Abstract: Rice bran protein hydrolysates (RBPH) were prepared from defatted rice bran of two different Thai rice cultivars (Plai-Ngahm-Prachinburi; PNP and Khao Dok Mali 105; KDM105) using an enzymatic method. This research aimed to optimize enzyme-assisted protein extraction. In addition, the functional properties of RBPH and their stabilities to environmental stresses including pH (3 to 8), ionic strength (0 mM to 500 mM) and the thermal treatment (30 °C to 90 °C) were investigated. Results showed that enzymatic process for protein extraction of defatted rice bran was as follows: enzyme concentration 0.075 g/ 5 g of protein, extraction temperature 50 °C and extraction time 4 h. The obtained protein hydrolysate powders had a degree of hydrolysis (%) of 21.05% in PNP and 19.92% in KDM105. The solubility of protein hydrolysates at pH 4-6 was ranged from 27.28-38.57% and 27.60-43.00% in PNP and KDM105, respectively. In general, antioxidant activities indicated by total phenolic content, FRAP, ferrous ion-chelating (FIC), and 2,2’-azino-bis-3-ethylbenzthiazoline-6-sulphonic acid (ABTS) of KDM105 had higher than PNP. In terms of functional properties, the emulsifying activity index (EAI) was was 8.78 m²/g protein in KDM105, whereas PNP was 5.05 m²/g protein. The foaming capacity at 5 minutes (%) was 47.33 and 52.98 in PNP and KDM105, respectively. Glutamine, Alanine, Valine, and Leucine are the major amino acid in protein hydrolysates where the total amino acid of KDM105 gave higher than PNP. Furthermore, we investigated environmental stresses on the stability of 5% oil in water emulsion (5% oil, 10 mM citrate buffer) stabilized by RBPH (3.5%). The droplet diameter of emulsion stabilized by KDM105 was smaller (d < 250 nm) than produced by PNP. For environmental stresses, RBPH stabilized emulsions were stable at pH around 3 and 5-6, at high salt (< 400 mM, pH 7) and at temperatures range between 30-50°C.
Abstract: Glucomannan can be found in the tuber of porang together with starch and proteinaceous components which were regarded as impurities. An enzymatic process for obtaining higher glucomannan content from Porang flour have been conducted. Papain was used for hydrolysing proteinaceous components in Porang flour which was conducted after a simultaneous extraction of glucomannan and enzymatic starch hydrolysis. Three variables affecting the rate were studied, i.e. temperature, the amount of enzyme and the stirring speed. The ninhydrin method was used to determine degree of protein hydrolysis. Results showed that the rising of degree of hydrolysis were fast in the first ten minutes of the reaction and then proceeded slowly afterward. The optimum temperature for hydrolysis was 60 oC. Increasing the amount of enzyme showed a remarkable effect to degree of hydrolysis, but the stirring speed had no significant effect. This indicated that the reaction controlled the rate of hydrolysis.
Abstract: The halophilic proteinase showed a maximal activity
at 50°C and pH 9~10, in 20% NaCl and was highly stabilized by
NaCl. It was able to hydrolyse natural actomyosin (NAM), collagen
and anchovy protein. For NAM hydrolysis, the myosin heavy chain
was completely digested by halophilic proteinase as evidenced by the
lowest band intensity remaining, but partially hydrolysed actin. The
SR5-3 proteinase was also capable hydrolyzing two major
components of collagen, β- and α-compounds, effectively. The
degree of hydrolysis (DH) of the halophilic proteinase and
commercial proteinases (Novozyme, Neutrase, chymotrypsin and
Flavourzyme) on the anchovy protein, were compared, and it was
found that the proteinase showed a greater degree of hydrolysis
towards anchovy protein than that from commercial proteinases. DH
of halophilic proteinase was sharply enhanced according to the
increase in the concentration of enzyme from 0.035 U to 0.105 U.
The results warranting that the acceleration of the production of fish
sauce with higher quality, may be achieved by adding of the
halophilic proteinase from this bacterium.
Abstract: The present work represents an investigation of the
hydrolysis of hull-less pumpkin (Cucurbita Pepo L.) oil cake protein
isolate (PuOC PI) by pepsin. To examine the effectiveness and
suitability of pepsin towards PuOC PI the kinetic parameters for
pepsin on PuOC PI were determined and then, the hydrolysis process
was studied using Response Surface Methodology (RSM). The
hydrolysis was carried out at temperature of 30°C and pH 3.00. Time
and initial enzyme/substrate ratio (E/S) at three levels were selected
as the independent parameters. The degree of hydrolysis, DH, was
mesuared after 20, 30 and 40 minutes, at initial E/S of 0.7, 1 and 1.3
mA/mg proteins. Since the proposed second-order polynomial model
showed good fit with the experimental data (R2 = 0.9822), the
obtained mathematical model could be used for monitoring the
hydrolysis of PuOC PI by pepsin, under studied experimental
conditions, varying the time and initial E/S. To achieve the highest
value of DH (39.13 %), the obtained optimum conditions for time
and initial E/S were 30 min and 1.024 mA/mg proteins.