The C1 expression system has the potential to change the way in which both animal health and human biotech and pharmaceutical companies bring their biologic vaccines and drugs to market faster, in greater volumes, at lower cost, and with newer beneficial properties, and most importantly save lives.

1. Jan 4, 2017
(OTCQX: DYAI)
Producing Biologics with C1

2. Safe Harbor Regarding Forward-Looking Statements
2
Certain statements contained in this presentation are forward-looking
statements within the meaning of the federal securities laws. These
forward-looking statements involve risks, uncertainties and other factors
that could cause Dyadic’s actual results, performance or achievements to
be materially different from any future results, performance or
achievements expressed or implied by such forward-looking statements.
Any forward-looking statements speak only as of the date of this
presentation and, except as required by law, Dyadic expressly disclaims
any intent or obligation to update or revise any forward-looking statements
to reflect actual results, any changes in expectations or any change in
events. Factors that could cause results to differ materially are discussed
in Dyadic’s publicly available filings, including information set forth under
the caption “Risk Factors” in our September 30, 2016 Quarterly Report
filed with the OTC Markets on November 10, 2016 and our December 31,
2015 Annual Report filed with OTC Markets on March 29, 2016. New risks
and uncertainties arise from time to time, and it is impossible for us to
predict these events or how they may affect us.

3. C1 – the most productive fungal expression system for biologics
3
A safe and reliable protein production platform,
C1-derived vaccine showed no adverse clinical effects in mice5
Safety &
Reliability
Produces batches of proteins that are significantly purer than traditional
production methods 12 Purity
Cuts preparation and production time in half compared to CHO3
Time
Saving
Achieves much higher yields than traditional production systems in
CHO, E. coli, S. cerevisiae, P. pastoris1 Yield
Grows under broader temperature & pH ranges and is easily
scalable compared to CHO4 Robustness
C1 can minimize CapEx investments, production costs of biologics and overcome
the limitations of traditional production systems
1 including CHO, E. coli, S. cerevisiae, P. pastoris

4. Dyadic Overview
 Revolutionary protein expression technology “C1”: based on Myceliopthora thermophila fungus
 Technology covered by over 20 patent families
 Listed on the stock exchange (OTCQX: DYAI), liquidity of > 60m USD (1)
 Experienced management & board
– 20+ Years of Experience with Fungal Production Systems
– 20+ Years in Pharmaceuticals
20+ Years of Commercial Enzyme
Production
 Platform optimized 2009 – 2015
 Hyper productive strain developed with
unparalleled purity: >100 g/l with ~80%
purity
 Production approved as safe by FDA
 Produced in up to 500,000l tanks
Biopharmaceuticals
 Strategic focus since 2016
 Powerful molecular toolbox enables
production of complex proteins
 Application proven successful:
mAbsVaccines
Non-
Glycosylated
Proteins
Dyadic has demonstrated the power of C1 for the production of biologics and is now
looking to establish partnerships with biopharmaceutical companies
(1) As of September 30, 2016, including ~ $7.4 million of restricted cash held in escrow until July 2017 from the DuPont
Transaction.
4

5. 0
5
10
15
20
25
30
35
40
Per.C6 CHO C1 Complex
Biologics Yield
3
10
30
9
15
< 60
0
10
20
30
40
50
60
S. cerevisiae P. pastoris C1
Industrial/Simple
Protein Yield
C1 produces more protein
Simple/Non-Glycosylated Proteins Complex Proteins, e.g. mAbs
Yielding/l
>3 times higher
yield 2 to 10 times
higher yield
Sources: 1 Boehringer Ingelheim, BioXcellence production: www.bioxcellence.com. & Shane Cox Gad (2007) Handbook of Pharmaceutical
Biotechnology. Wiley Interscience, New Jersey. 2 Non-GMP conditions, non purified. 3 Susan Gotensparre (2007) Crucell.
InPharmaTechnologist.com. 4 Non-GMP conditions, not purified, expected based on small scale production experience
 High cell density attainable
 More protein produced
 Protein is secreted
 Both for small and large scale production
 Codon optimization established
 For heterologous proteins of both bacterial and mammalian origin
High productivity of C1 proven
5
1
2
3
4
2 3
20
Key
Highest yield
claimed
Realistic
estimate
1
40
15
20

