 Open Access
 Total Downloads : 0
 Authors : Xufang Liu , Gennaro J. Maffia
 Paper ID : IJERTV7IS100067
 Volume & Issue : Volume 07, Issue 10 (October – 2018)
 Published (First Online): 05012019
 ISSN (Online) : 22780181
 Publisher Name : IJERT
 License: This work is licensed under a Creative Commons Attribution 4.0 International License
Modified Power Law Formula for the Characterization of Dispersions of Collagen Nanofibrils
Modified Power Law Formula for the Characterization of Dispersions of Collagen Nanofibrils
Xufang (Katie) Liu (MS, 18) Department of Chemical Engineering Manhattan College
Riverdale, New York
Abstract The United States patent, USP #6660829, pertains to the production of collagenbased products in the form of dispersions and macroporous structures using untreated raw fibrillar type I bovine corium as the starting material. The resulting dispersions have improved characteristics making them ideal for use in environmental applications as a settling aid, a filtration aid, a fractionation medium, an oil droplet stabilizer, a water purification aid, and a water siphoning aid. The dispersions may be further treated in accordance with the methods described in the patent to form macroporous structures suitable for biotechnological applications including use as a cell culturing substrate and nonbiotechnological applications including use as an organic aerogel. Analysis of the admixtures produced by blending standard formulations of collagen dispersions with metal dust, inerts or metallic particles indicate that the collagen matrix may be used as a sacrificial scaffold. In this analysis, physical properties and microscopy were used to assess the quality of the dispersion. Statistical analyses were used to identify the potential for characterization using dynamic power law parameters, hysteresis, pore size, density, morphology, number and nature of crosslinks, and the possibility of connecting channels and flowthrough. A modified power law formula and calculation technique is suggested for the characterization of the shear stressshear rate description of the rheology of the collagen dispersion. Experimental data and analyses are presented.
Keywords nanofibrils, power law, shear stress, shear rate, kurtosis

INTRODUCTION
Collagen is a biodegradable polymeric fibrous protein found in all animals. In a series of steps, the collagen molecule assembles into a fiber that has the appearance of a rope. The material is insoluble in water, but can retain many times its own mass in water near its charged surface. This and the ability to unravel the fiber thus maximizing the surface area is the key physical property that leads to numerous environmental and biotechnological applications[1],[2],[3],[4],[5]. With regard to environmental applications, when added to sludge or any material with suspended solids, a collagen dispersion causes agglomeration, the formation of large flocs, and settling, all at a very rapid rate. The material has proven to be effective in the rapid agglomeration of fine solids in all types of sludge: industrial, water treatment, wastewater, inert suspensions, and kaolin.
It has been discovered that collagen dispersions may also be used in other environmental applications such as, as an aid to
Gennaro J. Maffia, PhD
Department of Chemical Engineering Manhattan College
Riverdale, New York
filtration, separation of pollutants (including metals and soluble organic molecules) from aqueous streams, selective fractionation of molecules, and oil droplet stabilization. Moreover, because treated collagen can hold hundreds of times its mass in water, its use in water purification (with minimal energy consumption) and in water siphoning has been discovered and quantified. All of these applications are based on the affinity of the activated surface of collagen, carrying positive charges, for the negative end of the polar water molecule.
Further processing of the dispersions yields products suitable for biotechnological applications[6],[7]. When the collagen dispersion is frozen and then freeze dried, the resulting material retains the overall dimensions of the original frozen material. However, over 99% of the volume is empty and the structure of the protein is a spongy organic aerogel with controllable pore size, good mechanical properties and a density of one thousandth of water. This solid material can be crosslinked to anchor or memorize its shape, pore size and morphology.
Covalent bonds, between adjacent collagen molecules, are formed during crosslinking; thus the resulting material will no longer disperse or retain water. When placed in water, the crosslinked collagen sinks because the specific gravity is slightly higher than that of water. During the process of crosslinking, the material that is produced is also sterile. This material has enormous potential in biotechnology especially in the area of cell culture. Some of the cell culture applications include substrates for: a) achieving high cell density in bioreactors leading to increased productivity and reduced reactor sizes; b) hosting unusual and hardtoculture cells that are used for a variety of applications including biosensors; c) organ and tissue technology that have medical implications (examples are organ regrowth, skin replacement, coating of prostheses and implants, etc.); d) coating of cell culture devices such as roller bottles or glass beads; e) collagen membranes for cell culture and biomolecule delivery; and f) controlled release of pharmaceuticals. In nonbiotechnology applications the freeze dried, crosslinked collagen matrix can serve as an organic aerogel. Other possible uses for this material include encapsulation of a wide variety of organisms, enzymes and synthetic material.

