dataesr/scientific-paragraphs-categorization huggingface dataset:
The studied proteins were subjected to a specific "scanning" process which can be carried out in the BIOPEP-UWM database to find the so-called permutations with repetitions which indicate how many various fragments of sequences with antioxidant activity can be generated while having a monomeric protein molecule at one's disposal (hence, inter alia, the term "potential"). To this end, the generated profile of potential antioxidant activity and its numerical equivalent, i. e. , the A parameter, was used. Numerical values of the calculated A parameters, the number of potential bioactive fragments in the analysed protein sequence and the number of proteins in which such antioxidant fragments could be generated are presented in Table  1. Fragments of sequences with antioxidant activity are presented in the form of a single-letter amino acid code, in the same way as the fragments of amino acid sequences with different activities were recorded and are stored in the BIOPEP-UWM database resources.
1 , LHH (1) 2 , HL (1) 12 , AH (1) 13 (2), HH (2) 2 (3), EL (1) 12 , PYPQ (1) (2) 11 , (3) 5 (5), LHQ (1) 14 , LWQ (1) 14 , IR (1) 18 , TY (1) 16 , VY (1) 18 , LW (1) 14 , LLR (1) 2 , YQL (1) 16 , QYP (1) 16 (2) 2 , KYL, RW, AY, LY, HHH (1) 2 (2), PHQ (1)   8 , LHH, HL (1) 3 , AH (1) 8 (2), HH (2) (3), EL (1) 3 , PYPQ (2) 2 (3) 7 (5), LHQ (1) 7 , LWQ (1) 7 , IR (1) 11 , TY (1) 10 , VY (1) 10 , LW (1) 7 , YQL (1) 9 , QYP (1) 9 (2)  4 , PHQ (1) 7 (2) 19 , PWQ, PW (1) 4 , IR (1) 21 (2) 6 , SVNVPL (1) 2 , LWS (1) 20 , AQIPQQ (1) 23 , KP (1) 20 , VY (1) 23 , LW (1) 21 , VYV (1) 23 , LWQ, RYQ, MHI (1) 11 , TY (1) 5 , VPW (1) 3 , PYPQ (1) 12 , HH, FHH, LK (1) 3 , FC, YLL (1)   6 , PYPQ (1) 6 , LWS (1) 6 , PHQ (2) 6 , AQIPQQ (1) 6 , IR (1) 6 , KP (1) 6 , VY (1) 6 , LW (1) 6 , VYV (1) 6 , MHI (1)   5 , LQPGQGQQG (2) 5 , GYY (9) 5 (10) (12) (17) 2 (18) (20)  (22) , EL (1) 5 (2) 3 (3) 4 , WY (1) 7 (2), WYY (1) 7 (2), RYY (1) 6 , YYL (1) (2) 5 , YYS (1) 5 , SYY (1) 11 , PWY (1) 4 , PW (1) 10 , LK (2) 2 (3) 4 , WG (1) 12 , ACQ (1) 4 , PWS (1) 6 , MM, LH, HL, PYY, LHQ, RHY, QYP (4), LWG (1) 2 , PHQ (1) 2 , KP (1) 2  (2), LW (1)   4 (2) 8 (3) 3 (6)  (7) , LK (1) 5 (2) 4 (3), EL (1) 7 (2) 3 (3) 5 , RYY (1) 9 (2) 2 , SYY (1) 10 , WG (1) 13 , ACQ (1) 7 , PWS (1) 4 , PW (1) 5 , AY (1) 2 , LLR (1) 6 , YYL (1) 2 (2) 2 , LWQ, EYY (1) 2 , LWG (1) 2 , PWQ, LW (1) 3 , WY (1) 2 , WYY (1) 2 , YYS, AW, PYY  51 , AH (1) 18 , IY (1) 24 , RHE (1) 12 , IQY (1) 12 , IR (1) 55 , VY (1) 29 (2) 6 , AY (1) 27 , PHQ (1) 41 (2) 9 , PWQ (1) 23 , PW (1) 23 , SVNVPL (1) 32 , TY (1) 8 , LRTLPM (1) 3 , MM (1) 5 , LPM (1) 5 , PHK, WY (1) 4 , LWQ (1) 4 , LWY (1) 4 , KP (1) 10 , LW (2) 4 , HL (1) 15 , LH (1) 3 , HH (1) 8 (2) 4 , GPP (1) 3 , EL (1) 2 (2), SHH (1) 10 , HHH (1) 4 , LHN (1) 2 , PHL, RHQ, LHQ, THH  5 , EL (1) 4 (2) 3 , YCY (1) 2 , KD (1) 5 , LK (1) 3 , HL, LLPH, IY, YVL, KP, LW, LWI, PW (1) 4 , YVE, AH, MY (1) 2 , VKL (1) 3   3 , FC (1) 4 (2) 2 , YVE (1) 3 , EQC, EL (1) 2 , VKL, VKV, LK (1) 3  (3), KP (1) 5 , TY, VW (1) 2 , KD (1) 5 , YGY (1) 2 (2), WG (2) 3 , CGA (2) 3 , GAA (1)  n T -the number of total proteins including all protein fragments available from the BIOPEP-UWM database (access on August/September 2019 and from the 1st to the 10th December 2019.
