Page 61 - FoodFocusThailand No.213 DECEMBER 2023

STRATEGIC R&D

Enzymes Increase the Efficiency rat plasma, and GPH could be transported across the intestinal cell monolayer .
2
Extraction of Collagen Peptides While chemical hydrolysis can be used to produce collagen peptides, the
from By-products enzymatic treatment provides superior benefits as it is easy to implement and less
Collagen can be extracted from different waste generation. In addition, enzymatic treatment at optimum conditions resulted
sources. Common sources are porcine, in collagen peptides with a neutral taste and achieved a specific degree of hydrolysis
bovine, poultry, and fish by-products. with targeted molecular weight distribution. Moreover, the low salt concentration
Collagen extraction can be carried out in the final product can be obtained when using enzymatic treatment.
from different tissues such as bone, The benefit of collagen peptides is increasingly widely recognized. It makes it
tendon, lung tissue, scale, skin, or event a high-value additive, resulting in the rise of the utilization of collagen peptides as
connective tissue from mentioned dietary supplements in food and beverages and as bioactive ingredients in
animals. While collagen has a certain cosmetics, nutraceuticals, and pharmaceuticals.
biological functional value, apprehending
its efficacy and value is difficult because
of its considerable molecule weight and More Information Service Info C010
strong bonding, which humans cannot
quickly digest, absorb, and utilize. To
increase the bioavailability of collagen,
enzymatic treatment has been
implemented for collagen peptide
production.
Enzymatic hydrolysis using protease
has been widely used to produce
collagen peptides. The protease cuts the
large collagen molecule into small
fragments (peptides). This treatment can
break the bonds in the polypeptide chain
to obtain a large number of peptides.
The molecular weight of collagen
peptides obtained from hydrolysis is very
low (3-6 kDa) compared to that of its
precursor native collagen (285-300 kDa).
Furthermore, there is lots of attempt to
use a combination of proteases on Nano-
collagen peptide (<0.7 kDa) production
and also collagenase on di- or tripeptide
(<0.3 kDa) production. This advanced
technique in enzymology can bring
collagen into the smallest and most
stable unit with only two or three amino
acids in peptide linked together.
Enzymatic hydrolysis affects not only
the size of the peptides but also biological
properties. Depending on the specificity
of the protease that is used, the nature
of the substrate, hydrolysis conditions,
and the degree of hydrolysis, a wide
variety of peptide sizes and functionality
of peptides can be generated. Collagen
peptide has a noticeable improvement
in digestion, absorption, nutrition, and
functional effect and has better solubility
than native collagen. Collagen-derived
small peptides, such as Gly-Pro-Hyp
(GPH) and Pro-Hyp (PH), produced by
collagenase were reported to absorb
well and reach higher plasma levels after
the oral administration of these peptides
in rats compared to higher molecular
weight collagen peptides. GPH and PH
were stable in gastrointestinal fluid and

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