6. C1 delivers higher purity of protein and is highly robustPurity
C1 White
Strain 2.0 2
C1 1st
Generation2E. Coli 1
C1 delivers
 Higher levels of the target protein
 Significantly higher purity
C1 maintains high productivity
 Under a wider temperature than CHO
 Under a wider pH range than CHO
 At scales ranging from laboratory shake flasks to
20,000l tanks and above
40ºC
37ºC
-
32ºC
25ºC
pH range
71 14
5 9
C1 CHO
Robustness
CHO 2
1 After 2 Purification Steps, 2 No purification steps 3 Optimal range 32 - 37ºC. Source: Sellick, C. et al (2009) Optimizing CHO Cell
Culture Conditions. Genetic Engineering and Biotechnology News Tutorial.
6CHO3
45ºC
-
25ºC
C1

7.  Reproduction rate of cell 2x higher than for CHO
 Protein production rate at least 1.5 fold
 Higher purity of protein achieved may decrease recovery time
C1 enables shorter production cycles in comparison to CHO
1
1
2
2
3
3
0 1 2 3 4 5
CHO
C1
Duration of Steps in Production
*Note: Protein Recovery
may be faster due to
higher purity of C1
production
Week 1 Week 2 Week 3 Week 4
Batch Cycle time is reduced by >50% in
comparison to CHO, freeing up capacity
Production time reduced
by >14 days
1: Biomass Expansion 2: Protein Production 3: Protein Recovery*
7

8. C1’s unique morphology enables non-viscous fungal production
The low viscosity allows C1 to be used in
established microbial production facilities,
requiring
no additional CapEx investment
8
Viscosity(cP)
Protein Yield
500
400
300
200
100
100
80
60
40
20
Protein(g/l)
Viscosity
Standard Fungal Line C1
Low Viscosity, High Yield
Filamentous fungi face challenges
for their use in production due to
high viscosity
C1 exhibits a unique morphology
resulting in low viscosity
*

9. C1 enables 50 - 85% reduction in manufacturing costs
Expected OpEx savings of 60 - 85% vis-à-vis CHO
Possibility of decreasing CapEx investments by 80 %
4
12
0
5
10
15
Column1
 Decrease direct labor cost by >80%
 Decrease indirect labor cost by >80%
 Decrease consumables cost by >90%
 Decrease capital charge by 60-70%2
 Same extraction and purification costs 3
g/1000US$
1 Depreciation cost of facility over 10 years included, savings increase with increased production need 2 Depending on production requirements, investment into 10,000 l
tanks can be reduced to 1 – 2,000l tanks, 3 Cost savings likely higher due to higher purity of proteins from C1
4 Based on production needs of ~800kg,
Output
~tripled
Cost Efficiency of C1 vs. CHO
(Exemplary ~20kg mAb Production1)
 Lower CapEx Investment
 Smaller production facilities faster to build
Additional benefits
CapEx Investment of C1 vs. CHO
(Exemplary large scale mAb Production4)
0
100
200
300
400
500
CHO C1
MillionUS$
CHO C1
CapEx reduced by
80%
9
OpEx upstream savings
Four 10,000l
tanks
Three 2,000l
tanks

10. C1 is easy to engineer to achieved desired protein profile1
Dyadic has experience with each of the molecular tools necessary to optimize the strain for high
productivity and functionality for the targeted protein class
Genetic manipulation
Computational
biology
Man9 G0 G2F
Changing the
cellular
regulatory circuit
✔
Libraries of
efficient strong
promoters
✔
Libraries of TF
and signal
peptides and / or
carrier proteins
✔
Libraries of
protease
deletion strains
✔
Glycoengineering to
form mammalian-like
glycan structures in
progress
✔
1. First proof of concept studies have been successful for these tools in Trichoderma. 10
Gene 1Pr Carrier