The number of bioactive fragments with a particular amino acid sequence found in a single analysed protein is provided in brackets. The number of proteins in which the particular bioactive fragment(s) was (were) found is provided in the superscript. The histidine residues found in the bioactive sequences are highlighted in bold, *****, ******-the results provided in Table  1  do not include the data originating from analyses of two proteins (IDs 1365, 1364-classified into different groups of wheat proteins), even though they satisfied the conditions of the adopted molecular criterion. Results for both proteins are presented below Table  1. HMW-high molecular weight, LMW-low molecular weight. In the analysed protein groups, the analysis results for the molecules recorded in the BIOPEP-UWM database resources with identification numbers (IDs) of 1435, 1436, 1437, 1438 and 1431 were not taken into account due to the adopted molecular criterion (at least 100 amino acid residues in a protein monomer).
The number of bioactive fragments with a particular amino acid sequence found in a single analysed protein is provided in brackets. The number of proteins in which the particular bioactive fragment(s) was (were) found is provided in the superscript. The histidine residues found in the bioactive sequences are highlighted in bold, *****-globulins results have been marked, ******-expansin-B1 results has been marked. Other (1-4)-based on the number of amino acid residues found in the analysed protein or protein fragment and the A parameters were classified proteins. 1 ) 3 (2) 3 , PHQ (1) 8 (2) (15), PWQ (1) 2 (3), PW (1) 2 (2) 2 (3), IR (1) 4 , LLPF (1) 2 , QCL, EL (1) 3 (2) 2 , PYPQ (1) 2 (2) (3) 2 , PHI, LK (1) 2 , KP (1) 3     2 ), AH, EL (1) 3 (2), WY (1) 4 , RHG (1) 4 , MY (2) 3 , KD (2) 3 , TY (1) 2 (2), MM (1) 3 (2), IR (1) 3 , VY (1) 3  LH (1) 10 , GYY (1) 8 , EL (1) 10 , YYW (1) 8 , LHD (1) 10 , RWW (1) 8 (2) 2 , VKV (1) 10 , KVI (1) 10 , KD (1) 10 (2) 4 , RW (1) 8 (2) 2 , TW (1) 6 (2) 8 , YLL (1) 10 , IR (1) 4 , QYP 4 (2) 4 , YYQ, SYY, MY, KD (1) 5 (2), VY (1) 3 , CGA, VKL, PW (1) 3 , MWC, YCY, LK (1) 3 , PWT, GPP, FC (2), YVE, LY (1) 2 , LWI, YVL, LW, FKK, AY, AH (1) 3 , YYV (1) 2 , NYY (1) 2 , RHV (1) 2 , YVL (1) 2 , IR (1) 2 (2), AW, PHN, TY (1) (2), LH, LHI, HEH, HRH, PWE, RHR, RW, KP, IY n T -the number of total proteins including all protein fragments available from the BIOPEP-UWM database (access on August/September 2019 and from the 1st to the 10th December 2019.