MATERIALS AND METHODS POWER LAW PARAMETER

Method to Develop Collagen Nanofibrils

Weighed approximately 1kg of the Raw Bovine Dermis collagen sheets

Placed into ball mill with zirconia beads

Filled mill with deionized water until it covered the collagen and beads

Closed, sealed, and let run for approximately 2 days

Collected milled collagen and placed equally into 4 centrifuge bottles

Ran centrifuge at 5C for 15 minutes to separate the water from the collagen nanofibrils

Top liquid was discarded and centrifuge bottles were filled with clean DI water

Ran centrifuge twice more until top liquid looked clean

Collagen paste was ready to use and stored in the refrigerator


Method of Formulating 1% Collagen Dispersion

Added acetic acid and deionized water by weight to preweighed amount of collagen nanofibrils produced above

Blended for approximately 5 minutes or until dispersion became thicker and homogenous

Stored in refrigerator for later use


Method of Experimental Tests

Previously made 1% and 2% collagen dispersions were taken out of refrigerator and left out for an hour

These samples were analyzed by a Viscometer that collected the viscosity, shear stress, shear rate, and pressure

Each day, four replicated and two treatments (increase and decrease of shear rate) were performed using Viscometer

Viscosity, shear stress, shear rate and pressure data was monitored and recorded

These tests ran for a total of 11 days until the shear stress became steady

Data was collected and analyzed by excel


Summary of the Dispersion Process
Raw collagen from a variety of sources is the starting material in the manufacture and modification of collagen nanofibrils. The raw material has the appearance of white ground protein as shown in Fig. 1.
Fig. 1. A collagen molecule after a series of steps assembled into the fiber tat has the appearance of rope
It has been discovered that the above described existing collagenbased applications are enhanced, and novel applications possible, using raw fibrillar type I bovine corium as the starting material. Corium is the dermis layer of the hide and is rich in collagenbased connective tissue. While corium has been indicated as a preferred source of collagen for at least some applications, the applicant has discovered that use of a heterogeneous solution of corium as the starting material, as opposed to purified collagen derived from corium, produces superior endproducts including new applications and results not heretofore observed.
Previously, corium was pretreated to remove fats, triglycerides, and other soluble compounds. The resulting raw collagen was then conventionally dried and milled in a knife mill. In the present invention, a dilute solution of the corium itself is milled in a ball mill containing zirconia media for one to two weeks. The pretreatment steps are avoided. Once milling is completed, the resulting material is strained, washed, and then subjected to low temperature centrifugation and the supernatant decanted. This process is repeated several times until no fats or other soluble materials appear in the upper phase and the supernatant is clear. The lower phase containing collagen is then blended in a solution containing an organic acid to form a dispersion and allowed to thicken. The resulting dispersion has improved physical properties and results in enhanced performance when used in various environmental applications.
Fig. 2. Starting material fibers at 5 microns
The above dispersion may be further processed to form physically improved collagen macroporous structures or substrates capable of utilization in various biotechnological applications. During the blending stage any material for encapsulation or controlled release is added.
Fig. 3. Collagen nanofibrils before being unraveled in the ball mill
There has thus been outlined, rather broadly, some important features of the invention in order that the detailed description thereof that follows may be better understood, and in order that the present contribution to the art may be better appreciated. There are, of course, additional features of the invention that will be described hereinafter and which will form the subject matter of the claims appended hereto. In this respect, before explaining at least one embodiment of the invention in detail, it is to be understood that the invention is not limited in its application to the details of construction and to the arrangements of the components set forth in the following description or illustrated in the drawings.
Fig. 4. Final Bovine Nanofibrils[8]
This invention is capable of other embodiments as presented and of being practiced and carried out in various ways, biomedical and environmental. Also, it is to be understood that the phraseology and terminology employed herein are for the purpose of description and should not be regarded as limiting. As such, those scientists and engineers working in protein technology will appreciate that the conception, upon which this research is based, may readily be utilized as a basis for the designing of other structures, methods and systems for carrying out the several purposes of the present invention[9],[10],[11],[12].
Fig. 5. Atomic force microscope (AFM) micrograph of collagen nanofibrils. Note the visible dspacing.


