Abstract: Rice bran is normally used as a raw material for rice
bran oil production or sold as feed with a low price. Conventionally,
the protein in defatted rice bran was extracted using alkaline
extraction and acid precipitation, which involves in chemical usage
and lowering some nutritious component. This study was conducted
in order to extract of rice bran protein concentrate (RBPC) from
defatted rice bran using enzymes and employing polysaccharides in a
precipitating step. The properties of RBPC obtained will be compared
to those of a control sample extracted using a conventional method.
The results showed that extraction of protein from rice bran using
enzymes exhibited the higher protein recovery compared to that
extraction with alkaline. The extraction conditions using alcalase 2%
(v/w) at 50 C, pH 9.5 gave the highest protein (2.44%) and yield
(32.09%) in extracted solution compared to other enzymes. Rice bran
protein concentrate powder prepared by a precipitation step using
alginate (protein in solution: alginate 1:0.016) exhibited the highest
protein (27.55%) and yield (6.84%). Precipitation using alginate was
better than that of acid. RBPC extracted with alkaline (ALK) or
enzyme alcalase (ALC), then precipitated with alginate (AL)
(samples RBP-ALK-AL and RBP-ALC-AL) yielded the precipitation
rate of 75% and 91.30%, respectively. Therefore, protein
precipitation using alginate was then selected. Amino acid profile of
control sample, and sample precipitated with alginate, as compared to
casein and soy protein isolated, showed that control sample showed
the highest content among all sample. Functional property study of
RBP showed that the highest nitrogen solubility occurred in pH 8-10.
There was no statically significant between emulsion capacity and
emulsion stability of control and sample precipitated by alginate.
However, control sample showed a higher of foaming capacity and
foaming stability compared to those of sample precipitated with
alginate. The finding was successful in terms of minimizing
chemicals used in extraction and precipitation steps in preparation of
rice bran protein concentrate. This research involves in a production
of value-added product in which the double amount of protein (28%)
compared to original amount (14%) contained in rice bran could be
beneficial in terms of adding to food products e.g. healthy drink with
high protein and fiber. In addition, the basic knowledge of functional
property of rice bran protein concentrate was obtained, which can be
used to appropriately select the application of this value-added
product from rice bran.
Abstract: After cold pressing of pumpkin oil, the defatted oil cake (PUOC) was utilised as raw material for processing of bio-functional hydrolysates. In this study, the in vitro bioactivity of an alcalase (AH) and a pepsin hydrolysate (PH) prepared from the major pumpkin 12S globulin (cucurbitin) are compared. The hydrolysates were produced at optimum reaction conditions (temperature, pH) for the enzymes, during 60min. The bioactivity testing included antioxidant and angiotensin I converting enzyme inhibitory activity assays. The hydrolysates showed high potential as natural antioxidants and possibly antihypertensive agents in functional food or nutraceuticals. Additionally, preliminary studies have shown that both hydrolysates could exhibit modest α-amylase inhibitory activity, which indicates on their hypoglycemic potential.
Abstract: Two commercial proteases from Bacillus
licheniformis (Alcalase 2.4 L FG and Alcalase 2.5 L, Type DX) were
screened for the production of Z-Ala-Phe-NH2 in batch reaction.
Alcalase 2.4 L FG was the most efficient enzyme for the C-terminal
amidation of Z-Ala-Phe-OMe using ammonium carbamate as
ammonium source. Immobilization of protease has been achieved by
the sol-gel method, using dimethyldimethoxysilane (DMDMOS) and
tetramethoxysilane (TMOS) as precursors (unpublished results). In
batch production, about 95% of Z-Ala-Phe-NH2 was obtained at
30°C after 24 hours of incubation. Reproducibility of different
batches of commercial Alcalase 2.4 L FG preparations was also
investigated by evaluating the amidation activity and the entrapment
yields in the case of immobilization. A packed-bed reactor (0.68 cm
ID, 15.0 cm long) was operated successfully for the continuous
synthesis of peptide amides. The immobilized enzyme retained the
initial activity over 10 cycles of repeated use in continuous reactor at
ambient temperature. At 0.75 mL/min flow rate of the substrate
mixture, the total conversion of Z-Ala-Phe-OMe was achieved after 5
hours of substrate recycling. The product contained about 90%
peptide amide and 10% hydrolysis byproduct.
Abstract: Wheat gluten hydrolyzates (WGHs) and anchovy fine
powder hydrolyzates (AFPHs) were produced at 300 MPa using
combinations of Flavourzyme 500MG (F), Alcalase 2.4L (A),
Marugoto E (M) and Protamex (P), and then were compared to those
produced at ambient pressure concerning the contents of soluble solid
(SS), soluble nitrogen and electrophoretic profiles. The contents of SS
in the WGHs and AFPHs increased up to 87.2% according to the
increase in enzyme number both at high and ambient pressure. Based
on SS content, the optimum enzyme combinations for one-, two-,
three- and four-enzyme hydrolysis were determined as F, FA, FAM
and FAMP, respectively. Similar trends were found for the contents of
total soluble nitrogen (TSN) and TCA-soluble nitrogen (TCASN). The
contents of SS, TSN and TCASN in the hydrolyzates together with
electrophoretic mobility maps indicates that the high-pressure
treatment of this study accelerated protein hydrolysis compared to
ambient-pressure treatment.