0530 (0. 0272-0. 1165) EL (1) HL (1) FC (1) 2 (2) 2 , VYV (1) 2 , LH, IY (2) 2 , LHR I Avenins (9 T ) 210 (4 c ) (182-222) 4 (2-8) 0. 0166 (0. 0090-0. 0374) VY (1) 3 , VYV (1) 3 , AY, EL (2), PW, LK (2), TW (2) I Thaumatin-like pathogenesisrelated proteins (4 T ) 169 (4 c ) 8 (8-9) 0. 0488 (0. 0473-0. 0533) HHP (1) 3 , YHH (1) 3 , HH (1) 3 , AY (1) 4 , LK (1) 3 , VW (1) 4 , WG (1) 4 , FC (1) 4 , DYY, YYD, GGE, VY, TW I Avenoindolines + other (5 T ) 148 (2 c ) 10 (8-11) 0. 0642 (0. 0541-0. 0743) GYY (1) 2 , WY, YYW (1) 2 , RWW (1) 2 , KD (1) 2 , RW (1) 2 , TW (1) 2 , IR, EL, EAK, KVI, GPP, YLL n T -the number of total proteins including all protein fragments available from the BIOPEP-UWM database (access on August/September 2019 and from the 1st to the 10th December 2019. The data were updated as of 10 December 2019), n-the number of analysed proteins including selected fragments, c, f -protein sequence status ( c -complete, f -a protein fragment), x-a mean value, *NAAR-the number of amino acid residues found in the analysed protein or protein fragment, **NAFS-the number of potential sequence fragments with an antioxidant activity, ***A-the A parameter (the frequency of bioactive fragment occurrence in a protein sequence) (defined in the "Materials and Methods" section of the study), ****AAS-amino acid sequence presented in the form of a single-letter amino acid code: A-Alanine, R-Arginine, N-Asparagine, D-Aspartic acid, C-Cysteine, Q-Glutamine, E-Glutamic acid, G-Glycine, H-Histidine, I-Isoleucine, L-Leucine, K-Lysine, M-Methionine, F-Phenylalanine, P-Proline, S-Serine, T-Threonine, W-Tryptophan, Y-Tyrosine, V-Valine.
In Silico Hydrolysis of Selected Plant Proteins with the use of Selected Enzymes (BIOPEP-UWM) 1248 simulations of protein molecule proteolysis were carried out using the bioinformatic tools (in silico protein hydrolysis) available in the BIOPEP-UWM database. Enzymatic monocatalyses were carried out using ficin (EC 3. 4. 22. 3) or stem bromelain (EC 3. 4. 22. 32) or pepsin (pH > 2) (EC 3. 4. 23. 1) and a bioevaluation of the conducted processes was then carried out. The bioevaluation was conducted based on the obtained data on the bioactivity of the obtained proteolysis products (the number, the type of peptides with a given activity, including peptides with antioxidant activity), and the bioparameters characterising the process were calculated (DH t , A E , W) (the parameters were characterised in detail in the "Materials and Methods" section of the study).
0907 and 0. 1231, respectively, 0. 0853 and 0. 1452, and 0. 1285 and 0. 2666 (Table  6 ). Most antioxidant peptides with the TY sequences were obtained from gliadin proteins as a result of using ficin to carry out the hydrolysis. (2) 6 , WG (1) 12 , PWS (1) 5 , WY, IY 41. 02 (12 c ) 39. 01-43. 12 0. 0058 0. 0031-0. 0087 EL (1) 6 (2) 6 , YYL (1) (2) 5 , YYS (1) 5 , WG (1) 12   6 (2) 8 , WG (1) 13 , PWS (1) 4   24 , VY (1) 29 (2) 6 , PHQ (1) 41 (2) 9 , HL (1) 14 , PHK, WY (1) 4 , PWQ (1) 4 , PHL  n T -the number of total proteins including all protein fragments available from the BIOPEP-UWM database (access on August/September 2019 and from the 1st to the 10th December 2019. The data were updated as of 10 December 2019), n-the number of analysed proteins including selected fragments, c, f -protein sequence status ( c-complete, f -a protein fragment), x-a mean value, *DH t -the theoretical degree of hydrolysis.
0. 0088 0. 0032-0. 0212 AY (1) 7 (2) 2 (3) 2 AH (1) 9 (2) 4 , EL (1) 8 (2) 3 (4) 2 , PWS, IR (1) 8  (3) (5) 2 , TY (1) 8 (2) 2 (3), WG (1) 8 (2), VY (1) 2 (2) 4 , IY (1) 2 (2) 3  (3), EAK (1) 2   54. 74 (16 c ) 49. 82-59. 67 0. 0078 0. 0012-0. 0127 HL (1) 4 (2) 6 (3) 2 (4), EL (1) 3 (2) 8 (3), IR (1) 3 (2) 2 (3) 3 (4) 3 (5), DHG, WG (1) 9 (2), YYG, YYA (1) 2 , YYL (1) 2 , PWL, IKL (1) 5 , KYL (1) 3    2 ) 5 (3) TDY, AY (1) 10 , IR (1) 3 (2) 4 , AH (1) 3 , VY (1) 5  (2) 2 , TY (1) 3 , WG (1) 4 , IY (1) n T -the number of total proteins including all protein fragments available from the BIOPEP-UWM database (access on August/September 2019 and from the 1st to the 10th December 2019. The data were updated as of 10 December 2019), n-the number of analysed proteins including selected fragments, c, f -protein sequence status ( c-complete, f -a protein fragment), x-a mean value, *DH t -the theoretical degree of hydrolysis.