11. Trichoderma Reesi Fungal System
Production yields with different target proteins by Trichoderma reesei
Trichoderma Source: PEGS Boston, 2016: (Next - Generation Biotherapeutic Production System: The Filamentous Fungus Trichoderma Reesi)
 Antibodies produced in Δ7 strain, IFN in Δ9 strain, and IGF1 in Δ13 deletion strain as fusion with CBHI carrier
 However, this is far from the maximal theoretical output of 29 g/L for MAb01 based upon carrier
expression level
11

12. Trichoderma Reesi Fungal System (Cont.)
IgG production by Trichoderma reesei (TR)
Trichoderma Source: PEGS Boston, 2016: (Next - Generation Biotherapeutic Production System: The Filamentous Fungus Trichoderma Reesi)
 Protease deletion strains together with fermentation optimization work improved the IgG
 Antibody production levels up to 7.1 g/l
 The secretion carrier CBHI is produced in the fermentations at levels up to 38 g/l. This theoretically equates
to potential antibody expression levels of approximately 29 g/l
12
6
18
28
34
41
49
52
60
56 56
58
5.9
13.1
22.4
36.3
31.4
38.5
33.3
32
35.4
5.8 6.2 6.7 6.9 7.1 6.7
4.7
17
27.6
23.9
29.2
25.3 24.3
26.9
0
10
20
30
40
50
60
70
0 1 2 3 4 5 6 7 8 9 10 11 12 13
Protein(g/L)
Day in culture
TR - Total Protein
CBHI
TR - MAB01
TR - Theoretical MAB01
6
18
28
34
41
49
52
60
56 56
58
5.9
13.1
22.4
36.3
31.4
38.5
33.3
32
35.4
17
27.6
23.9
29.2
25.3 24.3
26.9
5.8 6.2 6.7 6.9 7.1 6.7
4.7
0
10
20
30
40
50
60
70
0 1 2 3 4 5 6 7 8 9 10 11 12 13
Protein(g/L)
Day in culture
TR - Total Protein
CBHI
TR - Theoretical MAB01
TR - MAB01

13. Higher potential production of IgG with C1
(1) Expression of heterologous fungal protein
Trichoderma Source: PEGS Boston, 2016: (Next - Generation Biotherapeutic Production System: The Filamentous Fungus Trichoderma Reesi)
 Total C1 cell protein expression reached a level of >100 g/l.
 The production level is almost 2 fold higher than the total protein production of T. reesei.
 The production phase starts earlier already after 1 day and can proceed to 5 – 7 days.
 Therefore, the potential of reaching much higher antibody productivity than 6.9 g/l is promising with C1 after
5-7 days of optimized fermentation process.
13
1.7
10.1
41
66
82
95
105
6
18
28
34
41 49
52
60
56 56 58
10
22
34
55.2
47.8
58.4
50.6
48.6
53.8
5.9
13.1
22.4
36.3
31.4
38.5
33.3 32
35.4
5
11
17
27.6
23.9
29.2
25.3 24.3
26.9
11.6
12.4 13.4 13.8 14.2 13.4
9.4
5.8 6.2 6.7 6.9 7.1 6.7
4.7
0
20
40
60
80
100
120
0 1 2 3 4 5 6 7 8 9 10 11 12 13
Protein(g/L)
Day in culture
C1 - Total Protein
TR - Total Protein
C1 - Theoretical
CBHI
TR - Theoretical MAB01
C1 - Expected
TR - MAB01

14. C1 for vaccine production – lower costs & higher efficacy
 Easy scale up, lower production costs due to higher yield (in comparison to CHO/yeast/ E. coli)
 C1 produced antigen generated an equal, or better, immune response in mice than the industry
standard antigen
 International collaboration ongoing in vaccine development
Key Advantages
14
The C1 technology platform:
A leap in technology that shows the potential
to change the way in which both Human and
Animal Health Biopharmaceutical companies
bring their biologic vaccines and drugs to
market faster, in greater volumes, at lower
cost, and with newer beneficial properties.