DATA: ANALYSIS OF RESULTS

ANOVA TEST F Distribution and tDistribution
TABLE I. DAY 2 DATA FROM 3.57% COLLAGEN PASTE
Day 2 : Data From 3.75% Collagen Paste
Parameter(a)
Parameter(b)
Directions
Trial 1
7.2218
0.1978
Increase
4.8652
0.2750
decrease
Trial 2
5.1141
0.2389
increase
5.0947
0.2360
decrease
Trial 3
5.1732
0.2321
increase
5.0405
0.2357
decrease
Trial 4
5.1732
0.2244
increase
5.0385
0.2318
decrease
average a
5.3401
std. dev. a
0.7666
average b
0.2340
std. dev. b
0.0211
Table 1 shows the average value of parameter(a) and Parameter(b) in different treatments (increase/ decrease the shear rate) for day 2, and also the average value and standard deviation of parameter (a) and parameter (b) for all four trials.
TABLE II. DATA ANALYSIS FROM DAY 2 RESULTS
Day 2: t Distribution
Testing of Means
Observations
Do increase first
H0: b=0.22
t0
0.3666
H1: b 0.22
absolute(t0)
0.3666
t(0.05,3)
3.1824
If t0 >t, reject
Fail to reject, therefore, b=0.22
Do decrease second
H0: b=0.24
t0
0.4548
H1: b 0.24
absolute(t0)
0.4548
t(0.05,3)
3.1824
If t0 >t, reject
Fail to reject, therefore, b=0.24
Table 2 is the tDistribution for day 2, from the t distrubution, one can conclde that the increase and decrease treatments dont matter for the value of parameter(b), where increase means increase the shear rate, and decrease means decrease shear rate to return to original shear rate.The purpose of the treatment is to test the hysteresis.
Day 2: SS Analysis
Trial
Increase
Decrease
1
0.1978
0.2750
2
0.2389
0.2360
3
0.2321
0.2357
4
0.2244
0.2318
Average
0.2233
0.2446
std deviation
0.0180
0.0203
Observations
Total
0.8932
0.9785
1.8717
Average
0.2233
0.2446
0.2340
0.2340
ss treatments
0.000910
Trial 1
0.000650
0.000923
Trial 2
0.000243
0.000074
Trial 3
0.000077
0.000080
Trial 4
0.000001
0.000164
Total
0.000972
0.001241
ss error
0.002213
ss total
0.003123
TABLE III. DAY 2 SS ANALYSIS
ss treatments
0.000425
Trial 1
0.000568
0.000049
Trial 2
0.000153
0.000000
Trial 3
0.000036
0.000010
Trial 4
0.000030
0.000018
Total
0.000786
0.000077
ss error
0.000863
ss Total
0.001288
Table 3 is the data analysis for OneWay ANOVA for the error and total Sum of Square for day 2.
Day 2: ANOVA
Between treatments
ss
DOF
Mean square
F0
ss treatments
0.000910
1
0.000910
2.4654
ss errors
0.002213
6
0.000369
ss Total
0.003123
7
F(0.05,1,6)
5.9874
H0:
Treatments( increase, decrease) don't matter
H1:
treatments matter
If F0>F,
reject H0
fail to reject, therefore, treatments don't matter
TABLE IV. DAY 2 DATA ANALYSIS FOR TREATMENT
Table 7 is the data analysis for OneWay ANOVA for the error and total Sum of Squares for Day 6.
Table 4 is the Test on Means of Normal Distribution Variance Known Analysis for Day 2.
Day 6: Data From 3.75% Collagen Paste
Parameter(a)
Parameter(b)
Directions
Trial 1
7.3082
0.2023
increase
5.7185
0.2477
decrease
Trial 2
5.8183
0.2385
increase
5.6019
0.2411
decrease
Trial 3
5.6763
0.2321
increase
5.4866
0.2375
decrease
Trial 4
5.5823
0.2316
increase
5.4390
0.2365
decrease
average a
5.8289
std. dev. a
0.6101
average b
0.2334
std. dev. b
0.0136
TABLE V. DAY 6 DATA FROM 3.57% COLLAGEN PASTE
Day 6 : ANOVA
Between treatments
ss
DOF
Mean square
F0
ss treatments
0.000425
1
0.000425
2.9522
ss errors
0.000863
6
0.000144
ss Total
0.001288
7
F(0.05,1,6)
5.9874
H0:
Treatments( increase, decrease) don't matter
H1:
treatments matter
If F0>F,
reject H0
fail to reject, therefore, treatments don't matter
TABLE VIII. DAY 6 DATA ANALYSIS FOR TREATMENT
Table 8 is the Test on Means of Normal Distribution Variance Known Analysis for Day 6.
Day 11: Data From 3.75% Collagen Paste
Parameter(a)
Parameter(b)
Directions
Trial 1
6.6619
0.2036
increase
5.1192
0.2569
decrease
Trial 2
5.0820
0.2530
increase
5.1213
0.2466
decrease
Trial 3
5.2425
0.2434
increase
5.2783
0.2391
decrease
Trial 4
5.2904
0.2355
increase
5.2683
0.2376
decrease
average a
5.3830
std. dev. a
0.5233
average b