The number of bioactive peptides with a particular amino acid sequence found in a single analysed protein is provided in brackets. The number of proteins in which the particular bioactive peptide(s) was (were) found is provided in the superscript. The histidine residues found in the bioactive sequences are highlighted in bold, ******-globulins results have been marked, *******-expansin-B1 results has been marked. Other (1-4)-based on the number of amino acid residues found in the analysed protein or protein fragment and the A parameters were classified proteins. n T -the number of total proteins including all protein fragments available from the BIOPEP-UWM database (access on August/September 2019 and from the 1st to the 10th December 2019. The data were updated as of 10 December 2019), n-the number of analysed proteins including selected fragments, c, f -protein sequence status ( c-complete, f -a protein fragment), x-a mean value, *DH t -the theoretical degree of hydrolysis.
The PDCAA index calculated for this protein group, which includes the protein digestibility, amounted to 58. 5% and was lower compared to e. g. , leguminous plants (69. 58%)  [38]. Despite such nutritional restrictions, cereal proteins (as any other proteins) may be potential BAP precursors  [5, [9] [10] [11] [12] [13] [14] [27] [28] [29] [30]. Table  9. The bioparameters characterising the in silico hydrolysis of oat proteins ( I Avena sativa) and the molecular characterisation of the obtained antioxidant peptides. n T -the number of total proteins including all protein fragments available from the BIOPEP-UWM database (access on August/September 2019 and from the 1st to the 10th December 2019. The data were updated as of 10 December 2019), n-the number of analysed proteins including selected fragments, c, f -protein sequence status ( c-complete, f -a protein fragment), x-a mean value, *DH t -the theoretical degree of hydrolysis.
The number of bioactive peptides with a particular amino acid sequence found in a single analysed protein is provided in brackets. The number of proteins in which the particular bioactive peptide(s) was (were) found is provided in the superscript. The histidine residues found in the bioactive sequences are highlighted in bold. Other-based on the number of amino acid residues found in the analysed protein or protein fragment and the A parameters were classified proteins. n T -the number of total proteins including all protein fragments available from the BIOPEP-UWM database (access on August/September 2019 and from the 1st to the 10th December 2019. The data were updated as of 10 December 2019), n-the number of analysed proteins including selected fragments, c, f -protein sequence status ( c-complete, f -a protein fragment), x-a mean value, *DH t -the theoretical degree of hydrolysis.
Materials The study used 416 plant protein monomers or/and their fragments, whose amino acid sequences were recorded using a single-letter amino acid code were derived from the base "Proteins" found in the BIOPEP-UWM database resources (http://www. uwm. edu. pl/biochemia/ index. php/pl/biopep) [61]. Based on the biologically active amino acid sequences defined as biologically active peptides and deposited in the base "Bioactive peptides" which are an integral part of the BIOPEP-UWM database resources, bioactive fragments of sequences with potential antioxidant activities were searched for in the analysed proteins. The BIOPEP-UWM database program compared the analysed protein sequence with 629 amino acid bioactive fragments with antioxidant activity deposited in the base "Bioactive peptides" which currently (data as at 10 December 2019) contains 3,820 biopeptides with 43 different activities.
Methods Selected plant proteins were characterised as sources of antioxidant bioactive fragments based on the obtained profiles of potential antioxidant activity of proteins, including the calculation of the frequency of occurrence of a bioactive fragment with a given activity in the protein sequence (the A parameter). A proteolysis simulation (in silico proteolysis, in silico protein hydrolysis) was carried out with the use of selected enzymes, and a bioevaluation of proteolysis products was conducted using unique and innovative bioinformatic tools available in the BIOPEP-UWM database  [20].
