal of Biotechnology Vol. 8 (18), pp. 4582-4589, 15 September, 2009 Available online at http://www.academicjournals.org/AJB ISSN 1684–5315 © 2009 Academic Journals Full Length Research Paper Extracellular acid protease from Aspergillus niger I1: purification and characterization Rayda Siala#, Alya Sellami-Kamoun#, Mohamed Hajji, Ines Abid, Neji Gharsallah and Moncef Nasri* Laboratoire de Génie Enzymatique et de Microbiologie, Ecole Nationale d'Ingénieurs de Sfax, B.P. (W) 3038 Sfax, Tunisia. Accepted 30 April, 2009 A new strain of Aspergillus niger producing acid protease was isolated and identified by universal primers NL1 and NL4. The acid protease from A. niger I1 was purified to homogeneity by ultrafiltration using a 10-KDa cut-off membrane, gel filtration on Sephadex G-75 and ion exchange chromatography on CM-Sephadex C-50, with a 3.55-fold increase in specific activity and 56% recovery. The molecular weight of the protease was estimated to be 50 kDa on SDS-PAGE and gel filtration, which is higher than those from other A. niger strains. Carbohydrate content of the purified protease, determined by the chemical anthrone method, was calculated to be 16%. The Km and Vmax for caseinolytic activity of the purified enzyme were found to be 1.02 mM and 2.2 µmol/min, respectively. The enzyme was optimally active at 60°C and pH 3.0. The most metal ions tested had no significant effect on protease activity. The enzyme activity was inhibited by pepstatin A, suggesting that the purified enzyme is an aspartic protease. Key words: Acid protease, Aspergillus niger, purification, aspergillopepsin, glycosylation.