0.2395
std. dev. b
0.0163
TABLE IX. DAY 11 DATA FROM 3.57% COLLAGEN PASTE
Table 5 shows the average value of parameter(a) and Parameter(b) in different treatments (increase/ decrease shear rate) for day 6, and the average value and standard deviation of parameter (a) and parameter (b) for all four trials.
Day 6: t Distribution
Testing of Means
Observations
Do increase first
H0: b=0.23
t0
0.4787
H1: b 0.23
absolute(t0)
0.4787
t(0.05,3)
3.1824
If t0 >t, reject
Fail to reject, therefore, b=0.23
Do decrease second
H0: b=0.24
t0
0.2763
H1: b 0.24
absolute(t0)
0.2763
t(0.05,3)
3.1824
If t0 >t, reject
Fail to reject, therefore, b=0.24
TABLE VI. DATA ANALYSIS FROM DAY 6 RESULTS
Table 6 is the tDistribution for day 6, from the t distrubution, one can conclde that treatments(increase and decrease shear rate) dont matter for the value of parameter(b).
Day 6: SS Analysis
Trial
Increase
Decrease
1
0.2023
0.2477
2
0.2385
0.2411
3
0.2321
0.2375
4
0.2316
0.2365
Average
0.2261
0.2407
std. dev.
0.0162
0.0051
Observations
Total
0.9045
0.9628
1.8673
Average
0.2261
0.2407
0.2334
0.2334
TABLE VII. DAY 6 SS ANALYSIS
Table 9 Shows the average value of parameter (a) and parameter (b) in Different treatments( increase/ decrease) for day 11, and the average value and standard deviation of parameter (a) and parameter (b) for all four trials
DAY 11: t Distribution
Testing of Means
Observations
Do increase first
H0: b=0.23
t0
0.3619
H1: b 0.23
absolute(t0)
0.3619
t(0.05,3)
3.1824
If t0 >t, reject
Fail to reject, therefore, b=0.23
Do decrease second
H0: b=0.25
t0
1.1216
H1: b 0.25
absolute(t0)
1.1216
t(0.05,3)
3.1824
If t0 >t, reject
Fail to reject, therefore, b=0.25
TABLE X. DATA ANALYSIS FROM DAY 11 RESULTS
Table 10 is the tDistribution for day 11, from the t Distrubution, one can conclde that the increase and decrease treatments dont matter for the value of parameter(b).
TABLE XI. DAY 11 SS ANALYSIS
Day 11: SS Analysis
Trial
Increase
Decrease
1
0.2036
0.2569
2
0.2530
0.2466
3
0.2434
0.2391
4
0.2355
0.2376
Average
0.2339
0.2451
std. dev.
0.0214
0.0088
Observations
Total
0.9355
0.9802
1.9157
Average
0.2339
0.2451
0.2395
0.2395
ss treatments
0.000250
Trial 1
0.000917
0.000140
Trial 2
0.000366
0.000002
Trial 3
0.000091
0.000035
Trial 4
0.000003
0.000056
Total
0.001376
0.000234
ss error
0.001609
ss Total
0.001859
TABLE XIII. AVERAGE DATA OF POWER LAW PARAMETER FOR 1% COLLAGEN DISPERSION IN 11 DAYS
1% collagen from 3.57% paste
Day
average parameter( a)
Average parameter( b)
1
4.97
0.197
2
5.34
0.23
3
5.22
0.22
4
4.92
0.23
5
6.53
0.23
6
5.83
0.23
7
5.45
0.24
8
8.63
0.18
9
5.68
0.25
10
5.5
0.24
11
5.38
0.24
Table 11 is the data analysis for OneWay ANOVA for the error and total Sum of Square for day 11.
Day 11: ANOVA
Between treatments
ss
DOF
Mean square
F0
ss treatments
0.000250
1
0.000250
0.9311
ss errors
0.001609
6
0.000268
ss Total
0.001859
7
F(0.05,1,6)
5.9874
H0:
Treatments( increase, decrease) don't matter
H1:
treatments matter
If F0>F, reject H0
fail to reject, treatment don't matter
TABLE XII. DAY 11 DATA ANALYSIS FOR TREATMENT
Table 13 is the average data of 1% collagen dispersion made from 3.57% collagen paste for parameter(a) and parameter(b) in 11 days.
Analysis for Average parameter(a)
Mean
5.7682
Standard Error
0.3155
Median
5.4500
Mode
N/A
std. dev. (Standard Deviation)
1.0462
Sample Variance
1.0946
Kurtosis
6.3142
Skewness
2.3915
Range
3.7100
Minimum
4.9200
Maximum
8.6300
Sum
63.4500
Count
11.0000
Confidence Level (95.0%)
0.7029
UL (Upper Limit)
6.4711
LL (Lower Limit)
5.0653
TABLE XIV. KURTOSIS AND SKEWNESS DATA OF PARAMETER A
Table 12 is the Test on Means of Normal Distribution Variance Known Analysis for Day 11.
From Fdistribution and tdistribution, all of the data failed to reject. Therefore, all of the parameter(b) value from the experiments are accepted. And all the treatments include increase and decrease rotor speed dont matter.