Profiles of Potential Antioxidant Activity of Selected Plant Proteins For each analysed protein or protein fragment, a profile of potential antioxidant activity was generated. To this end, after entering the base "Protein" which is part of the BIOPEP-UWM database resources, the "Analysis" tab was selected, followed by the "Profiles of potential biological activity", and then the activity "antioxidative" was selected from the window "Select activity" and after unfolding the list of activities, and the analysed protein (protein sequence) from the base "Protein database" (after unfolding the list of proteins). In this way, the data search was limited exclusively to antioxidant activity. The profile of potential biological activity is defined as the type and location of bioactive fragment in a protein chain, and, if no specific type of activity is selected at the stage of generating a profile of potential biological activity of protein, then all possible profiles of potential various activities of protein will be generated, and since the base "Bioactive peptides" currently contains 3,820 sequences of biologically active peptides (bioactive peptides, biopeptides) with 43 different bioactivities (data as at 10 December 2019), a large volume of various biological data, not necessarily of significance to the established bioinformatic experiment, could be obtained in this way (http: //www.
To calculate the above-mentioned parameter, similarly to the determination of the profiles of potential antioxidant activity, the tools available in the BIOPEP-UWM database were applied. To this end, the base "Proteins" was selected, followed by the tab "Analysis" and "Calculations". The activity "antioxidative" was then selected from the window "Select activity" after unfolding the list of activities, and the analysed protein (protein sentence) was selected from the base "Protein" (after unfolding the list of proteins)  [20, 61].
In Silico Hydrolysis of Selected Plant Proteins with the use of Selected Enzymes (BIOPEP-UWM) A simulation of proteolysis of the analysed proteins was conducted using two plant enzymes and one animal enzyme out of 33 different proteolytic enzymes with various specific effects on the protein molecule available in the BIOPEP-UWM database. The in silico hydrolysis was carried out with ficin (EC 3. 4. 22. 3) or stem bromelain (EC 3. 4. 22. 32) or pepsin (pH > 2) (EC 3. 4. 23. 1), i. e. , enzymes that had been assigned identification numbers (IDs) of 25, 30 and 39, respectively, in the BIOPEP-UWM database  [61]. A total of 1248 proteolysis simulations were conducted using the application "Enzyme(s) action". The application is available after opening the panel "Analysis" which was made available to BIOPEP-UWM database users only after the previous entering one of the bases making up its resources, e.
g. , "Proteins" or "Bioactive peptides". The tab "Protein database" was then opened, and the analysed molecule and enzymes were selected from the list of proteins and enzymes, respectively. Database users could select an enzyme only after unfolding the list of enzymes provided in the window "Select enzymes". Then, by selecting "View the report with the results", "BIOPEP: Report of enzyme action" was obtained  [20, 61].
Characteristics of Antioxidant Peptides Obtained from the Performed Proteolysis Simulation To obtain data on the released antioxidant peptides, the "Search for active fragments" tab was used. After opening the tab, a report was generated. The report contained data on biopeptides (with different activities) obtained from the performed monocatalytic proteolysis simulation and concerning inter alia the following: own identification number (ID) of biopeptide (deposited in the "Bioactive peptides" database), sequence, location in a protein sequence, name, function and activity. The conducted bioinformatic study selected only the peptides with antioxidant activity based on the amino acid sequence, ID, activity and the location of biopeptide in the protein polypeptide chain  [20, 61].
0), were used. In nature, these three enzymes are found in fig trees (ficin), pineapples (bromelain) and digestive tracts (pepsin (pH > 2)). Moreover, they are used in the food industry and are also ingredients of dietary supplements, inter alia those improving protein digestion in the human digestive tract. During the study, to release nutraceuticals from protein structures, resources of the BIOPEP-UWM database (amino acid sequences of cereal proteins-the "Proteins" database, and antioxidant peptides-the "Bioactive peptides" database), as well as selected tools available in it, were used to perform a simulated proteolysis. The data contained in the BIOPEP-UWM database are updated on an ongoing basis, and new bioinformatic tools are introduced to its resources. Moreover, new sequences of biopeptides, including antioxidant peptides, are continuously deposited in the database.
This highlights the innovation of in silico testing in the analysis of biopeptides with various effects on the human body. The study, whose results are presented in this paper, reflects the current state of knowledge about cereal proteins as peptide nutraceutical precursors, obtained from proteins of various cereal species, and the possibilities for obtaining such bioactive compounds under conditions of hydrolysis simulated by selected enzymes and those classified as compounds referred to as nutraceuticals. During the testing, cereal proteins were subjected to "specific scanning" that was carried out in the BIOPEP-UWM database,.