15. C1 has the potential to address several of the challenges facing the Diabetes market
1. High demand
 Insulin production needs are expected to exceed 16 tons by 2025. Current Insulin
production methods will not suffice to meet demand.1
1. Lower margins
 Published insulin CoGS lie at about 61 USD per gram, leaving a profit margin of about
35%.2
1. Payer pressures
 US payer pressures are driving down profit margins even further.
C1 for production of non-glycosylated proteins*
Based on production yields alone,
cost savings of > 50% may be achieved.
C1 exhibits higher production flexibility than
S. cerevisiae or E. coli
15
* With no to minimal post-translational modifications needed to functionality
Sources: 1. Baeshen et al. Cell factories for insulin production. Microbiol Cell Factories 2014. 13:141.
2 Harrison et all, Bioseparations Science and Engineering. Oxford University Press 2nd Edition, 2015. Note: Large scale manufacturers operating at highest efficiency
levels achieve lower costs (1/2 to 1/3 of cited cost).
Example Case: C1 for Insulin Production

16. C1 for mAb production shows promising initial results
 Production of heavy & light chain successful
 MS/MS data reveals correct structure
 Binding to target confirmed via ELISA
Heavy chain
Light chain
 Production of Fab successful
 The structure was confirmed by MS analysis
 Specificity of binding confirmed via ELISA
Lucentis
72h 96h Control
Case Study 1: Humira Case Study 2: Lucentis
 C1 has produced biologically-active monoclonal antibodies
 Protease deficient strains with no mAb degradation successfully generated
 Codon use for fungal expression optimized
 Glycosylation controllable and glycoengineering is expected to begin in 2017
Successful Initial Engineering of C1 for mAb Production
16

17. C1 production of mAbs could dramatically alter economics
17
42
18
124
60
110
360
0
50
100
150
200
250
300
350
400
C1 - 2000l tank C1 - 10,000l tank Standard Manufacturing
Annual OpEx
Initial CapEx Investment
Comparative Manufacturing Costs
(Example: Humira for US market)
* OpEx cost include depreciation cost that assume depreciation of facility over 10 years, costs from active ingredient production only, no further processing
1 requires two 2,000l tanks to satisfy annual production needs, 2 requires one 10,000l tank that will retain 10 months of production capacity, 3 requires three
10,000l tanks
CHO - 10,000l tank 3
CostinMillionUSD
21
Potential savings over current
production methods warrant
further engineering to realize
mAb production in C1
Biobetter mAbs
Robust strain engineering and Glycoengineering
Novel mAbs
H1 2017 H2 2017 H1 2018 H2 2018
New Product Platform Development
New Product Development
mAb Biobetter Development
H1 2019
Estimated timeline for Further C1 Strain Engineering
*
C1 - 2,000l tank 1
C1 - 10,000l tank 2

18. C1 production is safe
18
Non-Pathogenic
Not Genotoxic
 Strain is non-toxic and non-
infectious
 No toxic byproducts are
generated during production
 In vivo trials demonstrated:
 No adverse effects
 No foreign DNA
 Safety confirmed
 C1-cellulase accepted by FDA on
September 29, 2009
 GRAS notification letters are
broadly recognized in the food
and consumer products
industries as the safety standard
For Enzyme Production: Generally
Recognized as Safe (GRAS) Status
No Adverse Effects
 Mice experiments showed:
 No adverse clinical
effects induced by C1
produced vaccines

19. Summary - Key Advantages of C1
19
Dyadic is looking for partners in the biopharmaceutical space to
exploit the potential of C1.
For further inquiry, please contact
mjones@dyadic.com
Further benefits:
 Unique properties that can be
engineered for the desired product
profile
 A toolbox for strain engineering to
optimize production of different
biologics (vaccines, simple proteins,
antibodies)
Short
production
cycles
2
High purity of
produced
protein Robust and
reliable
manufacturing
3
4
First product
shown to be
safe in animal
studies
5
Unprecedented
protein yields
1