Raw Data
Kurtosis is a measurement of the probability distribution of a realvalued random variable. It is the fourth moment in statistics. It is a description of the shape of a probability distribution. A normal kurtosis value is +/ 3[13]. Skewness is a measurement of the asymmetry of the probability distribution of a realvalued random variable about its mean. A normal kurtosis value is +/1[14]. Following is the Kutosis and Skewness analysis for 1% and 2% collagen dispersion of the average parameter (a) and parameter (b) value from day 1 to day 11 as seen in Tables 13 and 14.
Table 14 is the analysis for average parameter (a), the kurtosis value of 6.3142 is greater than 3. And skewness 2.3915 is greater than 1. Both data are higher than the normal kurtosis and skewness.
Analysis for Average parameter( b)
Mean
0.2261
Standard Error
0.0062
Median
0.2300
Mode
0.2300
std. dev. (Standard Deviation)
0.0205
Sample Variance
0.0004
Kurtosis
1.6685
Skewness
1.4204
Range
0.0700
Minimum
0.1800
Maximum
0.2500
Sum
2.4870
Count
11.0000
Confidence Level (95.0%)
0.0138
UL (Uppr Limit)
0.2399
LL (Lower Limit)
0.2123
TABLE XV. KURTOSIS AND SKEWNESS DATA OF PARAMETER B
Table 15 is the analysis for average parameter (b), the kurtosis value of 1.6685 is less than 3. And skewness 1.4204 is out of the range between 1 and 1. Kurtosis value is in the range of the normal kurtosis, but skewness value is out of the normal range.