This highlights the innovation of in silico testing in the analysis of biopeptides with various effects on the human body. The study, whose results are presented in this paper, reflects the current state of knowledge about cereal proteins as peptide nutraceutical precursors, obtained from proteins of various cereal species, and the possibilities for obtaining such bioactive compounds under conditions of hydrolysis simulated by selected enzymes and those classified as compounds referred to as nutraceuticals. During the testing, cereal proteins were subjected to "specific scanning" that was carried out in the BIOPEP-UWM database, to find the so-called permutations with repetitions which indicate the number of fragments and the sequence with antioxidant activity (based on amino acid sequences of antioxidant peptides deposited in the "Bioactive peptides" database, which are the BIOPEP-UWM database resources).
Some of them were fragments with antioxidant activity only, e. g. , EL, LWQ, LHQ, PHQ, YQL, QYP, RYY, WYY, SYY and PYPQ, similarly to sequence fragments containing up to 10 amino acid residues QKPFPQQPPF, PQIPEQF, LRTLPM, SVNVPL, LQPGQGQQ and LQPGQGQQG. Sequence fragments composed of two amino acid molecules were multi-active fragments which may exhibit more than one biological activity, e. g. , they can be enzyme inhibitors (ACE, CaMPDE, DPPIV, renin) (the sequences of obtained antioxidant nutraceuticals were compared to sequences of other biopeptides available in the "Bioactive peptides" database). In hordein profiles, biological fragments that are very characteristic of this protein group, namely PHQ, PYPQ, QKPFPQQPPF, PQIPEQF, LRTLPM, SVNVPL, LQPGQGQQ and LQPGQGQQG, were found. The two latter bioactive fragments were also found in wheat and rye glutenins (HMW subunits).
, HYY, YYH, RWR, RW (1)2 , IR (2), RWN, FC IV Omega-secalins***** 18), EL (1)  (2), EYY (2) , RYY, YYI (1)2 , YYL (2), YYS, SYY (1) 2, LWG, PHQ, LK (3), KP (1) 2 , LW, WG (1) 2 , IY, YYQ, PHY, PWS, RHV, LQPGQGQQ (2), LQPGQGQQG (2), PW, HL (1) (2) 2 , AY (5) (6) (8), AH (1) 3 , LHA (1) 2 , PHS (1) 2 , TY (1) 2 , LHT, LLR, LLPF (2), LPM, IRn T -the number of total proteins including all protein fragments available from the BIOPEP-UWM database (access on August/September 2019 and from the 1st to the 10th December 2019. The data were updated as of 10 December 2019), n-the number of analysed proteins including selected fragments, c, f -protein sequence status ( c -complete, f -a protein fragment), x-a mean value, *NAAR-the number of amino acid residues found in the analysed protein or protein fragment, **NAFS-the number of potential sequence fragments with an antioxidant activity, ***A-the A parameter (the frequency of bioactive fragment occurrence in a protein sequence) (defined in the "Materials and Methods" section of the study), ****AAS-amino acid sequence presented in the form of a single-letter amino acid code: A-Alanine, R-Arginine, N-Asparagine, D-Aspartic acid, C-Cysteine, Q-Glutamine, E-Glutamic acid, G-Glycine, H-Histidine, I-Isoleucine, L-Leucine, K-Lysine, M-Methionine, F-Phenylalanine, P-Proline, S-Serine, T-Threonine, W-Tryptophan, Y-Tyrosine, V-Valine.
(a) (source: the database of protein and bioactive peptide sequences-BIOPEP-UWM, http://www. uwm. edu. pl/biochemia/index. php/pl/biopep, accessed: December 2019) DHt = 30. 07% MK-TF-L-IL-VL-L-AIVATTAPTAVR-F-PVPQL-QPQNPS-QQL-PQEQVPL-VQQQQF-L-G-QQQPF-PPQQPY-PQPQF-PS-QL-PY-L-QL-QPF-PQPQL-PY-S-QPQPF-R-PQQPY-PQPQPQY-S-QPQQPIS-QQQQQQQQQQQQQQQQQQQIL-QQIL-QQQL-IPCMDVVL-QQH-NK-AH-G-R-S-QVL-QQS-TY-QL-L-R-EL-CCQH-L-WQIPEQS-QCQAIH-NVVH-AIIL-H-QQQK-QQQQQPS-S-QVS-F-QQPL-QQY-PL-G-QG-S-F-R-PS-QQNPQTQG-S-VQPQQL-PQF-EEIR-NL-AL-QTL-PS-MCNVY-IPPY-CTIAPF-G-IF-G-TN Results of enzyme action: (b) ficin (EC 3. 4. 22. 3).