Goal Seek Application for R2
Goal seek is computed to further analyze the data to pick a power that is as close to 0.9999 as possible. In Table 16, these data shows the goal seek application for picked power law equation to reach the maximum R2 value. The shear rate and shear stress data came from the 1st trial decrease, R2 =0.9386 originally of 1% collagen dispersion made from 3.57% collagen at day 2. Following is the Power Law Equation:
Day 6 : Applying goal seek to get R2
Shear rate,1/s
Shear Stress
Shear ratek
0.418
5.9356
0.9395
0.522
6.2640
0.9546
0.836
7.0642
0.9873
1.045
7.4300
1.0032
2.09
8.7362
1.0541
4.18
10.2410
1.1077
10.45
12.0175
1.1827
12.51
12.0096
1.1980
20.94
13.4435
1.2429
41.82
15.0134
1.3059
Goal seek approach
slope
24.7349
intercept
17.3331
R2
0.9986
pick power in power law equation
0.0715
TABLE XVII. APPLYING GOAL SEEK TO GET R2
SS= Shear stress, Pa SR= Shear rate, 1/s
SS= a + b SRc (1)
a,b,c=modified power law parameter for nonNewtonian fluids[15].
Day 2: Applying goal seek to get R2
Shear rate,1/s
Shear Stress, Pa
Shear ratek
0.418
4.1089
0.4648
0.522
4.2125
0.5649
0.836
4.7401
0.8544
1.045
4.9533
1.0394
2.09
5.7893
1.9108
4.18
6.8134
3.5129
10.45
7.6076
7.8564
12.51
9.2199
9.2016
20.94
10.7003
14.4672
41.82
17.4808
26.5627
Goal seek approach
slope
0.4854
intercept
4.3378
R2
0.9855
pick power in power law equation
0.8784
TABLE XVI. APPLYING GOAL SEEK TO GET R2
In Table 17, these data shows the goal seek application for picked power in power law equation to reach the maximum R2. shear rate and shear stress data came from 1st trial increase, R2 =0.9932 originally of 1% collagen dispersion made from 3.57% collagen at day 6.
TABLE XVIII. APPLYING GOAL SEEK TO GET R2
Day 11 : Applying goal seek to get R2
Shear rate,1/s
Shear Stress
Shear ratek
0.418
5.4758
0.9245
0.522
5.7420
0.9432
0.836
6.4288
0.9840
1.045
6.7403
1.0040
2.09
7.9002
1.0686
4.18
9.1124
1.1373
10.45
11.0770
1.2351
12.51
11.0088
1.2552
20.94
12.4384
1.3148
41.82
13.7588
1.3992
Goal seek approach
slope
17.6879
intercept
10.9590
R2
0.9984
pick power in power law equation
0.0900
Table 16, these data shows the goal seek application for picked power in power law equation to reach the maximum R2. shear rate and shear stress data came from 1st trial increase, R2 =0.9932 originally of 1% collagen dispersion made from 3.57% collagen at day 2.
In Table 18, these data shows the goal seek application for picked power in power law equation to reach the maximum R2. shear rate and shear stress data came from 1st trial increase, R2 =0.9962 originally of 1% collagen dispersion made from 3.57% collagen at day 11.


APPENDIX 1: POWER LAW FORMULA
Appendix 2: Sample Power Law AnalysisFigure 6
Fig. 6. Log data of both the shear stress as a function of shear rate.
Appendix 3: Sample Power Law Parameters Analysis
Day 6( 1% collagen)
Parameter(a)
Parameter(b)
Directions
Trial 1
7.3082
0.2023
increase
5.7185
0.2477
decrease
Trial 2
5.8183
0.2385
increase
5.6019
0.2411
decrease
Trial 3
5.6763
0.2321
increase
5.4866
0.2375
decrease
Trial 4
5.5823
0.2316
increase
5.4390
0.2365
decrease
average a
5.8289
std. dev. a
0.6101
average b
0.2334
std. dev. b
0.0136
At Day 6, 1% of collagen dispersion was taken out from the refrigerate and then left for an hour. Then the 1% dispersion was analyzed by viscometer. Followed by monitoring and recording Viscosity, shear stress, Shear rate and pressure data in both increasing and decreasing shear rate directions. And then excel was used to analyze the data collected.

CONCLUSION
From all the data collected, power law Intercept is not zero for log equation. After series of data analysis, ln (shear stress) vs. ln (shear rate) equation are linear with nonzero intercept. Therefore, the power law formula was then Rewrite by Taking power law until it is Close to before by using Goal seek to get R2 as close to 0.9999. In conclusion, we discovered that from day1 to day 11, it follows the Power law. As the time increased, parameter (a) kept increasing. Parameter (b) kept constant. the shear stress increased as the time increased until day 11, shear stress kept constant.

ACKNOWLEDGMENT
The authors wish to thank Eugene Bender of Collagen Matrix, Inc. for their donation of Raw Bovine Dermis sheets. The authors also wish to thank Amanda Peterman from Manhattan College for editing the paper format.

REFERENCES

USP 8329091 Porous Metallic Structures

USP 6660829 Collagen Processing and Applications

USP 4863856 Weighted Collagen Microspheres

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Nicole Aylmer, Amanda Belluccio, Gennaro J. Maffia, Effect of Collagen Nanofibrils on Turbid Water, IJERT, Vol. 7, Issue 1, January, 2018

Amanda Peterman, Jane Alawi, Gennaro J. Maffia; Effect of Pore Size on the Density of Matrices Made from Collagen Nanofibrils, IJERT,
Volume 6, Issue 8, August ,2017

Control of Pore Size and Morphology in Artificial Tissue Made from Waste Corium, Gennaro Maffia, Manhattan College, Olivia Mason,
Manhattan College, USA ICSW, March 21, 2017

Use of Collagen Nanofibrils to Clarify Turbid Water, Gennaro Maffia, Manhattan College, Amanda Belluccio, Manhattan College, Nicole Aylmer, Manhattan College, USA, ICSW, March 21, 2017

Control of Pore Size and Morphology in Artificial Tissue Made from Waste Corium, Gennaro Maffia, Manhattan College, Olivia Mason,
Manhattan College, USA ICSW, March 21, 2017

Novel Separation Technique to Break the Ethanol Water Azeotrope. Journal of Solid Waste Technology & Management. Nov 2015, Vol. 41 Issue 4, p945948. 4p. Shivakumar, Snehanjani; Foglio, AnnMarie;
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Mathematical Model Characterizing the Release Rates of Vitamin B12 Loaded Collagen Matrices Shivakumar, 4(5): Snehanjani Shivakumar, Gennaro Maffia [May, 2015] ISSN: 22779655 (I2OR), (ISRA),
International Journal of Engineering Sciences & Research Technology

Novel Separation Technique to Break the Ethanol Water Azeotrope. Journal of Solid Waste Technology & Management. Nov2015, Vol. 41 Issue 4, p945948. 4p. Shivakumar, Snehanjani; Foglio, AnnMarie;
Maffia, Gennaro

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